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40 results on '"Arun, K."'

1. Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide

Author

Shukla, Arun K, Manglik, Aashish, Kruse, Andrew C, Xiao, Kunhong, Reis, Rosana I, Tseng, Wei-Chou, Staus, Dean P, Hilger, Daniel, Uysal, Serdar, Huang, Li-Yin, Paduch, Marcin, Tripathi-Shukla, Prachi, Koide, Akiko, Koide, Shohei, Weis, William I, Kossiakoff, Anthony A, Kobilka, Brian K, and Lefkowitz, Robert J

Subjects
Biochemistry and Cell Biology, Chemical Sciences, Biological Sciences, Animals, Arrestins, Crystallography, X-Ray, Humans, Immunoglobulin Fab Fragments, Models, Molecular, Phosphopeptides, Phosphorylation, Protein Binding, Protein Conformation, Protein Stability, Rats, Receptors, Vasopressin, Rotation, beta-Arrestin 1, beta-Arrestins, General Science & Technology
Abstract

The functions of G-protein-coupled receptors (GPCRs) are primarily mediated and modulated by three families of proteins: the heterotrimeric G proteins, the G-protein-coupled receptor kinases (GRKs) and the arrestins. G proteins mediate activation of second-messenger-generating enzymes and other effectors, GRKs phosphorylate activated receptors, and arrestins subsequently bind phosphorylated receptors and cause receptor desensitization. Arrestins activated by interaction with phosphorylated receptors can also mediate G-protein-independent signalling by serving as adaptors to link receptors to numerous signalling pathways. Despite their central role in regulation and signalling of GPCRs, a structural understanding of β-arrestin activation and interaction with GPCRs is still lacking. Here we report the crystal structure of β-arrestin-1 (also called arrestin-2) in complex with a fully phosphorylated 29-amino-acid carboxy-terminal peptide derived from the human V2 vasopressin receptor (V2Rpp). This peptide has previously been shown to functionally and conformationally activate β-arrestin-1 (ref. 5). To capture this active conformation, we used a conformationally selective synthetic antibody fragment (Fab30) that recognizes the phosphopeptide-activated state of β-arrestin-1. The structure of the β-arrestin-1-V2Rpp-Fab30 complex shows marked conformational differences in β-arrestin-1 compared to its inactive conformation. These include rotation of the amino- and carboxy-terminal domains relative to each other, and a major reorientation of the 'lariat loop' implicated in maintaining the inactive state of β-arrestin-1. These results reveal, at high resolution, a receptor-interacting interface on β-arrestin, and they indicate a potentially general molecular mechanism for activation of these multifunctional signalling and regulatory proteins.

