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1. THE CONCISE GUIDE TO PHARMACOLOGY 2017/18: Overview

Author: Alexander, Stephen PH, Kelly, Eamonn, Marrion, Neil V, Peters, John A, Faccenda, Elena, Harding, Simon D, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Buneman, O Peter, Cidlowski, John A, Christopoulos, Arthur, Davenport, Anthony P, Fabbro, Doriano, Spedding, Michael, Striessnig, Jörg, Davies, Jamie A, Abbracchio, M‐P, Aldrich, R, Al‐Hosaini, K, Arumugam, TV, Attali, B, Bäck, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Bettler, B, Biel, M, Birdsall, NJ, Blaho, V, Boison, D, Bräuner‐osborne, H, Bröer, S, Bryant, C, Burnstock, G, Calo, G, Catterall, WA, Ceruti, S, Chan, SL, Chandy, KG, Chazot, P, Chiang, N, Chun, JJ, Chung, J‐J, Clapham, DE, Clapp, L, Connor, MA, Cox, HM, Davies, P, Dawson, PA, Decaen, P, Dent, G, Doherty, P, Douglas, SD, Dubocovich, ML, Fong, TM, Fowler, CJ, Frantz, A, Fuller, P, Fumagalli, M, Futerman, AH, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Goudet, C, Gregory, K, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hamann, J, Hammond, JR, Hancox, JC, Hanson, J, Hanukoglu, I, Hay, DL, Hobbs, AJ, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Irving, AJ, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, MF, Jensen, R, Jockers, R, Kaczmarek, LK, Kanai, Y, Karnik, S, Kellenberger, S, Kemp, S, Kennedy, C, Kerr, ID, Kihara, Y, Kukkonen, J, Larhammar, D, Leach, K, Lecca, D, Leeman, S, Leprince, J, Lolait, SJ, Macewan, D, Maguire, JJ, Marshall, F, Mazella, J, Mcardle, CA, Michel, MC, Miller, LJ, Mitolo, V, Mizuno, H, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J‐L, Nerbonne, J, Nichols, CG, Norel, X, Offermanns, S, Palmer, LG, Panaro, MA, Papapetropoulos, A, Perez‐reyes, E, Pertwee, RG, Pintor, S, Pisegna, JR, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ramachandran, R, Ren, D, Rondard, P, Ruzza, C, Sackin, H, Sanger, G, Sanguinetti, MC, Schild, L, Schiöth, H, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Singh, KD, Slesinger, PA, Snutch, TP, Sobey, CG, Stewart, G, Stoddart, LA, Summers, RJ, Szabo, C, Thwaites, D, Toll, L, Trimmer, JS, Tucker, S, Vaudry, H, Verri, T, Vilargada, J‐P, Waldman, SA, Ward, DT, Waxman, SG, Wei, AD, Willars, GB, Wong, SS, Woodruff, TM, Wulff, H, Ye, RD, Yung, Y, and Zajac, J‐M
Published: 2017
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2. THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: G protein-coupled receptors

Author: Alexander, SPH, Christopoulos, A, Davenport, AP, Kelly, E, Mathie, A, Peters, JA, Veale, EL, Armstrong, JF, Faccenda, E, Harding, SD, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Arumugam, TV, Bennett, A, Sjogren, B, Sobey, C, Wong, SS, Abbracchio, MP, Alexander, W, Al-hosaini, K, Back, M, Beaulieu, J-M, Bernstein, KE, Bettler, B, Birdsall, NJM, Blaho, V, Bousquet, C, Brauner-Osborne, H, Burnstock, G, Calo, G, Castano, JP, Catt, KJ, Ceruti, S, Chazot, P, Chiang, N, Chun, J, Cianciulli, A, Clapp, LH, Couture, R, Csaba, Z, Dent, G, Singh, KD, Douglas, SD, Dournaud, P, Eguchi, S, Escher, E, Filardo, E, Fong, TM, Fumagalli, M, Gainetdinov, RR, de Gasparo, M, Gershengorn, M, Gobeil, F, Goodfriend, TL, Goudet, C, Gregory, KJ, Gundlach, AL, Hamann, J, Hanson, J, Hauger, RL, Hay, D, Heinemann, A, Hollenberg, MD, Holliday, ND, Horiuchi, M, Hoyer, D, Hunyady, L, Husain, A, Ijzerman, AP, Inagami, T, Jacobson, KA, Jensen, RT, Jockers, R, Jonnalagadda, D, Karnik, S, Kaupmann, K, Kemp, J, Kennedy, C, Kihara, Y, Kozielewicz, P, Kreienkamp, H-J, Kukkonen, JP, Langenhan, T, Leach, K, Lecca, D, Lee, JD, Leeman, SE, Leprince, J, Lolait, SJ, Lupp, A, Macrae, R, Maguire, J, Mazella, J, McArdle, CA, Melmed, S, Michel, MC, Miller, L, Mitolo, V, Mouillac, B, Murphy, PM, Nahon, J-L, Norel, X, Nyimanu, D, O'Carroll, A-M, Offermanns, S, Panaro, MA, Pertwee, RG, Pin, J-P, Prossnitz, E, Ramachandran, R, Reinscheid, RK, Rondard, P, Rovati, GE, Ruzza, C, Sanger, G, Schoeneberg, T, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Stoddart, LA, Sugimoto, Y, Summers, R, Tan, V, Thomas, W, Timmermans, PBMWM, Tirupula, K, Tulipano, G, Unal, H, Unger, T, Vanderheyden, P, Vaudry, D, Vaudry, H, Vilardaga, J-P, Walker, CS, Ward, DT, Wester, H-J, Willars, GB, Williams, TL, Woodruff, TM, Yao, C, Aldrich, RW, Becirovic, E, Biel, M, Catterall, WA, Conner, AC, Davies, P, Delling, M, Di Virgilio, F, Falzoni, S, George, C, Goldstein, SAN, Grissmer, S, Ha, K, Hammelmann, V, Hanukoglu, I, Jarvis, M, Jensen, AA, Kaczmarek, LK, Kellenberger, S, King, B, Lynch, JW, Perez-Reyes, E, Plant, LD, Rash, LD, Ren, D, Sivilotti, LG, Smart, TG, Snutch, TP, Tian, J, Van den Eynde, C, Vriens, J, Wei, AD, Winn, BT, Wulff, H, Xu, H, Yue, L, Zhang, X, Zhu, M, Coons, L, Fuller, P, Korach, KS, Young, M, Bryant, C, Farndale, RW, Hobbs, A, Jarvis, GE, MacEwan, D, Monie, TP, Waldman, S, Beuve, A, Boison, D, Brouckaert, P, Burnett, JC, Burns, K, Dessauer, C, Friebe, A, Garthwaite, J, Gertsch, J, Helsby, N, Izzo, AA, Koesling, D, Kuhn, M, Ostrom, R, Papapetropoulos, A, Potter, LR, Pyne, NJ, Pyne, S, Russwurm, M, Schmidt, HHHW, Seifert, R, Stasch, J-P, Szabo, C, van der Stelt, M, van der Vliet, A, Watts, V, Anderson, CMH, Broer, S, Dawson, P, Hagenbuch, B, Hammond, JR, Hancox, J, Inui, K-I, Kanai, Y, Kemp, S, Thwaites, DT, Verri, T, Alexander, SPH, Christopoulos, A, Davenport, AP, Kelly, E, Mathie, A, Peters, JA, Veale, EL, Armstrong, JF, Faccenda, E, Harding, SD, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Arumugam, TV, Bennett, A, Sjogren, B, Sobey, C, Wong, SS, Abbracchio, MP, Alexander, W, Al-hosaini, K, Back, M, Beaulieu, J-M, Bernstein, KE, Bettler, B, Birdsall, NJM, Blaho, V, Bousquet, C, Brauner-Osborne, H, Burnstock, G, Calo, G, Castano, JP, Catt, KJ, Ceruti, S, Chazot, P, Chiang, N, Chun, J, Cianciulli, A, Clapp, LH, Couture, R, Csaba, Z, Dent, G, Singh, KD, Douglas, SD, Dournaud, P, Eguchi, S, Escher, E, Filardo, E, Fong, TM, Fumagalli, M, Gainetdinov, RR, de Gasparo, M, Gershengorn, M, Gobeil, F, Goodfriend, TL, Goudet, C, Gregory, KJ, Gundlach, AL, Hamann, J, Hanson, J, Hauger, RL, Hay, D, Heinemann, A, Hollenberg, MD, Holliday, ND, Horiuchi, M, Hoyer, D, Hunyady, L, Husain, A, Ijzerman, AP, Inagami, T, Jacobson, KA, Jensen, RT, Jockers, R, Jonnalagadda, D, Karnik, S, Kaupmann, K, Kemp, J, Kennedy, C, Kihara, Y, Kozielewicz, P, Kreienkamp, H-J, Kukkonen, JP, Langenhan, T, Leach, K, Lecca, D, Lee, JD, Leeman, SE, Leprince, J, Lolait, SJ, Lupp, A, Macrae, R, Maguire, J, Mazella, J, McArdle, CA, Melmed, S, Michel, MC, Miller, L, Mitolo, V, Mouillac, B, Murphy, PM, Nahon, J-L, Norel, X, Nyimanu, D, O'Carroll, A-M, Offermanns, S, Panaro, MA, Pertwee, RG, Pin, J-P, Prossnitz, E, Ramachandran, R, Reinscheid, RK, Rondard, P, Rovati, GE, Ruzza, C, Sanger, G, Schoeneberg, T, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Stoddart, LA, Sugimoto, Y, Summers, R, Tan, V, Thomas, W, Timmermans, PBMWM, Tirupula, K, Tulipano, G, Unal, H, Unger, T, Vanderheyden, P, Vaudry, D, Vaudry, H, Vilardaga, J-P, Walker, CS, Ward, DT, Wester, H-J, Willars, GB, Williams, TL, Woodruff, TM, Yao, C, Aldrich, RW, Becirovic, E, Biel, M, Catterall, WA, Conner, AC, Davies, P, Delling, M, Di Virgilio, F, Falzoni, S, George, C, Goldstein, SAN, Grissmer, S, Ha, K, Hammelmann, V, Hanukoglu, I, Jarvis, M, Jensen, AA, Kaczmarek, LK, Kellenberger, S, King, B, Lynch, JW, Perez-Reyes, E, Plant, LD, Rash, LD, Ren, D, Sivilotti, LG, Smart, TG, Snutch, TP, Tian, J, Van den Eynde, C, Vriens, J, Wei, AD, Winn, BT, Wulff, H, Xu, H, Yue, L, Zhang, X, Zhu, M, Coons, L, Fuller, P, Korach, KS, Young, M, Bryant, C, Farndale, RW, Hobbs, A, Jarvis, GE, MacEwan, D, Monie, TP, Waldman, S, Beuve, A, Boison, D, Brouckaert, P, Burnett, JC, Burns, K, Dessauer, C, Friebe, A, Garthwaite, J, Gertsch, J, Helsby, N, Izzo, AA, Koesling, D, Kuhn, M, Ostrom, R, Papapetropoulos, A, Potter, LR, Pyne, NJ, Pyne, S, Russwurm, M, Schmidt, HHHW, Seifert, R, Stasch, J-P, Szabo, C, van der Stelt, M, van der Vliet, A, Watts, V, Anderson, CMH, Broer, S, Dawson, P, Hagenbuch, B, Hammond, JR, Hancox, J, Inui, K-I, Kanai, Y, Kemp, S, Thwaites, DT, and Verri, T
Abstract: The Concise Guide to PHARMACOLOGY 2019/20 is the fourth in this series of biennial publications. The Concise Guide provides concise overviews of the key properties of nearly 1800 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.14748. G protein-coupled receptors are one of the six major pharmacological targets into which the Guide is divided, with the others being: ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2019, and supersedes data presented in the 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the International Union of Basic and Clinical Pharmacology Committee on Receptor Nomenclature and Drug Classification (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.
Published: 2019

3. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Transporters

Author: Alexander, SPH, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13355/full. G protein-coupled receptors are one of the eight major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

4. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Ligand-gated ion channels

Author: Alexander, SPH, Peters, JA, Kelly, E, Marrion, N, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Peters, JA, Kelly, E, Marrion, N, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13349/full. Ligand-gated ion channels are one of the eight major pharmacological targets into which the Guide is divided, with the others being: ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

5. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Nuclear hormone receptors

Author: Alexander, SPH, Cidlowski, JA, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Cidlowski, JA, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13352/full. Nuclear hormone receptors are one of the eight major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

6. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Overview

Author: Alexander, SPH, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Buneman, OP, Catterall, WA, Cidlowski, JA, Davenport, AP, Fabbro, D, Fan, G, McGrath, JC, Spedding, M, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Buneman, OP, Catterall, WA, Cidlowski, JA, Davenport, AP, Fabbro, D, Fan, G, McGrath, JC, Spedding, M, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13347/full. This compilation of the major pharmacological targets is divided into eight areas of focus: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

7. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: G protein-coupled receptors

Author: Alexander, SPH, Davenport, AP, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Davenport, AP, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13348/full. G protein-coupled receptors are one of the eight major pharmacological targets into which the Guide is divided, with the others being: ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

8. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Catalytic receptors

Author: Alexander, SPH, Fabbro, D, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Fabbro, D, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13353/full. G protein-coupled receptors are one of the eight major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

9. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Enzymes

Author: Alexander, SPH, Fabbro, D, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Fabbro, D, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13354/full. G protein-coupled receptors are one of the eight major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

10. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Other ion channels

Author: Alexander, SPH, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13351/full. Other ion channels are one of the eight major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

11. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Voltage-gated ion channels

Author: Alexander, SPH, Catterall, WA, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Catterall, WA, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13350/full. Voltage-gated ion channels are one of the eight major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, ligand-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

12. [Untitled]

Author: Alexander, Stephen PH, Kelly, Eamonn, Marrion, Neil, Peters, John A, Benson, Helen E, Faccenda, Elena, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Buneman, O Peter, Catterall, William A, Cidlowski, John A, Davenport, Anthony P, Fabbro, Doriano, Fan, Grace, McGrath, John C, Spedding, Michael, Davies, Jamie A, Aldrich, R, Attali, B, Bäck, Ml, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Bräuner‐Osborne, H, Bröer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J‐J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hébert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb‐Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, Mcardle, CA, Mcdonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J‐L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez‐Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M‐J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J‐P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J‐M
Subjects: Pharmacology, Summary information, business.industry, The Concise Guide to PHARMACOLOGY 2015/16, Medicine, Catalytic receptors, business, 3. Good health
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13347/full. This compilation of the major pharmacological targets is divided into eight areas of focus: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
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13. Mechanism of an animal toxin-antidote system.

Author: Caro L, Wei AD, Thomas CA, Posch G, Uremis A, Franzi MC, Abell SJ, Laszlo AH, Gundlach JH, Ramirez JM, and Ailion M
Abstract: Toxin-antidote systems are selfish genetic elements composed of a linked toxin and antidote. The peel-1 zeel-1 toxin-antidote system in C. elegans consists of a transmembrane toxin protein PEEL-1 which acts cell autonomously to kill cells. Here we investigate the molecular mechanism of PEEL-1 toxicity. We find that PEEL-1 requires a small membrane protein, PMPL-1, for toxicity. Together, PEEL-1 and PMPL-1 are sufficient for toxicity in a heterologous system, HEK293T cells, and cause cell swelling and increased cell permeability to monovalent cations. Using purified proteins, we show that PEEL-1 and PMPL-1 allow ion flux through lipid bilayers and generate currents which resemble ion channel gating. Our work suggests that PEEL-1 kills cells by co-opting PMPL-1 and creating a cation channel., Competing Interests: Competing interests: Authors declare no competing interests.
Published: 2024
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14. Chronic intermittent hypoxia elicits distinct transcriptomic responses among neurons and oligodendrocytes within the brainstem of mice.