Published
2013

2. A gravitational-wave standard siren measurement of the Hubble constant

Author

Abbott, B. P., Abbott, R., Abbott, T. D., Acernese, F., Ackley, K., Adams, C., Adams, T., Addesso, P., Adhikari, R. X., Adya, V. B., Affeldt, C., Afrough, M., Agarwal, B., Agathos, M., Agatsuma, K., Aggarwal, N., Aguiar, O. D., Aiello, L., Ain, A., Ajith, P., Allen, B., Allen, G., Allocca, A., Altin, P. A., Amato, A., Ananyeva, A., Anderson, S. B., Anderson, W. G., Angelova, S. V., Antier, S., Appert, S., Arai, K., Araya, M. C., Areeda, J. S., Arnaud, N., Arun, K. G., Ascenzi, S., Ashton, G., Ast, M., Aston, S. M., Astone, P., Atallah, D. V., Aufmuth, P., Aulbert, C., AultONeal, K., Austin, C., Avila-Alvarez, A., Babak, S., Bacon, P., Bader, M. K. M., Bae, S., Baker, P. T., Baldaccini, F., Ballardin, G., Ballmer, S. W., Banagiri, S., Barayoga, J. C., Barclay, S. E., Barish, B. C., Barker, D., Barkett, K., Barone, F., Barr, B., Barsotti, L., Barsuglia, M., Barta, D., Bartlett, J., Bartos, I., Bassiri, R., Basti, A., Batch, J. C., Bawaj, M., Bayley, J. C., Bazzan, M., Bcsy, B., Beer, C., Bejger, M., Belahcene, I., Bell, A. S., Berger, B. K., Bergmann, G., Bero, J. J., Berry, C. P. L., Bersanetti, D., Bertolini, A., Betzwieser, J., Bhagwat, S., Bhandare, R., Bilenko, I. A., Billingsley, G., Billman, C. R., Birch, J., Birney, R., Birnholtz, O., Biscans, S., Biscoveanu, S., Bisht, A., Bitossi, M., Biwer, C., Bizouard, M. A., Blackburn, J. K., Blackman, J., Blair, C. D., Blair, D. G., Blair, R. M., Bloemen, S., Bock, O., Bode, N., Boer, M., Bogaert, G., Bohe, A., Bondu, F., Bonilla, E., Bonnand, R., Boom, B. A., Bork, R., Boschi, V., Bose, S., Bossie, K., Bouffanais, Y., Bozzi, A., Bradaschia, C., Brady, P. R., Branchesi, M., Brau, J. E., Briant, T., Brillet, A., Brinkmann, M., Brisson, V., Brockill, P., Broida, J. E., Brooks, A. F., Brown, D. A., Brown, D. D., Brunett, S., Buchanan, C. C., Buikema, A., Bulik, T., Bulten, H. J., Buonanno, A., Buskulic, D., Buy, C., Byer, R. L., Cabero, M., Cadonati, L., Cagnoli, G., Cahillane, C., Bustillo, J. Caldern, Callister, T. A., Calloni, E., Camp, J. B., Canepa, M., Canizares, P., Cannon, K. C., Cao, H., Cao, J., Capano, C. D., Capocasa, E., Carbognani, F., Caride, S., Carney, M. F., Diaz, J. Casanueva, Casentini, C., Caudill, S., Cavagli, M., Cavalier, F., Cavalieri, R., Cella, G., Cepeda, C. B., Cerd-Durn, P., Cerretani, G., Cesarini, E., Chamberlin, S. J., Chan, M., Chao, S., Charlton, P., Chase, E., Chassande-Mottin, E., Chatterjee, D., Chatziioannou, K., Cheeseboro, B. D., Chen, H. Y., Chen, X., Chen, Y., Cheng, H.-P., Chia, H., Chincarini, A., Chiummo, A., Chmiel, T., Cho, H. S., Cho, M., Chow, J. H., Christensen, N., Chu, Q., Chua, A. J. K., Chua, S., Chung, A. K. W., Chung, S., Ciani, G., Ciolfi, R., Cirelli, C. E., Cirone, A., Clara, F., Clark, J. A., Clearwater, P., Cleva, F., Cocchieri, C., Coccia, E., Cohadon, P.-F., Cohen, D., Colla, A., Collette, C. G., Cominsky, L. R., Constancio, M., Jr., Conti, L., Cooper, S. J., Corban, P., Corbitt, T. R., Cordero-Carrin, I., Corley, K. R., Cornish, N., Corsi, A., Cortese, S., Costa, C. A., Coughlin, M. W., Coughlin, S. B., Coulon, J.-P., Countryman, S. T., Couvares, P., Covas, P. B., Cowan, E. E., Coward, D. M., Cowart, M. J., Coyne, D. C., Coyne, R., Creighton, J. D. E., Creighton, T. D., Cripe, J., Crowder, S. G., Cullen, T. J., Cumming, A., Cunningham, L., Cuoco, E., Dal Canton, T., Dlya, G., Danilishin, S. L., DAntonio, S., Danzmann, K., Dasgupta, A., Da Silva Costa, C. F., Datrier, L. E. H., Dattilo, V., Dave, I., Davier, M., Davis, D., Daw, E. J., Day, B., De, S., DeBra, D., Degallaix, J., De Laurentis, M., Delglise, S., Del Pozzo, W., Demos, N., Denker, T., Dent, T., De Pietri, R., Dergachev, V., De Rosa, R., DeRosa, R. T., De Rossi, C., DeSalvo, R., de Varona, O., Devenson, J., Dhurandhar, S., Daz, M. C., Di Fiore, L., Di Giovanni, M., Di Girolamo, T., Di Lieto, A., Di Pace, S., Di Palma, I., Di Renzo, F., Doctor, Z., Dolique, V., Donovan, F., Dooley, K. L., Doravari, S., Dorrington, I., Douglas, R., Dovale lvarez, M., Downes, T. P., Drago, M., Dreissigacker, C., Driggers, J. C., Du, Z., Ducrot, M., Dupej, P., Dwyer, S. E., Edo, T. B., Edwards, M. C., Effler, A., Eggenstein, H.-B., Ehrens, P., Eichholz, J., Eikenberry, S. S., Eisenstein, R. A., Essick, R. C., Estevez, D., Etienne, Z. B., Etzel, T., Evans, M., Evans, T. M., Factourovich, M., Fafone, V., Fair, H., Fairhurst, S., Fan, X., Farinon, S., Farr, B., Farr, W. M., Fauchon-Jones, E. J., Favata, M., Fays, M., Fee, C., Fehrmann, H., Feicht, J., Fejer, M. M., Fernandez-Galiana, A., Ferrante, I., Ferreira, E. C., Ferrini, F., Fidecaro, F., Finstad, D., Fiori, I., Fiorucci, D., Fishbach, M., Fisher, R. P., Fitz-Axen, M., Flaminio, R., Fletcher, M., Fong, H., Font, J. A., Forsyth, P. W. F., Forsyth, S. S., Fournier, J.-D., Frasca, S., Frasconi, F., Frei, Z., Freise, A., Frey, R., Frey, V., Fries, E. M., Fritschel, P., Frolov, V. V., Fulda, P., Fyffe, M., Gabbard, H., Gadre, B. U., Gaebel, S. M., Gair, J. R., Gammaitoni, L., Ganija, M. R., Gaonkar, S. G., Garcia-Quiros, C., Garufi, F., Gateley, B., Gaudio, S., Gaur, G., Gayathri, V., Gehrels, N., Gemme, G., Genin, E., Gennai, A., George, D., George, J., Gergely, L., Germain, V., Ghonge, S., Ghosh, Abhirup, Ghosh, Archisman, Ghosh, S., Giaime, J. A., Giardina, K. D., Giazotto, A., Gill, K., Glover, L., Goetz, E., Goetz, R., Gomes, S., Goncharov, B., Gonzlez, G., Castro, J. M. Gonzalez, Gopakumar, A., Gorodetsky, M. L., Gossan, S. E., Gosselin, M., Gouaty, R., Grado, A., Graef, C., Granata, M., Grant, A., Gras, S., Gray, C., Greco, G., Green, A. C., Gretarsson, E. M., Groot, P., Grote, H., Grunewald, S., Gruning, P., Guidi, G. M., Guo, X., Gupta, A., Gupta, M. K., Gushwa, K. E., Gustafson, E. K., Gustafson, R., Halim, O., Hall, B. R., Hall, E. D., Hamilton, E. Z., Hammond, G., Haney, M., Hanke, M. M., Hanks, J., Hanna, C., Hannam, M. D., Hannuksela, O. A., Hanson, J., Hardwick, T., Harms, J., Harry, G. M., Harry, I. W., Hart, M. J., Haster, C.-J., Haughian, K., Healy, J., Heidmann, A., Heintze, M. C., Heitmann, H., Hello, P., Hemming, G., Hendry, M., Heng, I. S., Hennig, J., Heptonstall, A. W., Heurs, M., Hild, S., Hinderer, T., Hoak, D., Hofman, D., Holt, K., Holz, D. E., Hopkins, P., Horst, C., Hough, J., Houston, E. A., Howell, E. J., Hreibi, A., Hu, Y. M., Huerta, E. A., Huet, D., Hughey, B., Husa, S., Huttner, S. H., Huynh-Dinh, T., Indik, N., Inta, R., Intini, G., Isa, H. N., Isac, J.-M., Isi, M., Iyer, B. R., Izumi, K., Jacqmin, T., Jani, K., Jaranowski, P., Jawahar, S., Jimnez-Forteza, F., Johnson, W. W., Jones, D. I., Jones, R., Jonker, R. J. G., Ju, L., Junker, J., Kalaghatgi, C. V., Kalogera, V., Kamai, B., Kandhasamy, S., Kang, G., Kanner, J. B., Kapadia, S. J., Karki, S., Karvinen, K. S., Kasprzack, M., Katolik, M., Katsavounidis, E., Katzman, W., Kaufer, S., Kawabe, K., Kflian, F., Keitel, D., Kemball, A. J., Kennedy, R., Kent, C., Key, J. S., Khalili, F. Y., Khan, I., Khan, S., Khan, Z., Khazanov, E. A., Kijbunchoo, N., Kim, Chunglee, Kim, J. C., Kim, K., Kim, W., Kim, W. S., Kim, Y.-M., Kimbrell, S. J., King, E. J., King, P. J., Kinley-Hanlon, M., Kirchhoff, R., Kissel, J. S., Kleybolte, L., Klimenko, S., Knowles, T. D., Koch, P., Koehlenbeck, S. M., Koley, S., Kondrashov, V., Kontos, A., Korobko, M., Korth, W. Z., Kowalska, I., Kozak, D. B., Krmer, C., Kringel, V., Krishnan, B., Krlak, A., Kuehn, G., Kumar, P., Kumar, R., Kumar, S., Kuo, L., Kutynia, A., Kwang, S., Lackey, B. D., Lai, K. H., Landry, M., Lang, R. N., Lange, J., Lantz, B., Lanza, R. K., Lartaux-Vollard, A., Lasky, P. D., Laxen, M., Lazzarini, A., Lazzaro, C., Leaci, P., Leavey, S., Lee, C. H., Lee, H. K., Lee, H. M., Lee, H. W., Lee, K., Lehmann, J., Lenon, A., Leonardi, M., Leroy, N., Letendre, N., Levin, Y., Li, T. G. F., Linker, S. D., Littenberg, T. B., Liu, J., Liu, X., Lo, R. K. L., Lockerbie, N. A., London, L. T., Lord, J. E., Lorenzini, M., Loriette, V., Lormand, M., Losurdo, G., Lough, J. D., Lousto, C. O., Lovelace, G., Lck, H., Lumaca, D., Lundgren, A. P., Lynch, R., Ma, Y., Macas, R., Macfoy, S., Machenschalk, B., MacInnis, M., Macleod, D. M., Hernandez, I. Magaa, Magaa-Sandoval, F., Zertuche, L. Magaa, Magee, R. M., Majorana, E., Maksimovic, I., Man, N., Mandic, V., Mangano, V., Mansell, G. L., Manske, M., Mantovani, M., Marchesoni, F., Marion, F., Mrka, S., Mrka, Z., Markakis, C., Markosyan, A. S., Markowitz, A., Maros, E., Marquina, A., Martelli, F., Martellini, L., Martin, I. W., Martin, R. M., Martynov, D. V., Mason, K., Massera, E., Masserot, A., Massinger, T. J., Masso-Reid, M., Mastrogiovanni, S., Matas, A., Matichard, F., Matone, L., Mavalvala, N., Mazumder, N., McCarthy, R., McClelland, D. E., McCormick, S., McCuller, L., McGuire, S. C., McIntyre, G., McIver, J., McManus, D. J., McNeill, L., McRae, T., McWilliams, S. T., Meacher, D., Meadors, G. D., Mehmet, M., Meidam, J., Mejuto-Villa, E., Melatos, A., Mendell, G., Mercer, R. A., Merilh, E. L., Merzougui, M., Meshkov, S., Messenger, C., Messick, C., Metzdorff, R., Meyers, P. M., Miao, H., Michel, C., Middleton, H., Mikhailov, E. E., Milano, L., Miller, A. L., Miller, B. B., Miller, J., Millhouse, M., Milovich-Goff, M. C., Minazzoli, O., Minenkov, Y., Ming, J., Mishra, C., Mitra, S., Mitrofanov, V. P., Mitselmakher, G., Mittleman, R., Moffa, D., Moggi, A., Mogushi, K., Mohan, M., Mohapatra, S. R. P., Montani, M., Moore, C. J., Moraru, D., Moreno, G., Morriss, S. R., Mours, B., Mow-Lowry, C. M., Mueller, G., Muir, A. W., Mukherjee, Arunava, Mukherjee, D., Mukherjee, S., Mukund, N., Mullavey, A., Munch, J., Muiz, E. A., Muratore, M., Murray, P. G., Napier, K., Nardecchia, I., Naticchioni, L., Nayak, R. K., Neilson, J., Nelemans, G., Nelson, T. J. N., Nery, M., Neunzert, A., Nevin, L., Newport, J. M., Newton, G., Ng, K. K. Y., Nguyen, T. T., Nichols, D., Nielsen, A. B., Nissanke, S., Nitz, A., Noack, A., Nocera, F., Nolting, D., North, C., Nuttall, L. K., Oberling, J., ODea, G. D., Ogin, G. H., Oh, J. J., Oh, S. H., Ohme, F., Okada, M. A., Oliver, M., Oppermann, P., Oram, Richard