Author: Bhagavan H, Wei AD, Oliveira LM, Aldinger KA, and Ramirez JM
Subjects: Animals, Mice, Male, Brain Stem metabolism, Oligodendroglia metabolism, Transcriptome, Hypoxia metabolism, Hypoxia genetics, Neurons metabolism, Neurons pathology, Mice, Inbred C57BL
Abstract: Chronic intermittent hypoxia (CIH) is a prevalent condition characterized by recurrent episodes of oxygen deprivation, linked to respiratory and neurological disorders. Prolonged CIH is known to have adverse effects, including endothelial dysfunction, chronic inflammation, oxidative stress, and impaired neuronal function. These factors can contribute to serious comorbidities, including metabolic disorders and cardiovascular diseases. To investigate the molecular impact of CIH, we examined male C57BL/6J mice exposed to CIH for 21 days, comparing with normoxic controls. We used single-nucleus RNA sequencing to comprehensively examine the transcriptomic impact of CIH on key cell classes within the brainstem, specifically excitatory neurons, inhibitory neurons, and oligodendrocytes. These cell classes regulate essential physiological functions, including autonomic tone, cardiovascular control, and respiration. Through analysis of 10,995 nuclei isolated from pontine-medullary tissue, we identified seven major cell classes, further subdivided into 24 clusters. Our findings among these cell classes, revealed significant differential gene expression, underscoring their distinct responses to CIH. Notably, neurons exhibited transcriptional dysregulation of genes associated with synaptic transmission, and structural remodeling. In addition, we found dysregulated genes encoding ion channels and inflammatory response. Concurrently, oligodendrocytes exhibited dysregulated genes associated with oxidative phosphorylation and oxidative stress. Utilizing CellChat network analysis, we uncovered CIH-dependent altered patterns of diffusible intercellular signaling. These insights offer a comprehensive transcriptomic cellular atlas of the pons-medulla and provide a fundamental resource for the analysis of molecular adaptations triggered by CIH. NEW & NOTEWORTHY This study on chronic intermittent hypoxia (CIH) from pons-medulla provides initial insights into the molecular effects on excitatory neurons, inhibitory neurons, and oligodendrocytes, highlighting our unbiased approach, in comparison with earlier studies focusing on single target genes. Our findings reveal that CIH affects cell classes distinctly, and the dysregulated genes in distinct cell classes are associated with synaptic transmission, ion channels, inflammation, oxidative stress, and intercellular signaling, advancing our understanding of CIH-induced molecular responses.
Published: 2024
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15. AAV-mediated interneuron-specific gene replacement for Dravet syndrome.

Author: Mich JK, Ryu J, Wei AD, Gore BB, Guo R, Bard AM, Martinez RA, Bishaw Y, Luber E, Oliveira Santos LM, Miranda N, Ramirez JM, Ting JT, Lein ES, Levi BP, and Kalume FK
Abstract: Dravet syndrome (DS) is a devastating developmental epileptic encephalopathy marked by treatment-resistant seizures, developmental delay, intellectual disability, motor deficits, and a 10-20% rate of premature death. Most DS patients harbor loss-of-function mutations in one copy of SCN1A , which has been associated with inhibitory neuron dysfunction. Here we developed an interneuron-targeting AAV human SCN1A gene replacement therapy using cell class-specific enhancers. We generated a split-intein fusion form of SCN1A to circumvent AAV packaging limitations and deliver SCN1A via a dual vector approach using cell class-specific enhancers. These constructs produced full-length Na V 1.1 protein and functional sodium channels in HEK293 cells and in brain cells in vivo . After packaging these vectors into enhancer-AAVs and administering to mice, immunohistochemical analyses showed telencephalic GABAergic interneuron-specific and dose-dependent transgene biodistribution. These vectors conferred strong dose-dependent protection against postnatal mortality and seizures in two DS mouse models carrying independent loss-of-function alleles of Scn1a, at two independent research sites, supporting the robustness of this approach. No mortality or toxicity was observed in wild-type mice injected with single vectors expressing either the N-terminal or C-terminal halves of SCN1A , or the dual vector system targeting interneurons. In contrast, nonselective neuronal targeting of SCN1A conferred less rescue against mortality and presented substantial preweaning lethality. These findings demonstrate proof-of-concept that interneuron-specific AAV-mediated SCN1A gene replacement is sufficient for significant rescue in DS mouse models and suggest it could be an effective therapeutic approach for patients with DS.
Published: 2023
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16. The Concise Guide to PHARMACOLOGY 2023/24: Ion channels.

Author: Alexander SPH, Mathie AA, Peters JA, Veale EL, Striessnig J, Kelly E, Armstrong JF, Faccenda E, Harding SD, Davies JA, Aldrich RW, Attali B, Baggetta AM, Becirovic E, Biel M, Bill RM, Caceres AI, Catterall WA, Conner AC, Davies P, De Clerq K, Delling M, Di Virgilio F, Falzoni S, Fenske S, Fortuny-Gomez A, Fountain S, George C, Goldstein SAN, Grimm C, Grissmer S, Ha K, Hammelmann V, Hanukoglu I, Hu M, Ijzerman AP, Jabba SV, Jarvis M, Jensen AA, Jordt SE, Kaczmarek LK, Kellenberger S, Kennedy C, King B, Kitchen P, Liu Q, Lynch JW, Meades J, Mehlfeld V, Nicke A, Offermanns S, Perez-Reyes E, Plant LD, Rash L, Ren D, Salman MM, Sieghart W, Sivilotti LG, Smart TG, Snutch TP, Tian J, Trimmer JS, Van den Eynde C, Vriens J, Wei AD, Winn BT, Wulff H, Xu H, Yang F, Fang W, Yue L, Zhang X, and Zhu M
Subjects: Humans, Ion Channels chemistry, Ligands, Receptors, G-Protein-Coupled, Databases, Factual, Databases, Pharmaceutical, Pharmacology
Abstract: The Concise Guide to PHARMACOLOGY 2023/24 is the sixth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of approximately 1800 drug targets, and over 6000 interactions with about 3900 ligands. There is an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (https://www.guidetopharmacology.org/), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes almost 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.16178. Ion channels are one of the six major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2023, and supersedes data presented in the 2021/22, 2019/20, 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate., (© 2023 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of The British Pharmacological Society.)
Published: 2023
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17. Health-Related Quality of Life Following Simultaneous Resection for Synchronous Colorectal Cancer Liver Metastases.

Author: Griffiths CD, Karanicolas P, Gallinger S, Wei AD, Francescutti V, and Serrano PE
Subjects: Humans, Quality of Life, Prospective Studies, Pain, Fatigue etiology, Liver Neoplasms secondary, Colorectal Neoplasms surgery, Colorectal Neoplasms pathology
Abstract: Introduction: Up to 25% of colorectal cancer patients present with synchronous liver metastases that can be treated with two operations or a single 'simultaneous' operation. Morbidity and mortality appear similar between approaches, however changes in health-related quality-of-life following simultaneous resection are not well reported., Methods: A prospective, feasibility trial for simultaneous resection of synchronous colorectal liver metastases was conducted. Patients completed the European Organization for Research and Treatment of Cancer QLQ-C30 and LMC21 at baseline (preoperatively), and 4 and 12 weeks postoperatively. Week 4 and 12 scores were compared with baseline using t-tests. Minimally important clinical differences were considered as a 10-point difference from baseline., Results: C30 and QLQ-LMC21 were completed at baseline, 4 weeks, and 12 weeks by 39 (95%), 35 (85%) and 34 (83%) patients, and 39 (95%), 33 (80%) and 33 (80%) patients, respectively; 79% and 75% had at least one MICD according to QLQ-C30 at 4 and 12 weeks. At 4 weeks, physical functioning (mean difference (MD) - 11.9%, p = 0.002), role functioning (MD - 23.6, p = 0.007), and pain (MD + 19.7, p = 0.017) had significant worsening from baseline. At 12 weeks postoperatively, role functioning (MD - 19.7, p = 0.011) and fatigue (MD + 14.3, p = 0.03) were the only domains that remained significantly worse. By 12 weeks, pain and physical functioning had returned to baseline. There were no major demographic differences among those with and without an MICD at 12 weeks., Conclusions: Simultaneous resection of colorectal liver metastases led to clinically significant worsening fatigue and role functioning that persisted at 12 weeks post-surgery., (© 2022. Society of Surgical Oncology.)
Published: 2023
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18. Human KCNQ5 de novo mutations underlie epilepsy and intellectual disability.