J., OReilly, B., Ormiston, R., Ortega, L. F., OShaughnessy, R., Ossokine, S., Ottaway, D. J., Overmier, H., Owen, B. J., Pace, A. E., Page, J., Page, M. A., Pai, A., Pai, S. A., Palamos, J. R., Palashov, O., Palomba, C., Pal-Singh, A., Pan, Howard, Pan, Huang-Wei, Pang, B., Pang, P. T. H., Pankow, C., Pannarale, F., Pant, B. C., Paoletti, F., Paoli, A., Papa, M. A., Parida, A., Parker, W., Pascucci, D., Pasqualetti, A., Passaquieti, R., Passuello, D., Patil, M., Patricelli, B., Pearlstone, B. L., Pedraza, M., Pedurand, R., Pekowsky, L., Pele, A., Penn, S., Perez, C. J., Perreca, A., Perri, L. M., Pfeiffer, H. P., Phelps, M., Piccinni, O. J., Pichot, M., Piergiovanni, F., Pierro, V., Pillant, G., Pinard, L., Pinto, I. M., Pirello, M., Pitkin, M., Poe, M., Poggiani, R., Popolizio, P., Porter, E. K., Post, A., Powell, J., Prasad, J., Pratt, J. W. W., Pratten, G., Predoi, V., Prestegard, T., Prijatelj, M., Principe, M., Privitera, S., Prodi, G. A., Prokhorov, L. G., Puncken, O., Punturo, M., Puppo, P., Prrer, M., Qi, H., Quetschke, V., Quintero, E. A., Quitzow-James, R., Raab, F. J., Rabeling, D. S., Radkins, H., Raffai, P., Raja, S., Rajan, C., Rajbhandari, B., Rakhmanov, M., Ramirez, K. E., Ramos-Buades, A., Rapagnani, P., Raymond, V., Razzano, M., Read, J., Regimbau, T., Rei, L., Reid, S., Reitze, D. H., Ren, W., Reyes, S. D., Ricci, F., Ricker, P. M., Rieger, S., Riles, K., Rizzo, M., Robertson, N. A., Robie, R., Robinet, F., Rocchi, A., Rolland, L., Rollins, J. G., Roma, V. J., Romano, J. D., Romano, R., Romel, C. L., Romie, J. H., Rosiska, D., Ross, M. P., Rowan, S., Rdiger, A., Ruggi, P., Rutins, G., Ryan, K., Sachdev, S., Sadecki, T., Sadeghian, L., Sakellariadou, M., Salconi, L., Saleem, M., Salemi, F., Samajdar, A., Sammut, L., Sampson, L. M., Sanchez, E. J., Sanchez, L. E., Sanchis-Gual, N., Sandberg, V., Sanders, J. R., Sassolas, B., Sathyaprakash, B. S., Saulson, P. R., Sauter, O., Savage, R. L., Sawadsky, A., Schale, P., Scheel, M., Scheuer, J., Schmidt, J., Schmidt, P., Schnabel, R., Schofield, R. M. S., Schnbeck, A., Schreiber, E., Schuette, D., Schulte, B. W., Schutz, B. F., Schwalbe, S. G., Scott, J., Scott, S. M., Seidel, E., Sellers, D., Sengupta, A. S., Sentenac, D., Sequino, V., Sergeev, A., Shaddock, D. A., Shaffer, T. J., Shah, A. A., Shahriar, M. S., Shaner, M. B., Shao, L., Shapiro, B., Shawhan, P., Sheperd, A., Shoemaker, D. H., Shoemaker, D. M., Siellez, K., Siemens, X., Sieniawska, M., Sigg, D., Silva, A. D., Singer, L. P., Singh, A., Singhal, A., Sintes, A. M., Slagmolen, B. J. J., Smith, B., Smith, J. R., Smith, R. J. E., Somala, S., Son, E. J., Sonnenberg, J. A., Sorazu, B., Sorrentino, F., Souradeep, T., Spencer, A. P., Srivastava, A. K., Staats, K., Staley, A., Steer, D., Steinke, M., Steinlechner, J., Steinlechner, S., Steinmeyer, D., Stevenson, S. P., Stone, R., Stops, D. J., Strain, K. A., Stratta, G., Strigin, S. E., Strunk, A., Sturani, R., Stuver, A. L., Summerscales, T. Z., Sun, L., Sunil, S., Suresh, J., Sutton, P. J., Swinkels, B. L., Szczepaczyk, M. J., Tacca, M., Tait, S. C., Talbot, C., Talukder, D., Tanner, D. B., Tpai, M., Taracchini, A., Tasson, J. D., Taylor, J. A., Taylor, R., Tewari, S. V., Theeg, T., Thies, F., Thomas, E. G., Thomas, M., Thomas, P., Thorne, K. A., Thrane, E., Tiwari, S., Tiwari, V., Tokmakov, K. V., Toland, K., Tonelli, M., Tornasi, Z., Torres-Forn, A., Torrie, C. I., Tyr, D., Travasso, F., Traylor, G., Trinastic, J., Tringali, M. C., Trozzo, L., Tsang, K. W., Tse, M., Tso, R., Tsukada, L., Tsuna, D., Tuyenbayev, D., Ueno, K., Ugolini, D., Unnikrishnan, C. S., Urban, A. L., Usman, S. A., Vahlbruch, H., Vajente, G., Valdes, G., van Bakel, N., van Beuzekom, M., van den Brand, J. F. J., Van Den Broeck, C., Vander-Hyde, D. C., van der Schaaf, L., van Heijningen, J. V., van Veggel, A. A., Vardaro, M., Varma, V., Vass, S., Vasth, M., Vecchio, A., Vedovato, G., Veitch, J., Veitch, P. J., Venkateswara, K., Venugopalan, G., Verkindt, D., Vetrano, F., Vicer, A., Viets, A. D., Vinciguerra, S., Vine, D. J., Vinet, J.-Y., Vitale, S., Vo, T., Vocca, H., Vorvick, C., Vyatchanin, S. P., Wade, A. R., Wade, L. E., Wade, M., Walet, R., Walker, M., Wallace, L., Walsh, S., Wang, G., Wang, H., Wang, J. Z., Wang, W. H., Wang, Y. F., Ward, R. L., Warner, J., Was, M., Watchi, J., Weaver, B., Wei, L.-W., Weinert, M., Weinstein, A. J., Weiss, R., Wen, L., Wessel, E. K., Weels, P., Westerweck, J., Westphal, T., Wette, K., Whelan, J. T., Whitcomb, S. E., Whiting, B. F., Whittle, C., Wilken, D., Williams, D., Williams, R. D., Williamson, A. R., Willis, J. L., Willke, B., Wimmer, M. H., Winkler, W., Wipf, C. C., Wittel, H., Woan, G., Woehler, J., Wofford, J., Wong, K. W. K., Worden, J., Wright, J. L., Wu, D. S., Wysocki, D. M., Xiao, S., Yamamoto, H., Yancey, C. C., Yang, L., Yap, M. J., Yazback, M., Yu, Hang, Yu, Haocun, Yvert, M., Zadrony, A., Zanolin, M., Zelenova, T., Zendri, J.-P., Zevin, M., Zhang, L., Zhang, M., Zhang, T., Zhang, Y.-H., Zhao, C., Zhou, M., Zhou, Z., Zhu, S. J., Zhu, X. J., Zimmerman, A. B., Zucker, M. E., Zweizig, J., Foley, R. J., Coulter, D. A., Drout, M. R., Kasen, D., Kilpatrick, C. D., Madore, B. F., Murguia-Berthier, A., Pan, Y.-C., Piro, A. L., Prochaska, J. X., Ramirez-Ruiz, E., Rest, A., Rojas-Bravo, C., Shappee, B. J., Siebert, M. R., Simon, J. D., Ulloa, N., Annis, J., Soares-Santos, M., Brout, D., Scolnic, D., Diehl, H. T., Frieman, J., Berger, E., Alexander, K. D., Allam, S., Balbinot, E., Blanchard, P., Butler, R. E., Chornock, R., Cook, E. R., Cowperthwaite, P., Drlica-Wagner, A., Durret, F., Eftekhari, T., Finley, D. A., Fong, W., Fryer, C. L., Garca-Bellido, J., Gill, M. S. S., Gruendl, R. A., Hartley, W., Herner, K., Huterer, D., Kessler, R., Li, T. S., Lin, H., Lopes, P. A. A., Loureno, A. C. C., Margutti, R., Marriner, J., Marshall, J. L., Matheson, T., Medina, G. E., Metzger, B. D., Muoz, R. R., Muir, J., Nicholl, M., Nugent, P., Palmese, A., Paz-Chinchn, F., Quataert, E., Sako, M., Sauseda, M., Schlegel, D. J., Secco, L. F., Smith, N., Sobreira, F., Stebbins, A., Villar, V. A., Vivas, A. K., Wester, W., Williams, P. K. G., Yanny, B., Zenteno, A., Abbott, T. M. C., Abdalla, F. B., Bechtol, K., Benoit-Lvy, A., Bertin, E., Bridle, S. L., Brooks, D., Buckley-Geer, E., Burke, D. L., Rosell, A. Carnero, Kind, M. Carrasco, Carretero, J., Castander, F. J., Cunha, C. E., DAndrea, C. B., da Costa, L. N., Davis, C., DePoy, D. L., Desai, S., Dietrich, J. P., Estrada, J., Fernandez, E., Flaugher, B., Fosalba, P., Gaztanaga, E., Gerdes, D. W., Giannantonio, T., Goldstein, D. A., Gruen, D., Gutierrez, G., Hartley, W. G., Honscheid, K., Jain, B., James, D. J., Jeltema, T., Johnson, M. W. G., Kent, S., Krause, E., Kron, R., Kuehn, K., Kuhlmann, S., Kuropatkin, N., Lahav, O., Lima, M., Maia, M. A. G., March, M., Miller, C. J., Miquel, R., Neilsen, E., Nord, B., Ogando, R. L. C., Plazas, A. A., Romer, A. K., Roodman, A., Rykoff, E. S., Sanchez, E., Scarpine, V., Schubnell, M., Sevilla-Noarbe, I., Smith, M., Smith, R. C., Suchyta, E., Tarle, G., Thomas, D., Thomas, R. C., Troxel, M. A., Tucker, D. L., Vikram, V., Walker, A. R., Weller, J., Zhang, Y., Haislip, J. B., Kouprianov, V. V., Reichart, D. E., Tartaglia, L., Sand, D. J., Valenti, S., Yang, S., Arcavi, Iair, Hosseinzadeh, Griffin, Howell, D. Andrew, McCully, Curtis, Poznanski, Dovi, Vasylyev, Sergiy, Tanvir, N. R., Levan, A. J., Hjorth, J., Cano, Z., Copperwheat, C., de Ugarte-Postigo, A., Evans, P. A., Fynbo, J. P. U., Gonzlez-Fernndez, C., Greiner, J., Irwin, M., Lyman, J., Mandel, I., McMahon, R., Milvang-Jensen, B., OBrien, P., Osborne, J. P., Perley, D. A., Pian, E., Palazzi, E., Rol, E., Rosetti, S., Rosswog, S., Rowlinson, A., Schulze, S., Steeghs, D. T. H., Thne, C. C., Ulaczyk, K., Watson, D., Wiersema, K., Lipunov, V. M., Gorbovskoy, E., Kornilov, V. G., Tyurina, N., Balanutsa, P., Vlasenko, D., Gorbunov, I., Podesta, R., Levato, H., Saffe, C., Buckley, D. A. H., Budnev, N. M., Gress, O., Yurkov, V., Rebolo, R., and Serra-Ricart, M.