Author: Wei AD, Wakenight P, Zwingman TA, Bard AM, Sahai N, Willemsen MH, Schelhaas HJ, Stegmann APA, Verhoeven JS, de Man SA, Wessels MW, Kleefstra T, Shinde DN, Helbig KL, Basinger A, Wagner VF, Rodriguez-Buritica D, Bryant E, Millichap JJ, Millen KJ, Dobyns WB, Ramirez JM, and Kalume FK
Subjects: Animals, Child, Cricetinae, Cricetulus, HEK293 Cells, Humans, KCNQ Potassium Channels, Mice, Mutation, Missense, Seizures, Epilepsy genetics, Intellectual Disability genetics
Abstract: We identified six novel de novo human KCNQ5 variants in children with motor/language delay, intellectual disability (ID), and/or epilepsy by whole exome sequencing. These variants, comprising two nonsense and four missense alterations, were functionally characterized by electrophysiology in HEK293/CHO cells, together with four previously reported KCNQ5 missense variants (Lehman A, Thouta S, Mancini GM, Naidu S, van Slegtenhorst M, McWalter K, Person R, Mwenifumbo J, Salvarinova R; CAUSES Study; EPGEN Study; Guella I, McKenzie MB, Datta A, Connolly MB, Kalkhoran SM, Poburko D, Friedman JM, Farrer MJ, Demos M, Desai S, Claydon T. Am J Hum Genet 101: 65-74, 2017). Surprisingly, all eight missense variants resulted in gain of function (GOF) due to hyperpolarized voltage dependence of activation or slowed deactivation kinetics, whereas the two nonsense variants were confirmed to be loss of function (LOF). One severe GOF allele ( P369T ) was tested and found to extend a dominant GOF effect to heteromeric KCNQ5/3 channels. Clinical presentations were associated with altered KCNQ5 channel gating: milder presentations with LOF or smaller GOF shifts in voltage dependence [change in voltage at half-maximal conduction (Δ V 50 ) = ∼-15 mV] and severe presentations with larger GOF shifts in voltage dependence (Δ V 50 = ∼-30 mV). To examine LOF pathogenicity, two Kcnq5 LOF mouse lines were created with CRISPR/Cas9. Both lines exhibited handling- and thermal-induced seizures and abnormal cortical EEGs consistent with epileptiform activity. Our study thus provides evidence for in vivo KCNQ5 LOF pathogenicity and strengthens the contribution of both LOF and GOF mutations to global pediatric neurological impairment, including ID/epilepsy. NEW & NOTEWORTHY Six novel de novo human KCNQ5 variants were identified from children with neurodevelopmental delay, intellectual disability, and/or epilepsy. Expression of these variants along with four previously reported KCNQ5 variants from a similar cohort revealed GOF potassium channels, negatively shifted in V 50 of activation and/or delayed deactivation kinetics. GOF is extended to KCNQ5/3 heteromeric channels, making these the predominant channels affected in heterozygous de novo patients. Kcnq5 LOF mice exhibited seizures, consistent with in vivo pathogenicity.
Published: 2022
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19. Overexpressing Histone Deacetylase 5 in Rat Dorsal Striatum Alters Reward-Guided Decision-Making and Associated Neural Encoding.

Author: Pribut HJ, Vázquez D, Wei AD, Tennyson SS, Davis IR, Roesch MR, and Li X
Subjects: Animals, Female, Male, Rats, Rats, Sprague-Dawley, Reward, Corpus Striatum metabolism, Decision Making physiology, Histone Deacetylases metabolism
Abstract: Accumulating evidence in the past decade implicates histone-modifying enzymes, such as class I histone deacetylases (HDACs), in learning and memory and, recently, habit formation. However, it is unclear whether HDACs play roles in complex cognitive function. To address this issue, we examined the role of dorsal striatal HDAC5, a class II HDAC, in reward-guided decision-making and associated neural encoding in rats. We first injected adeno-associated virus to overexpress a nuclear-localized HDAC5 in dorsal striatum (DS). We then recorded neural correlates from dorsolateral striatum (DLS) as rats performed two reward-guided choice tasks, in which we manipulated either the size of or delay to reward. During these tasks, rats first learned which of two options led to the better reward and then reversed those contingencies in a second block of trials. We found that rats with HDAC5 overexpression in DS responded faster and chose higher value reward more often during the first block of trials but were less able to reverse those contingencies in the second block of trials. At the neural level, HDAC5 overexpression in DS elevated and reduced the number of cells in DLS that increased firing to stimuli and reward, respectively, and shifted encoding toward cues that predicted more immediate reward. These results suggest that the HDAC5 overexpression in DS contributes to inflexible decision-making, demonstrating a role of histone-modifying enzymes in complex cognitive function. SIGNIFICANCE STATEMENT HDACs are important for learning and habit formation. Here, we expanded on these functions and found that overexpression of HDAC5 produced faster and more automatic behavior, and related changes in dorsolateral striatal neural firing in rats performing a value-based decision-making task. These results implicate HDAC5 as a potential therapeutic target for psychiatric conditions that impair decision-making and executive function., (Copyright © 2021 Pribut et al.)
Published: 2021
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20. THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: Ion channels.

Author: Alexander SP, Mathie A, Peters JA, Veale EL, Striessnig J, Kelly E, Armstrong JF, Faccenda E, Harding SD, Pawson AJ, Southan C, Davies JA, Aldrich RW, Attali B, Baggetta AM, Becirovic E, Biel M, Bill RM, Catterall WA, Conner AC, Davies P, Delling M, Virgilio FD, Falzoni S, Fenske S, George C, Goldstein SAN, Grissmer S, Ha K, Hammelmann V, Hanukoglu I, Jarvis M, Jensen AA, Kaczmarek LK, Kellenberger S, Kennedy C, King B, Kitchen P, Lynch JW, Perez-Reyes E, Plant LD, Rash L, Ren D, Salman MM, Sivilotti LG, Smart TG, Snutch TP, Tian J, Trimmer JS, Van den Eynde C, Vriens J, Wei AD, Winn BT, Wulff H, Xu H, Yue L, Zhang X, and Zhu M
Subjects: Humans, Ion Channels, Knowledge Bases, Ligands, Receptors, G-Protein-Coupled, Databases, Pharmaceutical, Pharmacology
Abstract: The Concise Guide to PHARMACOLOGY 2021/22 is the fifth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of nearly 1900 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes over 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/bph.15539. Ion channels are one of the six major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2021, and supersedes data presented in the 2019/20, 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate., (© 2021 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of The British Pharmacological Society.)
Published: 2021
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21. Prior Cocaine Exposure Increases Firing to Immediate Reward While Attenuating Cue and Context Signals Related to Reward Value in the Insula.

Author: Pribut HJ, Vázquez D, Brockett AT, Wei AD, Tennyson SS, and Roesch MR
Subjects: Animals, Cerebral Cortex physiology, Female, Male, Rats, Rats, Long-Evans, Cerebral Cortex drug effects, Choice Behavior drug effects, Cocaine pharmacology, Cues, Reward
Abstract: The insula contributes to behavioral control and is disrupted by substance abuse, yet we know little about the neural signals underlying these functions or how they are disrupted after chronic drug self-administration. Here, male and female rats self-administered either cocaine (experimental group) or sucrose (control) for 12 consecutive days. After a 1 month withdrawal period, we recorded from insula while rats performed a previously learned reward-guided decision-making task. Cocaine-exposed rats were more sensitive to value manipulations and were faster to respond. These behavioral changes were accompanied by elevated counts of neurons in the insula that increased firing to reward. These neurons also fired more strongly at the start of long-delay trials, when a more immediate reward would be expected, and fired less strongly in anticipation of the actual delivery of delayed rewards. Although reward-related firing to immediate reward was enhanced after cocaine self-administration, reward-predicting cue and context signals were attenuated. In addition to revealing novel firing patterns unique to insula, our data suggest changes in such neural activity likely contribute to impaired decision making observed after drug use. SIGNIFICANCE STATEMENT The insula plays a clear role in drug addiction and drug-induced impairments of decision making, yet there is little understanding of its underlying neural signals. We found that chronic cocaine self-administration reduces cue and context encoding in insula while enhancing signals related to immediate reward. These changes in neural activity likely contribute to impaired decision making and impulsivity observed after drug use., (Copyright © 2021 Pribut et al.)
Published: 2021
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22. Neuronal mechanisms underlying opioid-induced respiratory depression: our current understanding.