Subjects
Gravitational waves -- Measurement, Hubble constant -- Measurement, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): The LIGO Scientific Collaboration and The Virgo Collaboration; B. P. Abbott [1]; R. Abbott [1]; T. D. Abbott [2]; F. Acernese [3, 4]; K. Ackley [5, 6]; C. Adams [...]

Published
2017
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3. Visualization of arrestin recruitment by a G-protein-coupled receptor

Author

Shukla, Arun K., Westfield, Gerwin H., Xiao, Kunhong, Reis, Rosanal., Huang, Li- Yin, Tripathi-Shukla, Prachi, Qian, Jiang, Li, Sheng, Blanc, Adi, Oleskie, Austin N., Dosey, Anne M., Su, Min, Liang, Cui-Rong, Gu, Ling-Ling, Shan, Jin-Ming, Chen, Xin, Hanna, Rachel, Choi, Minjung, Yao, Xiao Jie, Klink, Bjoern U., Kahsai, Alem W., Sidhu, Sachdev S., Koide, Shohei, Penczek, Pawel A., Kossiakoff, Anthony A., Woods, Jr., Virgil L., Kobilka, Brian K., Skiniotis, Georgios, and Lefkowitz, Robert J.

Subjects
Crosslinked polymers -- Research, Crystals -- Structure, G proteins -- Research, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

G-protein-coupled receptors (GPCRs) are critically regulated by β- arrestins, which not only desensitize G-protein signalling but also initiate a G-protein-independent wave of signalling (1-5). A recent surge of structural data on a number of GPCRs, including the b2 adrenergic receptor ([β.sub.2]AR)-G-protein complex, has provided novel insights into the structural basis of receptor activation (6-11). However, complementary information has been lacking on the recruitment of β-arrestins to activated GPCRs, primarily owing to challenges in obtaining stable receptor-β-arrestin complexes for structural studies. Here we devised a strategy for forming and purifying a functional human [β.sub.2]AR-β- arrestin-1 complex that allowed us to visualize its architecture by single-particle negative-stain electron microscopy and to characterize the interactions between [β.sub.2]AR and β-arrestin 1 using hydrogendeuterium exchange mass spectrometry (HDX-MS) and chemical crosslinking. Electron microscopy two-dimensional averages and threedimensional reconstructions reveal bimodal binding of β-arrestin 1 to the [β.sub.2]AR, involving two separate sets of interactions, one with the phosphorylated carboxy terminus of the receptor and the other with its seven-transmembrane core. Areas of reduced HDX together with identification of crosslinked residues suggest engagement of the finger loop of β-arrestin 1 with the seven-transmembrane core of the receptor. In contrast, focal areas of raised HDX levels indicate regions of increased dynamics in both the N and C domains of barrestin 1 when coupled to the [β.sub.2]AR. A molecular model of the [β.sub.2]ARβ-arrestin signalling complex was made by docking activated β-arrestin 1 and [β.sub.2]AR crystal structures into the electron microscopy map densities with constraints provided by HDX-MS and crosslinking, allowing us to obtain valuable insights into the overall architecture of a receptor-arrestin complex. The dynamic and structural information presented here provides a framework for better understanding the basis of GPCR regulation by arrestins., To facilitate the isolation of a stable [β.sub.2]AR-β-arrestin complex, we used a modified [β.sub.2]AR construct with its C terminus replaced by that of the arginine vasopressin type 2 receptor (AVP[R.sub.2]). [...]

Published
2014

4. Cross-neutralization of influenza A viruses mediated by a single antibody loop

Author

Ekiert, Damian C., Kashyap, Arun K., Steel, John, Rubrum, Adam, Bhabha, Gira, Khayat, Reza, Lee, Jeong Hyun, Dillon, Michael A., O'Neil, Ryann E., Faynboym, Aleksandr M., Horowitz, Michael, Horowitz, Lawrence, Ward, Andrew B., Palese, Peter, Webby, Richard, Lerner, Richard A., Bhatt, Ramesh R., and Wilson, Ian A.

Subjects
Influenza viruses -- Research, Agglutinins -- Research, Viruses -- Inactivation, Complementarity-determining regions -- Observations, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the size and shape of protein surfaces that can be targeted. Single protein loops can mediate extremely high-affinity binding, but it is unclear whether such a mechanism is available to antibodies. Here we report the isolation and characterization of an antibody called C05, which neutralizes strains from multiple subtypes of influenza A virus, including H1, H2 and H3. X-ray and electron microscopy structures show that C05 recognizes conserved elements of the receptor-binding site on the haemagglutinin surface glycoprotein. Recognition of the haemagglutinin receptor-binding site is dominated by a single heavy-chain complementarity-determining region 3 loop, with minor contacts from heavy-chain complementarity-determining region 1, and is sufficient to achieve nanomolar binding with a minimal footprint. Thus, binding predominantly with a single loop can allow antibodies to target small, conserved functional sites on otherwise hypervariable antigens., Antibody recognition of protein antigens is predominantly mediated by four to six complementarity-determining regions (CDRs), which are the variable loops at the tip of each Fab. The relatively large footprint [...]

Published
2012
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5. The tomato genome sequence provides insights into fleshy fruit evolution