Author: Ramirez JM, Burgraff NJ, Wei AD, Baertsch NA, Varga AG, Baghdoyan HA, Lydic R, Morris KF, Bolser DC, and Levitt ES
Subjects: Analgesics, Opioid adverse effects, Animals, Humans, Analgesics, Opioid pharmacology, Central Pattern Generators drug effects, Medulla Oblongata drug effects, Opioid-Related Disorders complications, Respiratory Insufficiency chemically induced
Abstract: Opioid-induced respiratory depression (OIRD) represents the primary cause of death associated with therapeutic and recreational opioid use. Within the United States, the rate of death from opioid abuse since the early 1990s has grown disproportionally, prompting the classification as a nationwide "epidemic." Since this time, we have begun to unravel many fundamental cellular and systems-level mechanisms associated with opioid-related death. However, factors such as individual vulnerability, neuromodulatory compensation, and redundancy of opioid effects across central and peripheral nervous systems have created a barrier to a concise, integrative view of OIRD. Within this review, we bring together multiple perspectives in the field of OIRD to create an overarching viewpoint of what we know, and where we view this essential topic of research going forward into the future.
Published: 2021
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23. HCN Channel Phosphorylation Sites Mapped by Mass Spectrometry in Human Epilepsy Patients and in an Animal Model of Temporal Lobe Epilepsy.

Author: Concepcion FA, Khan MN, Ju Wang JD, Wei AD, Ojemann JG, Ko AL, Shi Y, Eng JK, Ramirez JM, and Poolos NP
Subjects: Animals, Cyclic Nucleotide-Gated Cation Channels metabolism, Humans, Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels, Male, Mass Spectrometry, Phosphorylation, Potassium Channels metabolism, Rats, Rats, Sprague-Dawley, Epilepsy, Epilepsy, Temporal Lobe
Abstract: Because hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channels modulate the excitability of cortical and hippocampal principal neurons, these channels play a key role in the hyperexcitability that occurs during the development of epilepsy after a brain insult, or epileptogenesis. In epileptic rats generated by pilocarpine-induced status epilepticus, HCN channel activity is downregulated by two main mechanisms: a hyperpolarizing shift in gating and a decrease in amplitude of the current mediated by HCN channels, I h . Because these mechanisms are modulated by various phosphorylation signaling pathways, we hypothesized that phosphorylation changes occur at individual HCN channel amino acid residues (phosphosites) during epileptogenesis. We collected CA1 hippocampal tissue from male Sprague Dawley rats made epileptic by pilocarpine-induced status epilepticus, and age-matched naïve controls. We also included resected human brain tissue containing epileptogenic zones (EZs) where seizures arise for comparison to our chronically epileptic rats. After enrichment for HCN1 and HCN2 isoforms by immunoprecipitation and trypsin in-gel digestion, the samples were analyzed by mass spectrometry. We identified numerous phosphosites from HCN1 and HCN2 channels, representing a novel survey of phosphorylation sites within HCN channels. We found high levels of HCN channel phosphosite homology between humans and rats. We also identified a novel HCN1 channel phosphosite S791, which underwent significantly increased phosphorylation during the chronic epilepsy stage. Heterologous expression of a phosphomimetic mutant, S791D, replicated a hyperpolarizing shift in I h gating seen in neurons from chronically epileptic rats. These results show that HCN1 channel phosphorylation is altered in epilepsy and may be of pathogenic importance., (Copyright © 2021 IBRO. Published by Elsevier Ltd. All rights reserved.)
Published: 2021
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24. Presynaptic Mechanisms and KCNQ Potassium Channels Modulate Opioid Depression of Respiratory Drive.

Author: Wei AD and Ramirez JM
Abstract: Opioid-induced respiratory depression (OIRD) is the major cause of death associated with opioid analgesics and drugs of abuse, but the underlying cellular and molecular mechanisms remain poorly understood. We investigated opioid action in vivo in unanesthetized mice and in in vitro medullary slices containing the preBötzinger Complex (preBötC), a locus critical for breathing and inspiratory rhythm generation. Although hypothesized as a primary mechanism, we found that mu-opioid receptor (MOR1)-mediated GIRK activation contributed only modestly to OIRD. Instead, mEPSC recordings from genetically identified Dbx1- derived interneurons, essential for rhythmogenesis, revealed a prevalent presynaptic mode of action for OIRD. Consistent with MOR1-mediated suppression of presynaptic release as a major component of OIRD, Cacna1a KO slices lacking P/Q-type Ca 2+ channels enhanced OIRD. Furthermore, OIRD was mimicked and reversed by KCNQ potassium channel activators and blockers, respectively. In vivo whole-body plethysmography combined with systemic delivery of GIRK- and KCNQ-specific potassium channel drugs largely recapitulated these in vitro results, and revealed state-dependent modulation of OIRD. We propose that respiratory failure from OIRD results from a general reduction of synaptic efficacy, leading to a state-dependent collapse of rhythmic network activity., (Copyright © 2019 Wei and Ramirez.)
Published: 2019
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25. Cold acclimation via the KQT-2 potassium channel is modulated by oxygen in Caenorhabditis elegans .

Author: Okahata M, Wei AD, Ohta A, and Kuhara A
Subjects: Animals, Gene Expression, KCNQ2 Potassium Channel genetics, Models, Biological, Mutation, Sensory Receptor Cells metabolism, Acclimatization, Caenorhabditis elegans physiology, Cold Temperature, KCNQ2 Potassium Channel metabolism, Oxygen metabolism
Abstract: Adaptive responses to external temperatures are essential for survival in changing environments. We show here that environmental oxygen concentration affects cold acclimation in Caenorhabditis elegans and that this response is regulated by a KCNQ-type potassium channel, KQT-2. Depending on culture conditions, kqt-2 mutants showed supranormal cold acclimation, caused by abnormal thermosensation in ADL chemosensory neurons. ADL neurons are responsive to temperature via transient receptor potential channels-OSM-9, OCR-2, and OCR-1-with OCR-1 negatively regulating ADL function. Similarly, KQT-2 and KQT-3 regulate ADL activity, with KQT-2 positively regulating ADL function. Abnormal cold acclimation and acute temperature responses of ADL neurons in kqt-2 mutants were suppressed by an oxygen-receptor mutation in URX coelomic sensory neurons, which are electrically connected to ADL via RMG interneurons. Likewise, low oxygen suppressed supranormal kqt-2 cold acclimation. These data thus demonstrate a simple neuronal circuit integrating two different sensory modalities, temperature and oxygen, that determines cold acclimation.
Published: 2019
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26. International Union of Basic and Clinical Pharmacology. C. Nomenclature and Properties of Calcium-Activated and Sodium-Activated Potassium Channels.

Author: Kaczmarek LK, Aldrich RW, Chandy KG, Grissmer S, Wei AD, and Wulff H
Subjects: Animals, Humans, Intermediate-Conductance Calcium-Activated Potassium Channels classification, Intermediate-Conductance Calcium-Activated Potassium Channels metabolism, Large-Conductance Calcium-Activated Potassium Channel alpha Subunits classification, Large-Conductance Calcium-Activated Potassium Channel alpha Subunits metabolism, Male, Spermatozoa metabolism, Calcium metabolism, Chlorides metabolism, Ion Channel Gating, Potassium Channels classification, Potassium Channels metabolism, Potassium Channels, Calcium-Activated classification, Potassium Channels, Calcium-Activated metabolism, Sodium metabolism, Terminology as Topic
Abstract: A subset of potassium channels is regulated primarily by changes in the cytoplasmic concentration of ions, including calcium, sodium, chloride, and protons. The eight members of this subfamily were originally all designated as calcium-activated channels. More recent studies have clarified the gating mechanisms for these channels and have documented that not all members are sensitive to calcium. This article describes the molecular relationships between these channels and provides an introduction to their functional properties. It also introduces a new nomenclature that differentiates between calcium- and sodium-activated potassium channels., (Copyright © 2016 by The American Society for Pharmacology and Experimental Therapeutics.)
Published: 2017
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27. A novel excitatory network for the control of breathing.

Author: Anderson TM, Garcia AJ 3rd, Baertsch NA, Pollak J, Bloom JC, Wei AD, Rai KG, and Ramirez JM
Subjects: Animals, Cholinergic Neurons metabolism, Female, Glutamine metabolism, Male, Mice, Neural Inhibition physiology, Neural Pathways cytology, Respiratory Center anatomy & histology, Respiratory Center cytology, Synapses metabolism, Time Factors, gamma-Aminobutyric Acid metabolism, Neural Pathways physiology, Respiration, Respiratory Center physiology
Abstract: Breathing must be tightly coordinated with other behaviours such as vocalization, swallowing, and coughing. These behaviours occur after inspiration, during a respiratory phase termed postinspiration. Failure to coordinate postinspiration with inspiration can result in aspiration pneumonia, the leading cause of death in Alzheimer's disease, Parkinson's disease, dementia, and other neurodegenerative diseases. Here we describe an excitatory network that generates the neuronal correlate of postinspiratory activity in mice. Glutamatergic-cholinergic neurons form the basis of this network, and GABA (γ-aminobutyric acid)-mediated inhibition establishes the timing and coordination relative to inspiration. We refer to this network as the postinspiratory complex (PiCo). The PiCo has autonomous rhythm-generating properties and is necessary and sufficient for postinspiratory activity in vivo.The PiCo also shows distinct responses to neuromodulators when compared to other excitatory brainstem networks. On the basis of the discovery of the PiCo, we propose that each of the three phases of breathing is generated by a distinct excitatory network: the pre-Bötzinger complex, which has been linked to inspiration; the PiCo, as described here for the neuronal control of postinspiration; and the lateral parafacial region (pF(L)), which has been associated with active expiration, a respiratory phase that is recruited during high metabolic demand.
Published: 2016
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28. Bidirectional modulation of deep cerebellar nuclear cells revealed by optogenetic manipulation of inhibitory inputs from Purkinje cells.

Author: Han VZ, Magnus G, Zhang Y, Wei AD, and Turner EE
Subjects: Animals, Cerebellar Nuclei cytology, Cerebellar Nuclei drug effects, Channelrhodopsins, Mice, Transgenic, Microscopy, Confocal, Neuronal Plasticity physiology, Optogenetics, Patch-Clamp Techniques, Tissue Culture Techniques, Cerebellar Nuclei physiology, Neural Inhibition physiology, Purkinje Cells physiology, Synaptic Transmission physiology
Abstract: In the mammalian cerebellum, deep cerebellar nuclear (DCN) cells convey all information from cortical Purkinje cells (PCs) to premotor nuclei and other brain regions. However, how DCN cells integrate inhibitory input from PCs with excitatory inputs from other sources has been difficult to assess, in part due to the large spatial separation between cortical PCs and their target cells in the nuclei. To circumvent this problem we have used a Cre-mediated genetic approach to generate mice in which channelrhodopsin-2 (ChR2), fused with a fluorescent reporter, is selectively expressed by GABAergic neurons, including PCs. In recordings from brain slice preparations from this model, mammalian PCs can be robustly depolarized and discharged by brief photostimulation. In recordings of postsynaptic DCN cells, photostimulation of PC axons induces a strong inhibition that resembles these cells' responses to focal electrical stimulation, but without a requirement for the glutamate receptor blockers typically applied in such experiments. In this optogenetic model, laser pulses as brief as 1 ms can reliably induce an inhibition that shuts down the spontaneous spiking of a DCN cell for ∼50 ms. If bursts of such brief light pulses are delivered, a fixed pattern of bistable bursting emerges. If these pulses are delivered continuously to a spontaneously bistable cell, the immediate response to such photostimulation is inhibitory in the cell's depolarized state and excitatory when the membrane has repolarized; a less regular burst pattern then persists after stimulation has been terminated. These results indicate that the spiking activity of DCN cells can be bidirectionally modulated by the optically activated synaptic inhibition of cortical PCs., (Copyright © 2014 IBRO. Published by Elsevier Ltd. All rights reserved.)
Published: 2014
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29. When norepinephrine becomes a driver of breathing irregularities: how intermittent hypoxia fundamentally alters the modulatory response of the respiratory network.

Author: Zanella S, Doi A, Garcia AJ 3rd, Elsen F, Kirsch S, Wei AD, and Ramirez JM
Subjects: Animals, Brain Stem drug effects, Brain Stem metabolism, Female, Male, Mice, Nerve Net drug effects, Norepinephrine physiology, Organ Culture Techniques, Respiration drug effects, Respiratory Center drug effects, Respiratory Mechanics drug effects, Synaptic Transmission drug effects, Synaptic Transmission physiology, Time Factors, Hypoxia metabolism, Nerve Net metabolism, Norepinephrine pharmacology, Respiratory Center metabolism, Respiratory Mechanics physiology
Abstract: Neuronal networks are endogenously modulated by aminergic and peptidergic substances. These modulatory processes are critical for maintaining normal activity and adapting networks to changes in metabolic, behavioral, and environmental conditions. However, disturbances in neuromodulation have also been associated with pathologies. Using whole animals (in vivo) and functional brainstem slices (in vitro) from mice, we demonstrate that exposure to acute intermittent hypoxia (AIH) leads to fundamental changes in the neuromodulatory response of the respiratory network located within the preBötzinger complex (preBötC), an area critical for breathing. Norepinephrine, which normally regularizes respiratory activity, renders respiratory activity irregular after AIH. Respiratory irregularities are caused both in vitro and in vivo by AIH, which increases synaptic inhibition within the preBötC when norepinephrine is endogenously or exogenously increased. These irregularities are prevented by blocking synaptic inhibition before AIH. However, regular breathing cannot be reestablished if synaptic inhibition is blocked after AIH. We conclude that subtle changes in synaptic transmission can have dramatic consequences at the network level as endogenously released neuromodulators that are normally adaptive become the drivers of irregularity. Moreover, irregularities in the preBötC result in irregularities in the motor output in vivo and in incomplete transmission of inspiratory activity to the hypoglossus motor nucleus. Our finding has basic science implications for understanding network functions in general, and it may be clinically relevant for understanding pathological disturbances associated with hypoxic episodes such as those associated with myocardial infarcts, obstructive sleep apneas, apneas of prematurity, Rett syndrome, and sudden infant death syndrome.
Published: 2014
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30. Medial habenula output circuit mediated by α5 nicotinic receptor-expressing GABAergic neurons in the interpeduncular nucleus.

Author: Hsu YW, Tempest L, Quina LA, Wei AD, Zeng H, and Turner EE
Subjects: Animals, Female, Male, Mice, Mice, Inbred C57BL, Mice, Transgenic, Organ Culture Techniques, Serotonergic Neurons metabolism, GABAergic Neurons metabolism, Gene Expression Regulation, Habenula physiology, Nerve Net physiology, Receptors, GABA-A biosynthesis
Abstract: The Chrna5 gene encodes the α5 nicotinic acetylcholine receptor subunit, an "accessory" subunit of pentameric nicotinic receptors, that has been shown to play a role in nicotine-related behaviors in rodents and is genetically linked to smoking behavior in humans. Here we have used a BAC transgenic mouse line, α5(GFP), to examine the cellular phenotype, connectivity, and function of α5-expressing neurons. Although the medial habenula (MHb) has been proposed as a site of α5 function, α5(GFP) is not detectable in the MHb, and α5 mRNA is expressed there only at very low levels. However, α5(GFP) is strongly expressed in a subset of neurons in the interpeduncular nucleus (IP), median raphe/paramedian raphe (MnR/PMnR), and dorsal tegmental area (DTg). Double-label fluorescence in situ hybridization reveals that these neurons are exclusively GABAergic. Transgenic and conventional tract tracing show that α5(GFP) neurons in the IP project principally to the MnR/PMnR and DTg/interfascicular dorsal raphe, both areas rich in serotonergic neurons. The α5(GFP) neurons in the IP are located in a region that receives cholinergic fiber inputs from the ventral MHb, and optogenetically assisted circuit mapping demonstrates a monosynaptic connection between these cholinergic neurons and α5(GFP) IP neurons. Selective inhibitors of both α4β2- and α3β4-containing nicotinic receptors were able to reduce nicotine-evoked inward currents in α5(GFP) neurons in the IP, suggesting a mixed nicotinic receptor profile in these cells. Together, these findings show that the α5-GABAergic interneurons form a link from the MHb to serotonergic brain centers, which is likely to mediate some of the behavioral effects of nicotine.
Published: 2013
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31. Stable respiratory activity requires both P/Q-type and N-type voltage-gated calcium channels.