Author

Sato, Shusei, Tabata, Satoshi, Hirakawa, Hideki, Asamizu, Erika, Shirasawa, Kenta, Isobe, Sachiko, Kaneko, Takakazu, Nakamura, Yasukazu, Shibata, Daisuke, Aoki, Koh, Egholm, Michael, Knight, James, Bogden, Robert, Li, Changbao, Shuang, Yang, Xu, Xun, Pan, Shengkai, Cheng, Shifeng, Liu, Xin, Ren, Yuanyuan, Wang, Jun, Albiero, Alessandro, Dal Pero, Francesca, Todesco, Sara, Van Eck, Joyce, Buels, Robert M., Bombarely, Aureliano, Gosselin, Joseph R., Huang, Minyun, Leto, Jonathan A., Menda, Naama, Strickler, Susan, Mao, Linyong, Gao, Shan, Tecle, Isaak Y., York, Thomas, Zheng, Yi, Vrebalov, Julia T., Lee, JeMin, Zhong, Silin, Mueller, Lukas A., Stiekema, Willem J., Ribeca, Paolo, Alioto, Tyler, Yang, Wencai, Huang, Sanwen, Du, Yongchen, Zhang, Zhonghua, Gao, Jianchang, Guo, Yanmei, Wang, Xiaoxuan, Li, Ying, He, Jun, Li, Chuanyou, Cheng, Zhukuan, Zuo, Jianru, Ren, Jianfeng, Zhao, Jiuhai, Yan, Liuhua, Jiang, Hongling, Wang, Bao, Li, Hongshuang, Li, Zhenjun, Fu, Fuyou, Chen, Bingtang, Han, Bin, Feng, Qi, Fan, Danlin, Wang, Ying, Ling, Hongqing, Xue, Yongbiao, Ware, Doreen, Richard McCombie, W., Lippman, Zachary B., Chia, Jer-Ming, Jiang, Ke, Pasternak, Shiran, Gelley, Laura, Kramer, Melissa, Anderson, Lorinda K., Chang, Song-Bin, Royer, Suzanne M., Shearer, Lindsay A., Stack, Stephen M., Rose, Jocelyn K. C., Xu, Yimin, Eannetta, Nancy, Matas, Antonio J., McQuinn, Ryan, Tanksley, Steven D., Camara, Francisco, Guigó, Roderic, Rombauts, Stephane, Fawcett, Jeffrey, Van de Peer, Yves, Zamir, Dani, Liang, Chunbo, Spannagl, Manuel, Gundlach, Heidrun, Bruggmann, Remy, Mayer, Klaus, Jia, Zhiqi, Zhang, Junhong, Ye, Zhibiao, Bishop, Gerard J., Butcher, Sarah, Lopez-Cobollo, Rosa, Buchan, Daniel, Filippis, Ioannis, Abbott, James, Dixit, Rekha, Singh, Manju, Singh, Archana, Kumar Pal, Jitendra, Pandit, Awadhesh, Kumar Singh, Pradeep, Kumar Mahato, Ajay, Dogra, Vivek, Gaikwad, Kishor, Raj Sharma, Tilak, Mohapatra, Trilochan, Kumar Singh, Nagendra, Causse, Mathilde, Rothan, Christophe, Schiex, Thomas, Noirot, Céline, Bellec, Arnaud, Klopp, Christophe, Delalande, Corinne, Berges, Hélène, Mariette, Jérôme, Frasse, Pierre, Vautrin, Sonia, Zouine, Mohamed, Latché, Alain, Rousseau, Christine, Regad, Farid, Pech, Jean-Claude, Philippot, Murielle, Bouzayen, Mondher, Pericard, Pierre, Osorio, Sonia, Fernandez del Carmen, Asunción, Monforte, Antonio, Granell, Antonio, Fernandez-Muñoz, Rafael, Conte, Mariana, Lichtenstein, Gabriel, Carrari, Fernando, De Bellis, Gianluca, Fuligni, Fabio, Peano, Clelia, Grandillo, Silvana, Termolino, Pasquale, Pietrella, Marco, Fantini, Elio, Falcone, Giulia, Fiore, Alessia, Giuliano, Giovanni, Lopez, Loredana, Facella, Paolo, Perrotta, Gaetano, Daddiego, Loretta, Bryan, Glenn, Orozco, Modesto, Pastor, Xavier, Torrents, David, van Schriek, Marco G. M., Feron, Richard M.C., van Oeveren, Jan, de Heer, Peter, daPonte, Lorena, Jacobs-Oomen, Saskia, Cariaso, Mike, Prins, Marcel, van Eijk, Michiel J. T., Janssen, Antoine, van Haaren, Mark J. J., Jo, Sung-Hwan, Kim, Jungeun, Kwon, Suk-Yoon, Kim, Sangmi, Koo, Dal-Hoe, Lee, Sanghyeob, Hur, Cheol-Goo, Clouser, Christopher, Rico, Alain, Hallab, Asis, Gebhardt, Christiane, Klee, Kathrin, Jöcker, Anika, Warfsmann, Jens, Göbel, Ulrike, Kawamura, Shingo, Yano, Kentaro, Sherman, Jamie D., Fukuoka, Hiroyuki, Negoro, Satomi, Bhutty, Sarita, Chowdhury, Parul, Chattopadhyay, Debasis, Datema, Erwin, Smit, Sandra, Schijlen, Elio G. W. M., van de Belt, Jose, van Haarst, Jan C., Peters, Sander A., van Staveren, Marjo J., Henkens, Marleen H. C., Mooyman, Paul J. W., Hesselink, Thamara, van Ham, Roeland C. H. J., Jiang, Guoyong, Droege, Marcus, Choi, Doil, Kang, Byung-Cheol, Dong Kim, Byung, Park, Minkyu, Kim, Seungill, Yeom, Seon-In, Lee, Yong-Hwan, Choi, Yang-Do, Li, Guangcun, Gao, Jianwei, Liu, Yongsheng, Huang, Shengxiong, Fernandez-Pedrosa, Victoria, Collado, Carmen, Zuñiga, Sheila, Wang, Guoping, Cade, Rebecca, Dietrich, Robert A., Rogers, Jane, Knapp, Sandra, Fei, Zhangjun, White, Ruth A., Thannhauser, Theodore W., Giovannoni, James J., Angel Botella, Miguel, Gilbert, Louise, Gonzalez, Ramon, Luis Goicoechea, Jose, Yu, Yeisoo, Kudrna, David, Collura, Kristi, Wissotski, Marina, Wing, Rod, Schoof, Heiko, Meyers, Blake C., Bala Gurazada, Aishwarya, Green, Pamela J., Mathur, Saloni, Vyas, Shailendra, Solanke, Amolkumar U., Kumar, Rahul, Gupta, Vikrant, Sharma, Arun K., Khurana, Paramjit, Khurana, Jitendra P., Tyagi, Akhilesh K., Dalmay, Tamas, Mohorianu, Irina, Walts, Brandon, Chamala, Srikar, Brad Barbazuk, W., Li, Jingping, Guo, Hui, Lee, Tae-Ho, Wang, Yupeng, Zhang, Dong, Paterson, Andrew H., Wang, Xiyin, Tang, Haibao, Barone, Amalia, Luisa Chiusano, Maria, Raffaella Ercolano, Maria, D’Agostino, Nunzio, Di Filippo, Miriam, Traini, Alessandra, Sanseverino, Walter, Frusciante, Luigi, Seymour, Graham B., Elharam, Mounir, Fu, Ying, Hua, Axin, Kenton, Steven, Lewis, Jennifer, Lin, Shaoping, Najar, Fares, Lai, Hongshing, Qin, Baifang, Qu, Chunmei, Shi, Ruihua, White, Douglas, White, James, Xing, Yanbo, Yang, Keqin, Yi, Jing, Yao, Ziyun, Zhou, Liping, Roe, Bruce A., Vezzi, Alessandro, D’Angelo, Michela, Zimbello, Rosanna, Schiavon, Riccardo, Caniato, Elisa, Rigobello, Chiara, Campagna, Davide, Vitulo, Nicola, Valle, Giorgio, Nelson, David R., De Paoli, Emanuele, Szinay, Dora, de Jong, Hans H., Bai, Yuling, Visser, Richard G. F., Klein Lankhorst, René M., Beasley, Helen, McLaren, Karen, Nicholson, Christine, Riddle, Claire, and Gianese, Giulio

Published
2012
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6. Molecular basis of β-arrestin coupling to formoterol-bound β1-adrenoceptor

Author

Lee, Yang, primary, Warne, Tony, additional, Nehmé, Rony, additional, Pandey, Shubhi, additional, Dwivedi-Agnihotri, Hemlata, additional, Chaturvedi, Madhu, additional, Edwards, Patricia C., additional, García-Nafría, Javier, additional, Leslie, Andrew G. W., additional, Shukla, Arun K., additional, and Tate, Christopher G., additional

Published
2020
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7. An upper limit on the stochastic gravitational-wave background of cosmological origin