Author: Koch H, Zanella S, Elsen GE, Smith L, Doi A, Garcia AJ 3rd, Wei AD, Xun R, Kirsch S, Gomez CM, Hevner RF, and Ramirez JM
Subjects: Animals, Animals, Newborn, Brain Stem physiology, Calcium Channels, N-Type deficiency, Calcium Channels, P-Type deficiency, Calcium Channels, P-Type physiology, Calcium Channels, Q-Type deficiency, Calcium Channels, Q-Type physiology, Excitatory Postsynaptic Potentials genetics, Excitatory Postsynaptic Potentials physiology, Female, Male, Mice, Mice, 129 Strain, Mice, Knockout, Organ Culture Techniques, Respiratory Mechanics genetics, Calcium Channels, N-Type physiology, Respiratory Mechanics physiology
Abstract: P/Q-type voltage-gated calcium channels (Ca(v)2.1) play critical presynaptic and postsynaptic roles throughout the nervous system and have been implicated in a variety of neurological disorders. Here we report that mice with a genetic ablation of the Ca(v)2.1 pore-forming α(1A) subunit (α(1A)⁻/⁻) encoded by CACNA1a (Jun et al., 1999) suffer during postnatal development from increasing breathing disturbances that lead ultimately to death. Breathing abnormalities include decreased minute ventilation and a specific loss of sighs, which was associated with lung atelectasis. Similar respiratory alterations were preserved in the isolated in vitro brainstem slice preparation containing the pre-Bötzinger complex. The loss of Ca(v)2.1 was associated with an alteration in the functional dependency on N-type calcium channels (Ca(v)2.2). Blocking N-type calcium channels with conotoxin GVIA had only minor effects on respiratory activity in slices from control (CT) littermates, but abolished respiratory activity in all slices from α(1A)⁻/⁻ mice. The amplitude of evoked EPSPs was smaller in inspiratory neurons from α(1A)⁻/⁻ mice compared with CTs. Conotoxin GVIA abolished all EPSPs in inspiratory neurons from α(1A)⁻/⁻ mice, while the EPSP amplitude was reduced by only 30% in CT mice. Moreover, neuromodulation was significantly altered as muscarine abolished respiratory network activity in α(1A)⁻/⁻ mice but not in CT mice. We conclude that excitatory synaptic transmission dependent on N-type and P/Q-type calcium channels is required for stable breathing and sighing. In the absence of P/Q-type calcium channels, breathing, sighing, and neuromodulation are severely compromised, leading to early mortality.
Published: 2013
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32. Inter-α/β subunits coupling mediating pre-inactivation and augmented activation of BKCa(β2).

Author: Hou P, Zeng W, Gan G, Lv C, Guo X, Zhang Z, Liu H, Wu Y, Yao J, Wei AD, Wang S, and Ding J
Subjects: Computer Simulation, Protein Conformation, Protein Subunits, Static Electricity, Calcium chemistry, Ion Channel Gating, Large-Conductance Calcium-Activated Potassium Channels chemistry, Large-Conductance Calcium-Activated Potassium Channels ultrastructure, Models, Chemical, Models, Molecular
Abstract: Large-conductance calcium-activated potassium (BK) channels regulate the electric properties and neurotransmitter release in excitable cells. Its auxiliary β2 subunits not only enhance gating, but also confer inactivation via a short-lived preinactivated state. However, the mechanism of enhancement and preinactivation of BK channels by β2 remains elusive. Using our newly developed methods, we demonstrated that electrostatic forces played a crucial role in forming multiple complementary pairs of binding sites between α and β subunits including a "PI site" required for channel preinactivation, an "E site" enhancing calcium sensitivity and an "ECaB" coupling site transferring force to gate from the Ca(2+)-bowl via the β2(K33, R34, K35), E site and S6-C linker, independent of another Ca(2+) binding site mSlo1(D362,D367). A comprehensive structural model of the BK(β2) complex was reconstructed based on these functional studies, which paves the way for a clearer understanding of the structural mechanisms of activation and preinactivation of other BK(β) complexes.
Published: 2013
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33. The cellular building blocks of breathing.

Author: Ramirez JM, Doi A, Garcia AJ 3rd, Elsen FP, Koch H, and Wei AD
Subjects: Animals, Brain Stem physiology, Calcium physiology, Carbon Dioxide physiology, Chemoreceptor Cells physiology, Humans, Neurons physiology, Oxygen physiology, Potassium physiology, Receptors, G-Protein-Coupled physiology, Sodium physiology, Synapses physiology, Nerve Net physiology, Neurotransmitter Agents physiology, Respiratory Mechanics physiology
Abstract: Respiratory brainstem neurons fulfill critical roles in controlling breathing: they generate the activity patterns for breathing and contribute to various sensory responses including changes in O2 and CO2. These complex sensorimotor tasks depend on the dynamic interplay between numerous cellular building blocks that consist of voltage-, calcium-, and ATP-dependent ionic conductances, various ionotropic and metabotropic synaptic mechanisms, as well as neuromodulators acting on G-protein coupled receptors and second messenger systems. As described in this review, the sensorimotor responses of the respiratory network emerge through the state-dependent integration of all these building blocks. There is no known respiratory function that involves only a small number of intrinsic, synaptic, or modulatory properties. Because of the complex integration of numerous intrinsic, synaptic, and modulatory mechanisms, the respiratory network is capable of continuously adapting to changes in the external and internal environment, which makes breathing one of the most integrated behaviors. Not surprisingly, inspiration is critical not only in the control of ventilation, but also in the context of "inspiring behaviors" such as arousal of the mind and even creativity. Far-reaching implications apply also to the underlying network mechanisms, as lessons learned from the respiratory network apply to network functions in general., (© 2012 American Physiological Society)
Published: 2012
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34. Draft genome of the filarial nematode parasite Brugia malayi.

Author: Ghedin E, Wang S, Spiro D, Caler E, Zhao Q, Crabtree J, Allen JE, Delcher AL, Guiliano DB, Miranda-Saavedra D, Angiuoli SV, Creasy T, Amedeo P, Haas B, El-Sayed NM, Wortman JR, Feldblyum T, Tallon L, Schatz M, Shumway M, Koo H, Salzberg SL, Schobel S, Pertea M, Pop M, White O, Barton GJ, Carlow CK, Crawford MJ, Daub J, Dimmic MW, Estes CF, Foster JM, Ganatra M, Gregory WF, Johnson NM, Jin J, Komuniecki R, Korf I, Kumar S, Laney S, Li BW, Li W, Lindblom TH, Lustigman S, Ma D, Maina CV, Martin DM, McCarter JP, McReynolds L, Mitreva M, Nutman TB, Parkinson J, Peregrín-Alvarez JM, Poole C, Ren Q, Saunders L, Sluder AE, Smith K, Stanke M, Unnasch TR, Ware J, Wei AD, Weil G, Williams DJ, Zhang Y, Williams SA, Fraser-Liggett C, Slatko B, Blaxter ML, and Scott AL
Subjects: Animals, Brugia malayi physiology, Caenorhabditis genetics, Drosophila melanogaster genetics, Drug Resistance genetics, Filariasis parasitology, Humans, Molecular Sequence Data, Brugia malayi genetics, Genome, Helminth
Abstract: Parasitic nematodes that cause elephantiasis and river blindness threaten hundreds of millions of people in the developing world. We have sequenced the approximately 90 megabase (Mb) genome of the human filarial parasite Brugia malayi and predict approximately 11,500 protein coding genes in 71 Mb of robustly assembled sequence. Comparative analysis with the free-living, model nematode Caenorhabditis elegans revealed that, despite these genes having maintained little conservation of local synteny during approximately 350 million years of evolution, they largely remain in linkage on chromosomal units. More than 100 conserved operons were identified. Analysis of the predicted proteome provides evidence for adaptations of B. malayi to niches in its human and vector hosts and insights into the molecular basis of a mutualistic relationship with its Wolbachia endosymbiont. These findings offer a foundation for rational drug design.
Published: 2007
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35. Chromanol 293B binding in KCNQ1 (Kv7.1) channels involves electrostatic interactions with a potassium ion in the selectivity filter.