Author

Abbott, B. P., Abbott, R., Acernese, F., Adhikari, R., Ajith, P., Allen, B., Allen, G., Alshourbagy, M., Amin, R. S., Anderson, S. B., Anderson, W. G., Antonucci, F., Aoudia, S., Arain, M. A., Araya, M., Armandula, H., Armor, P., Arun, K. G., Aso, Y., Aston, S., Astone, P., Aufmuth, P., Aulbert, C., Babak, S., Baker, P., Ballardin, G., Ballmer, S., Barker, C., Barker, D., Barone, F., Barr, B., Barriga, P., Barsotti, L., Barsuglia, M., Barton, M. A., Bartos, I., Bassiri, R., Bastarrika, M., Bauer, Th. S., Behnke, B., Beker, M., Benacquista, M., Betzwieser, J., Beyersdorf, P. T., Bigotta, S., Bilenko, I. A., Billingsley, G., Birindelli, S., Biswas, R., Bizouard, M. A., Black, E., Blackburn, J. K., Blackburn, L., Blair, D., Bland, B., Boccara, C., Bodiya, T. P., Bogue, L., Bondu, F., Bonelli, L., Bork, R., Boschi, V., Bose, S., Bosi, L., Braccini, S., Bradaschia, C., Brady, P. R., Braginsky, V. B., van den Brand, J. F. J., Brau, J. E., Bridges, D. O., Brillet, A., Brinkmann, M., Brisson, V., Van Den Broeck, C., Brooks, A. F., Brown, D. A., Brummit, A., Brunet, G., Bullington, A., Bulten, H. J., Buonanno, A., Burmeister, O., Buskulic, D., Byer, R. L., Cadonati, L., Cagnoli, G., Calloni, E., Camp, J. B., Campagna, E., Cannizzo, J., Cannon, K. C., Canuel, B., Cao, J., Carbognani, F., Cardenas, L., Caride, S., Castaldi, G., Caudill, S., Cavaglià, M., Cavalier, F., Cavalieri, R., Cella, G., Cepeda, C., Cesarini, E., Chalermsongsak, T., Chalkley, E., Charlton, P., Chassande-Mottin, E., Chatterji, S., Chelkowski, S., Chen, Y., Christensen, N., Chung, C. T. Y., Clark, D., Clark, J., Clayton, J. H., Cleva, F., Coccia, E., Cokelaer, T., Colacino, C. N., Colas, J., Colla, A., Colombini, M., Conte, R., Cook, D., Corbitt, T. R. C., Corda, C., Cornish, N., Corsi, A., Coulon, J.-P., Coward, D., Coyne, D. C., Creighton, J. D. E., Creighton, T. D., Cruise, A. M., Culter, R. M., Cumming, A., Cunningham, L., Cuoco, E., Danilishin, S. L., DʼAntonio, S., Danzmann, K., Dari, A., Dattilo, V., Daudert, B., Davier, M., Davies, G., Daw, E. J., Day, R., De Rosa, R., DeBra, D., Degallaix, J., del Prete, M., Dergachev, V., Desai, S., DeSalvo, R., Dhurandhar, S., Di Fiore, L., Di Lieto, A., Di Paolo Emilio, M., Di Virgilio, A., Díaz, M., Dietz, A., Donovan, F., Dooley, K. L., Doomes, E. E., Drago, M., Drever, R. W. P., Dueck, J., Duke, I., Dumas, J.-C., Dwyer, J. G., Echols, C., Edgar, M., Effler, A., Ehrens, P., Ely, G., Espinoza, E., Etzel, T., Evans, M., Evans, T., Fafone, V., Fairhurst, S., Faltas, Y., Fan, Y., Fazi, D., Fehrmann, H., Ferrante, I., Fidecaro, F., Finn, L. S., Fiori, I., Flaminio, R., Flasch, K., Foley, S., Forrest, C., Fotopoulos, N., Fournier, J.-D., Franc, J., Franzen, A., Frasca, S., Frasconi, F., Frede, M., Frei, M., Frei, Z., Freise, A., Frey, R., Fricke, T., Fritschel, P., Frolov, V. V., Fyffe, M., Galdi, V., Gammaitoni, L., Garofoli, J. A., Garufi, F., Genin, E., Gennai, A., Gholami, I., Giaime, J. A., Giampanis, S., Giardina, K. D., Giazotto, A., Goda, K., Goetz, E., Goggin, L. M., González, G., Gorodetsky, M. L., Goler, S., Gouaty, R., Granata, M., Granata, V., Grant, A., Gras, S., Gray, C., Gray, M., Greenhalgh, R. J. S., Gretarsson, A. M., Greverie, C., Grimaldi, F., Grosso, R., Grote, H., Grunewald, S., Guenther, M., Guidi, G., Gustafson, E. K., Gustafson, R., Hage, B., Hallam, J. M., Hammer, D., Hammond, G. D., Hanna, C., Hanson, J., Harms, J., Harry, G. M., Harry, I. W., Harstad, E. D., Haughian, K., Hayama, K., Heefner, J., Heitmann, H., Hello, P., Heng, I. S., Heptonstall, A., Hewitson, M., Hild, S., Hirose, E., Hoak, D., Hodge, K. A., Holt, K., Hosken, D. J., Hough, J., Hoyland, D., Huet, D., Hughey, B., Huttner, S. H., Ingram, D. R., Isogai, T., Ito, M., Ivanov, A., Johnson, B., Johnson, W. W., Jones, D. I., Jones, G., Jones, R., Sancho de la Jordana, L., Ju, L., Kalmus, P., Kalogera, V., Kandhasamy, S., Kanner, J., Kasprzyk, D., Katsavounidis, E., Kawabe, K., Kawamura, S., Kawazoe, F., Kells, W., Keppel, D. G., Khalaidovski, A., Khalili, F. Y., Khan, R., Khazanov, E., King, P., Kissel, J. S., Klimenko, S., Kokeyama, K., Kondrashov, V., Kopparapu, R., Koranda, S., Kozak, D., Krishnan, B., Kumar, R., Kwee, P., La Penna, P., Lam, P. K., Landry, M., Lantz, B., Laval, M., Lazzarini, A., Lei, H., Lei, M., Leindecker, N., Leonor, I., Leroy, N., Letendre, N., Li, C., Lin, H., Lindquist, P. E., Littenberg, T. B., Lockerbie, N. A., Lodhia, D., Longo, M., Lorenzini, M., Loriette, V., Lormand, M., Losurdo, G., Lu, P., Lubinski, M., Lucianetti, A., Lück, H., Machenschalk, B., MacInnis, M., Mackowski, J.-M., Mageswaran, M., Mailand, K., Majorana, E., Man, N., Mandel, I., Mandic, V., Mantovani, M., Marchesoni, F., Marion, F., Márka, S., Márka, Z., Markosyan, A., Markowitz, J., Maros, E., Marque, J., Martelli, F., Martin, I. W., Martin, R. M., Marx, J. N., Mason, K., Masserot, A., Matichard, F., Matone, L., Matzner, R. A., Mavalvala, N., McCarthy, R., McClelland, D. E., McGuire, S. C., McHugh, M., McIntyre, G., McKechan, D. J. A., McKenzie, K., Mehmet, M., Melatos, A., Melissinos, A. C., Mendell, G., Menéndez, D. F., Menzinger, F., Mercer, R. A., Meshkov, S., Messenger, C., Meyer, M. S., Michel, C., Milano, L., Miller, J., Minelli, J., Minenkov, Y., Mino, Y., Mitrofanov, V. P., Mitselmakher, G., Mittleman, R., Miyakawa, O., Moe, B., Mohan, M., Mohanty, S. D., Mohapatra, S. R. P., Moreau, J., Moreno, G., Morgado, N., Morgia, A., Morioka, T., Mors, K., Mosca, S., Mossavi, K., Mours, B., MowLowry, C., Mueller, G., Muhammad, D., zur Mühlen, H., Mukherjee, S., Mukhopadhyay, H., Mullavey, A., Müller-Ebhardt, H., Munch, J., Murray, P. G., Myers, E., Myers, J., Nash, T., Nelson, J., Neri, I., Newton, G., Nishizawa, A., Nocera, F., Numata, K., Ochsner, E., OʼDell, J., Ogin, G. H., OʼReilly, B., OʼShaughnessy, R., Ottaway, D. J., Ottens, R. S., Overmier, H., Owen, B. J., Pagliaroli, G., Palomba, C., Pan, Y., Pankow, C., Paoletti, F., Papa, M. A., Parameshwaraiah, V., Pardi, S., Pasqualetti, A., Passaquieti, R., Passuello, D., Patel, P., Pedraza, M., Penn, S., Perreca, A., Persichetti, G., Pichot, M., Piergiovanni, F., Pierro, V., Pinard, L., Pinto, I. M., Pitkin, M., Pletsch, H. J., Plissi, M. V., Poggiani, R., Postiglione, F., Principe, M., Prix, R., Prodi, G. A., Prokhorov, L., Punken, O., Punturo, M., Puppo, P., van der Putten, S., Quetschke, V., Raab, F. J., Rabaste, O., Rabeling, D. S., Radkins, H., Raffai, P., Raics, Z., Rainer, N., Rakhmanov, M., Rapagnani, P., Raymond, V., Re, V., Reed, C. M., Reed, T., Regimbau, T., Rehbein, H., Reid, S., Reitze, D. H., Ricci, F., Riesen, R., Riles, K., Rivera, B., Roberts, P., Robertson, N. A., Robinet, F., Robinson, C., Robinson, E. L., Rocchi, A., Roddy, S., Rolland, L., Rollins, J., Romano, J. D., Romano, R., Romie, J. H., Röver, C., Rowan, S., Rüdiger, A., Ruggi, P., Russell, P., Ryan, K., Sakata, S., Salemi, F., Sandberg, V., Sannibale, V., Santamaría, L., Saraf, S., Sarin, P., Sassolas, B., Sathyaprakash, B. S., Sato, S., Satterthwaite, M., Saulson, P. R., Savage, R., Savov, P., Scanlan, M., Schilling, R., Schnabel, R., Schofield, R., Schulz, B., Schutz, B. F., Schwinberg, P., Scott, J., Scott, S. M., Searle, A. C., Sears, B., Seifert, F., Sellers, D., Sengupta, A. S., Sentenac, D., Sergeev, A., Shapiro, B., Shawhan, P., Shoemaker, D. H., Sibley, A., Siemens, X., Sigg, D., Sinha, S., Sintes, A. M., Slagmolen, B. J. J., Slutsky, J., van der Sluys, M. V., Smith, J. R., Smith, M. R., Smith, N. D., Somiya, K., Sorazu, B., Stein, A., Stein, L. C., Steplewski, S., Stochino, A., Stone, R., Strain, K. A., Strigin, S., Stroeer, A., Sturani, R., Stuver, A. L., Summerscales, T. Z., Sun, K.-X., Sung, M., Sutton, P. J., Swinkels, B. L., Szokoly, G. P., Talukder, D., Tang, L., Tanner, D. B., Tarabrin, S. P., Taylor, J. R., Taylor, R., Terenzi, R., Thacker, J., Thorne, K. A., Thorne, K. S., Thüring, A., Tokmakov, K. V., Toncelli, A., Tonelli, M., Torres, C., Torrie, C., Tournefier, E., Travasso, F., Traylor, G., Trias, M., Trummer, J., Ugolini, D., Ulmen, J., Urbanek, K., Vahlbruch, H., Vajente, G., Vallisneri, M., Vass, S., Vaulin, R., Vavoulidis, M., Vecchio, A., Vedovato, G., van Veggel, A. A., Veitch, J., Veitch, P., Veltkamp, C., Verkindt, D., Vetrano, F., Viceré, A., Villar, A., Vinet, J.-Y., Vocca, H., Vorvick, C., Vyachanin, S. P., Waldman, S. J., Wallace, L., Ward, H., Ward, R. L., Was, M., Weidner, A., Weinert, M., Weinstein, A. J., Weiss, R., Wen, L., Wen, S., Wette, K., Whelan, J. T., Whitcomb, S. E., Whiting, B. F., Wilkinson, C., Willems, P. A., Williams, H. R., Williams, L., Willke, B., Wilmut, I., Winkelmann, L., Winkler, W., Wipf, C. C., Wiseman, A. G., Woan, G., Wooley, R., Worden, J., Wu, W., Yakushin, I., Yamamoto, H., Yan, Z., Yoshida, S., Yvert, M., Zanolin, M., Zhang, J., Zhang, L., Zhao, C., Zotov, N., Zucker, M. E., and Zweizig, J.

Published
2009
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9. Visualization of arrestin recruitment by a G-protein-coupled receptor

Author

Sachdev S. Sidhu, Brian K. Kobilka, Xin Chen, Li-Yin Huang, Arun K. Shukla, Austin N. Oleskie, Minjung Choi, Sheng Li, Ling Ling Gu, Anthony A. Kossiakoff, Jiang Qian, Gerwin Westfield, Rosana I. Reis, Robert J. Lefkowitz, Shohei Koide, Alem W. Kahsai, Georgios Skiniotis, Jin Ming Shan, Adi Blanc, Prachi Tripathi-Shukla, Pawel A. Penczek, Cui Rong Liang, Rachel Hanna, Anne M. Dosey, Bjoern U. Klink, Xiao Jie Yao, Kunhong Xiao, Min Su, and Virgil L. Woods

Subjects
Models, Molecular, genetic structures, Molecular model, Arrestins, Biology, Article, Receptors, G-Protein-Coupled, 03 medical and health sciences, 0302 clinical medicine, GTP-binding protein regulators, GTP-Binding Proteins, Sf9 Cells, Arrestin, Animals, Protein Structure, Quaternary, Receptor, beta-Arrestins, 030304 developmental biology, G protein-coupled receptor, 0303 health sciences, Multidisciplinary, Beta-Arrestins, beta-Arrestin 1, Biochemistry, Docking (molecular), Biophysics, Arrestin beta 2, Receptors, Adrenergic, beta-2, 030217 neurology & neurosurgery
Abstract

Single-particle electron microscopy and hydrogen–deuterium exchange mass spectrometry are used to characterize the structure and dynamics of a G-protein-coupled receptor–arrestin complex. Much has been learned about the structure of G-protein-coupled receptors (GCPRs) over the past seven years, but we still don't know what an activated GPCR looks like when it is bound to a β-arrestin. (Arrestins are cellular mediators with a broad range of functions, many of them involving GPCRs.) In this study the authors use single-particle electron microscopy and hydrogen–deuterium exchange mass spectrometry to characterize the structure and dynamics of a GPCR–arrestin complex. Their data support a 'biphasic' mechanism, in which the arrestin initially interacts with the phosphorylated carboxy terminus of the GPCR before re-arranging to more fully engage the membrane protein in a signalling-competent conformation. G-protein-coupled receptors (GPCRs) are critically regulated by β-arrestins, which not only desensitize G-protein signalling but also initiate a G-protein-independent wave of signalling1,2,3,4,5. A recent surge of structural data on a number of GPCRs, including the β2 adrenergic receptor (β2AR)–G-protein complex, has provided novel insights into the structural basis of receptor activation6,7,8,9,10,11. However, complementary information has been lacking on the recruitment of β-arrestins to activated GPCRs, primarily owing to challenges in obtaining stable receptor–β-arrestin complexes for structural studies. Here we devised a strategy for forming and purifying a functional human β2AR–β-arrestin-1 complex that allowed us to visualize its architecture by single-particle negative-stain electron microscopy and to characterize the interactions between β2AR and β-arrestin 1 using hydrogen–deuterium exchange mass spectrometry (HDX-MS) and chemical crosslinking. Electron microscopy two-dimensional averages and three-dimensional reconstructions reveal bimodal binding of β-arrestin 1 to the β2AR, involving two separate sets of interactions, one with the phosphorylated carboxy terminus of the receptor and the other with its seven-transmembrane core. Areas of reduced HDX together with identification of crosslinked residues suggest engagement of the finger loop of β-arrestin 1 with the seven-transmembrane core of the receptor. In contrast, focal areas of raised HDX levels indicate regions of increased dynamics in both the N and C domains of β-arrestin 1 when coupled to the β2AR. A molecular model of the β2AR–β-arrestin signalling complex was made by docking activated β-arrestin 1 and β2AR crystal structures into the electron microscopy map densities with constraints provided by HDX-MS and crosslinking, allowing us to obtain valuable insights into the overall architecture of a receptor–arrestin complex. The dynamic and structural information presented here provides a framework for better understanding the basis of GPCR regulation by arrestins.

Published
2014

10. Cross-neutralization of influenza A viruses mediated by a single antibody loop

Author

Michael Horowitz, Arun K. Kashyap, Ramesh R. Bhatt, Peter Palese, Ryann E. O’Neil, Adam Rubrum, Lawrence Horowitz, Richard A. Lerner, Richard J. Webby, Damian C. Ekiert, Aleksandr M. Faynboym, John Steel, Michael A. Dillon, Jeong Hyun Lee, Reza Khayat, Gira Bhabha, Ian A. Wilson, and Andrew B. Ward

Subjects
Models, Molecular, Protein Conformation, Viral protein, Molecular Sequence Data, Enzyme-Linked Immunosorbent Assay, Hemagglutinin Glycoproteins, Influenza Virus, Cross Reactions, Antibodies, Viral, Crystallography, X-Ray, medicine.disease_cause, Article, Epitope, Conserved sequence, Epitopes, Mice, Influenza A Virus, H1N1 Subtype, Protein structure, Orthomyxoviridae Infections, Antigen, Antibody Specificity, Influenza A virus, medicine, Animals, Binding site, Antigens, Viral, Conserved Sequence, Binding Sites, Multidisciplinary, biology, Influenza A Virus, H3N2 Subtype, Antibodies, Neutralizing, Complementarity Determining Regions, Virology, Influenza Vaccines, Mutation, biology.protein, Antibody
Abstract

Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the size and shape of protein surfaces that can be targeted. Single protein loops can mediate extremely high-affinity binding, but it is unclear whether such a mechanism is available to antibodies. Here we report the isolation and characterization of an antibody called C05, which neutralizes strains from multiple subtypes of influenza A virus, including H1, H2 and H3. X-ray and electron microscopy structures show that C05 recognizes conserved elements of the receptor-binding site on the haemagglutinin surface glycoprotein. Recognition of the haemagglutinin receptor-binding site is dominated by a single heavy-chain complementarity-determining region 3 loop, with minor contacts from heavy-chain complementarity-determining region 1, and is sufficient to achieve nanomolar binding with a minimal footprint. Thus, binding predominantly with a single loop can allow antibodies to target small, conserved functional sites on otherwise hypervariable antigens.

Published
2012

12. Formation of ozone by fireworks

Author

Arun K. Attri, Ujjwal Kumar, and Vinod Kumar Jain

Subjects
Sunlight, Pollutant, Multidisciplinary, Ozone, Meteorology, Air pollution, Fireworks, medicine.disease_cause, chemistry.chemical_compound, chemistry, Greenhouse gas, Environmental chemistry, medicine, Nitrogen oxide, Carbon monoxide
Abstract

Ozone is a secondary pollutant and greenhouse gas that is formed from molecular oxygen in the presence of sunlight and nitrogen oxides. The extent of production also depends on the presence of volatile hydrocarbons, carbon monoxide and methane1,2,3,4,5,6. But we have discovered a surprising source of ozone which is generated in spontaneous bursts even in the absence of sunlight and nitrogen oxides — namely, the exuberant mass of colour-emitting sparklers that are lit during the Diwali festivities, which take place every year during October and November in Delhi, India. The underlying process of ozone formation resembles that induced by ultraviolet radiation in the stratosphere7,8.

Published
2001

14. Ribonuclease activity of wheat leaves and rust infection

Author

Arun K. Chakravorty, Michael Shaw, and L.A. Scrubb

Subjects
Linum, Multidisciplinary, biology, Inoculation, RNase P, food and beverages, Melampsora, Stem rust, biology.organism_classification, Rust, Microbiology, Botany, biology.protein, Ribonuclease, Mycelium
Abstract

REMARKABLE changes in the levels and properties of ribonuclease (RNase) occur following the inoculation of a susceptible variety of flax (Linum usitatissimum L., var. Bison) with flax rust uredospores (Melampsora lini (Ehrenb.) Lev, race 3)1. The increase in RNase activity occurs in two distinct phases; an early phase between 2 to 4 d after inoculation (early RNase) and a later phase, beginning 5 d after inoculation (late RNase). These increases in RNase activity are accompanied by substantial changes in the properties of the enzyme including thermal stability, diethyl-pyrocarbonate-sensitivity and substrate preference1. Further studies (A. K. C., M. S., and L. A. S., unpublished) have revealed that these changes in the properties of RNase are due, at least in part, to the formation of new RNase molecules. These have kinetic and catalytic properties that are quite distinct from both of those ‘host’ RNase from healthy flax cotyledons and ‘rust’ RNase from flax rust uredospores or from rust mycelium grown axenically in a chemically defined medium. That changes in late RNase activity are specifically elicited by compatible host-parasite interactions is indicated by the appearance of late RNase which is not detectable in a resistant variety of flax (Bombay) inoculated with race 3 of Melampsora lini1. Furthermore, the characteristic bimodal increase in RNase activity and the accompanying changes in various properties of the enzyme have been found in a number of other rust-infected plants including pine and Ribes (A. E. Harvey, A. K. C., M. S. and L. A. S., unpublished), and mechanical injury of the healthy host tissues causes a significant increase in the level of RNase. The enzyme remains strictly ‘host-type’, however, no change in its physical or catalytic properties being detectable (ref. 1 and A. E. Harvey, A. K. C., M. S., and L. A. S., unpublished). Here we describe the effect of inoculation with uredospores of three races (56, 56A and Australian race 126 ANZ-6, 7) of wheat stem rust (Puccinia graminis (Pers.) f. sp. tritici Eriks. and E. Henn.) in causing quantitative and qualitative changes in the RNase activity of paired, near-isogenic lines of wheat (Triticum aestivum L.) derived from the variety Chinese Spring and carrying the alleles Sr6 and sr6 (refs 2 and 3), respectively. Both lines give susceptible reactions (infection type 4 (ref. 4)) with race 56A, independent of temperature. The homozygous recessive, sr6, imparts susceptibility (infection type 4) to races 56 and 126 ANZ-6, 7. The dominant allele, Sr6, confers a temperature sensitive reaction to these races; resistance is expressed (infection type 0 (ref. 4)) at 19 to 21° C but breaks down (infection type 4) at higher temperatures (25 to 26° C). A few intercellular hyphae are produced at each infection site at 19 to 21° C. These survive for several days and resume growth when infected plants are transferred to 25 to 26° C; but, in our experience, the longer infected plants are held at 19 to 21° C before transfer, the smaller are the number and size of the sporulating pustules to be developed.