Author: Lerche C, Bruhova I, Lerche H, Steinmeyer K, Wei AD, Strutz-Seebohm N, Lang F, Busch AE, Zhorov BS, and Seebohm G
Subjects: Amino Acid Sequence, Animals, Binding Sites, KCNQ1 Potassium Channel drug effects, Models, Molecular, Molecular Sequence Data, Potassium Channels, Voltage-Gated metabolism, Sequence Homology, Amino Acid, Xenopus laevis, Chromans pharmacology, KCNQ1 Potassium Channel metabolism, Sulfonamides pharmacology
Abstract: The chromanol 293B (293B, trans-6-cyano-4-(N-ethylsulfonyl-N-methylamino)-3-hydroxy-2,2-dimethyl-chroman) is a lead compound of potential class III antiarrhythmics that inhibit cardiac I(Ks) potassium channels. These channels are formed by the coassembly of KCNQ1 (Kv7.1, KvLQT1) and KCNE1 subunits. Although homomeric KCNQ1 channels are the principal molecular targets, entry of KCNE1 to the channel complex enhances the chromanol block. Because closely related neuronal KCNQ2 potassium channels are insensitive to the drug, we used KCNQ1/KCNQ2 chimeras to identify the binding site of the inhibitor. We localized the putative drug receptor to the H5 selectivity filter and the S6 transmembrane segment. Single residues affecting 293B inhibition were subsequently identified through systematic exchange of amino acids that were either different in KCNQ1 and KCNQ2 or predicted by a docking model of 293B in the open and closed conformation of KCNQ1. Mutant channel proteins T312S, I337V, and F340Y displayed dramatically lowered sensitivity to chromanol block. The predicted drug binding receptor lies in the inner pore vestibule containing the lower part of the selectivity filter, and the S6 transmembrane domain also reported to be important for binding of benzodiazepines. We propose that the block of the ion permeation pathway involves hydrophobic interactions with the S6 transmembrane residues Ile337 and Phe340, and stabilization of chromanol 293B binding through electrostatic interactions of its oxygen atoms with the most internal potassium ion within the selectivity filter.
Published: 2007
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36. Potassium channels in C. elegans.

Author: Salkoff L, Wei AD, Baban B, Butler A, Fawcett G, Ferreira G, and Santi CM
Subjects: Animals, Caenorhabditis elegans genetics, Genes, Helminth, Humans, Multigene Family, Potassium Channels genetics, Caenorhabditis elegans physiology, Potassium Channels physiology
Abstract: Ion channels are the "transistors" (electronic switches) of the brain that generate and propagate electrical signals in the aqueous environment of the brain and nervous system. Potassium channels are particularly important because, not only do they shape dynamic electrical signaling, they also set the resting potentials of almost all animal cells. Without them, animal life as we know it would not exist, much less higher brain function. Until the completion of the C. elegans genome sequencing project the size and diversity of the potassium channel extended gene family was not fully appreciated. Sequence data eventually revealed a total of approximately 70 genes encoding potassium channels out of the more than 19,000 genes in the genome. This seemed to be an unexpectedly high number of genes encoding potassium channels for an animal with a small nervous system of only 302 neurons. However, it became clear that potassium channels are expressed in all cell types, not only neurons, and that many cells express a complex palette of multiple potassium channels. All types of potassium channels found in C. elegans are conserved in mammals. Clearly, C. elegans is "simple" only in having a limited number of cells dedicated to each organ system; it is certainly not simple with respect to its biochemistry and cell physiology.
Published: 2005
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37. International Union of Pharmacology. LII. Nomenclature and molecular relationships of calcium-activated potassium channels.

Author: Wei AD, Gutman GA, Aldrich R, Chandy KG, Grissmer S, and Wulff H
Subjects: Animals, Humans, Potassium Channels, Calcium-Activated classification, Potassium Channels, Calcium-Activated drug effects, Potassium Channels, Calcium-Activated genetics, Structure-Activity Relationship, Terminology as Topic, Potassium Channels, Calcium-Activated physiology
Published: 2005
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38. KCNQ-like potassium channels in Caenorhabditis elegans. Conserved properties and modulation.

Author: Wei AD, Butler A, and Salkoff L
Subjects: Animals, Brain metabolism, Caenorhabditis elegans, Conserved Sequence, DNA, Complementary metabolism, Diglycerides metabolism, Dose-Response Relationship, Drug, Electrophysiology, Evolution, Molecular, Gene Library, Green Fluorescent Proteins metabolism, Humans, Inhibitory Concentration 50, KCNQ Potassium Channels, KCNQ1 Potassium Channel, Molecular Sequence Data, Multigene Family, Oocytes metabolism, Patch-Clamp Techniques, Phylogeny, Potassium metabolism, Potassium Channels, Voltage-Gated metabolism, Protein Kinase C metabolism, Protein Structure, Tertiary, Receptor, Muscarinic M1 metabolism, Receptors, Muscarinic metabolism, Recombinant Fusion Proteins chemistry, Time Factors, Xenopus, Potassium Channels, Voltage-Gated physiology
Abstract: The human KCNQ gene family encodes potassium channels linked to several genetic syndromes including neonatal epilepsy, cardiac arrhythmia, and progressive deafness. KCNQ channels form M-type potassium channels, which are critical regulators of neuronal excitability that mediate autonomic responses, pain, and higher brain function. Fundamental mechanisms of the normal and abnormal cellular roles for these channels may be gained from their study in simple model organisms. Here we report that a multigene family of KCNQ-like channels is present in the nematode, Caenorhabditis elegans. We show that many aspects of the functional properties, tissue expression pattern, and modulation of these C. elegans channels are conserved, including suppression by the M1 muscarinic receptor. We also describe a conserved mechanism of modulation by diacylglycerol for a subset of C. elegans and vertebrate KCNQ/KQT channels, which is dependent upon the carboxyl-terminal domains of channel subunits and activated protein kinase C.
Published: 2005
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39. Molecular cloning and functional expression of KCNQ5, a potassium channel subunit that may contribute to neuronal M-current diversity.

Author: Lerche C, Scherer CR, Seebohm G, Derst C, Wei AD, Busch AE, and Steinmeyer K
Subjects: Amino Acid Sequence, Animals, Cloning, Molecular, Genetic Variation, Humans, Ion Transport, KCNQ Potassium Channels, Molecular Sequence Data, Potassium metabolism, Potassium Channels metabolism, Sequence Alignment, Xenopus, Neurons physiology, Potassium Channels genetics, Potassium Channels, Voltage-Gated
Abstract: We have isolated KCNQ5, a novel human member of the KCNQ potassium channel gene family that is differentially expressed in subregions of the brain and in skeletal muscle. When expressed in Xenopus oocytes, KCNQ5 generated voltage-dependent, slowly activating K(+)-selective currents that displayed a marked inward rectification at positive membrane voltages. KCNQ5 currents were insensitive to the K(+) channel blocker tetraethylammonium but were strongly inhibited by the selective M-current blocker linopirdine. Upon coexpression with the structurally related KCNQ3 channel subunit, current amplitudes increased 4-5-fold. Compared with homomeric KCNQ5 currents, KCNQ3/KCNQ5 currents also displayed slower activation kinetics and less inward rectification, indicating that KCNQ5 combined with KCNQ3 to form functional heteromeric channel proteins. This functional interaction between KCNQ5 and KCNQ3, a component of the M-channel, suggests that KCNQ5 may contribute to a diversity of heteromeric channels underlying native neuronal M-currents.
Published: 2000
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