Published
1974

15. Protection of spermatogenesis by α2u globulin in rats treated with oestrogen

Author

Naren M. Biswas, Arun K. Roy, Ajit K. Chowdhury, and Jennie G. Byrd

Subjects
Male, Senescence, medicine.medical_specialty, Saliva, Globulin, medicine.drug_class, Period (gene), Stimulation, Epitopes, Internal medicine, Alpha-Globulins, Testis, medicine, Animals, Spermatogenesis, Testosterone, Multidisciplinary, Estradiol, biology, Estrogen Antagonists, Androgen, Rats, Endocrinology, biology.protein, Follicle Stimulating Hormone
Abstract

α2u GLOBULIN is an androgen-dependent rat urinary protein with a molecular weight of about 23,800 (ref. 1). In the male rat, starting from puberty until senescence, α2u globulin is synthesised and secreted by the hepatic tissue and is rapidly cleared by the kidneys into the urine2–4. In addition to its urinary concentration α2u globulin has been found to be concentrated by the salivary glands and released into the saliva (A.K.R., and J.G.B., in preparation). Synthesis of this protein could be induced in the spayed female rat by androgen, and oestrogenic compounds completely inhibited α2u synthesis in the mature male rat5. But α2u globulin does not bind testosterone, oestradiol-17β or any of their metabolites (unpublished results of A.K.R.). Pretreatment of mature male rats with oestrogen induces a dose-dependent temporary lag period within which α2u globulin is not synthesised even under androgenic stimulation. With a daily oestradiol dose of 50 µg per 100g body weight a lag period extending up to 3–4 weeks has been established6. Although the adult male rat synthesises 20–30 mg of α2u globulin per day, no physiological role of this protein has yet been established. The close parallel between the male reproductive capability and the production of α2u globulin4,5 prompted us to look into the possible reproductive role of this protein. The discovery of the oestrogen-mediated lag period in the mature male rats also provided an opportunity to look into the spermatogenic abnormalities within this lag period and any reparative effects which α2u globulin may have on such damage. The results reported here demonstrate considerable protection of spermatogenesis by α2u globulin against potential damage by oestrogen.

Published
1976

16. Androgenic induction of alpha-2-u-globulin in the rat: requirement of an intact pituitary

Author

Mahendra Kumar, A. E. Axelrod, and Arun K. Roy

Subjects
Immature male, Male, medicine.medical_specialty, Pituitary gland, Adult male, Globulin, Injections, Subcutaneous, Internal medicine, Alpha-Globulins, medicine, Animals, Testosterone, Castration, Gene, Hypophysectomy, Multidisciplinary, biology, Chemistry, Rats, Endocrinology, medicine.anatomical_structure, Pituitary Gland, biology.protein, Alpha-2 adrenergic receptor, Hormone
Abstract

A SEX dependent urinary protein in the rat has been described by Roy and Neuhaus1–4. This protein is an α2-globulin (α2U) of hepatic origin and has a molecular weight of 26,400 (refs. 2 and 3). It is rapidly excreted in the urine3. The level of α2U in blood is therefore very low (< 3 mg per 100 ml. blood)3. This protein is absent in females and immature male rats. The synthesis of α2U is very sensitive to hormonal manipulations4. Treatment with testosterone of the spayed females induces its synthesis whereas treatment of adult male rats with oestradiol brings about a complete repression4. A quantitative immunological method for the assay of α2U has been described3. All of these above mentioned properties make α2U a very convenient system for studying the possible hormonal control of gene action in the mammalian system. In this communication we report our studies on the requirement of the pituitary gland for the androgenic induction of α2U in spayed rats.

Published
1969

17. Androgenic control of a sex-dependent protein in the rat

Author

Arun K. Roy and Otto W. Neuhaus

Subjects
Electrophoresis, Male, medicine.medical_specialty, Immunodiffusion, Anabolism, Adult male, urologic and male genital diseases, Prostate, Internal medicine, medicine, Animals, Testosterone, Castration, α2u globulin, Sex Characteristics, Multidisciplinary, Proteinuria, Estradiol, business.industry, Ovary, Rats, Endocrinology, medicine.anatomical_structure, Liver, Female, medicine.symptom, business
Abstract

PROTEINURIA in the adult male rat has been recognized as a sex characteristic since 19331. At first the source of the sex-related proteins was considered to be the prostate gland1, but more recently evidence has suggested the kidneys2,3. These sites are likely because of the known anabolic effects of androgens on prostatic and renal tissues4,5.

Published
1967

29. Surface-active Characteristics of Sodium Anacardate isolated from Cashew Nut Shell Oil

Author

Anil Bandhu Roy and Arun K. Biswas

Subjects
chemistry.chemical_classification, Cardanol, Multidisciplinary, biology, Double bond, Anacardium, Resorcinol, biology.organism_classification, chemistry.chemical_compound, chemistry, Pulmonary surfactant, Organic chemistry, Molecule, Salicylic acid, Derivative (chemistry)
Abstract

CASHEW nut (Anacardium occidentale Linn.) shell liquid obtained from unroasted shells was found by Stadeler1 to consist chiefly of anacardic acid (A) (on heating, this is decarboxylated to cardanol (B)), a salicylic acid derivative with a long unsaturated side-chain in the position ortho to the carboxyl group, and cardol (C), a resorcinol derivative with a similar side-chain. Smith2 showed that the unbranched side-chain consisted of 15 carbon atoms and 2 double bonds ; other workers3 have shown that the oily liquid is really a mixture of saturated and mono-, di-, and tri-olefinic compounds in proportions that give, on average, about two double bonds per molecule. Although the surface-active properties of the sulphonated shell liquid have already been studied4, no thorough investigation has yet been carried out on anacardic acid, which, being an arylalkyl surfactant and a promising bactericidal agent, needs special attention5. Results of a preliminary study on sodium anacardate as a surfactant and bactericidal agent are reported here. .

Published
1958

30. Absorption Spectra of Saturated Chlorides of Multivalent Elements

Author

Arun K. Dutta and Megh Nad Saha

Subjects
Multidisciplinary, Absorption spectroscopy, Chemistry, Sodium, Inorganic chemistry, Analytical chemistry, Valency, Ionic bonding, Halide, chemistry.chemical_element, Absorption (chemistry), Alkali metal, Standard enthalpy of formation
Abstract

FRANCK and his co-workers have shown that the vapours of alkali halides show a continuous absorption spectrum beginning from a long waverlength limit and extending towards the ultra-violet. He interpreted the absorption spectrum as follows: if we take a substance like sodium chloride the valency electron of Na in the normal state may be supposed to pass over completely to Cl and the combination consists of Na+Cl-. Such a combination is called ionic. When light falls on sodium chloride vapour, the electron passes over from Cl- to Na+, the molecule thus splitting into Na and Cl. Franck obtains the heat of formation Q of NaCl from atomic Na and atomic Cl with the aid of a Born cycle and finds that Q =N hI½ where I½ = frequency of the beginning of continuous absorption.

Published
1931

31. Uranium (VI) – Chromotropic Acid Chelate

Author

Arun K. Dey and Samir K. Banerji

Subjects
Multidisciplinary, Inorganic chemistry, chemistry.chemical_element, Uranium, Chromotropic acid, Metal, chemistry.chemical_compound, Qualitative analysis, chemistry, visual_art, visual_art.visual_art_medium, Chelation, Trivial name, Titanium, Nuclear chemistry, Naphthalene
Abstract

DISODIUM- 1:8-dihydroxy naphthalene-3:6-disulphonate (trivial name chromotropic acid–sodium salt)yields coloured lakes with various cations1. Investigations of chelates of chromotropic acid with iron (III)2 and titanium (IV)3,4 have already been made. Sommer et al. have extensively examined chelates of titanium with chromotropic acid and various polyphenols5–7 and have discussed the structure of the metal chelates. The use of chromotropic acid in the colorimetric determination of uranium8,9has also been reported.

Published
1963

32. Protection of spermatogenesis by α2uglobulin in rats treated with oestrogen

Author

ROY, ARUN K., BYRD, JENNIE G., BISWAS, NAREN M., and CHOWDHURY, AJIT K.

Abstract

α2uGLOBULIN is an androgen-dependent rat urinary protein with a molecular weight of about 23,800 (ref. 1). In the male rat, starting from puberty until senescence, α2uglobulin is synthesised and secreted by the hepatic tissue and is rapidly cleared by the kidneys into the urine2–4. In addition to its urinary concentration α2uglobulin has been found to be concentrated by the salivary glands and released into the saliva (A.K.R., and J.G.B., in preparation). Synthesis of this protein could be induced in the spayed female rat by androgen, and oestrogenic compounds completely inhibited α2usynthesis in the mature male rat5. But α2uglobulin does not bind testosterone, oestradiol-17β or any of their metabolites (unpublished results of A.K.R.). Pretreatment of mature male rats with oestrogen induces a dose-dependent temporary lag period within which α2uglobulin is not synthesised even under androgenic stimulation. With a daily oestradiol dose of 50 µg per 100g body weight a lag period extending up to 3–4 weeks has been established6. Although the adult male rat synthesises 20–30 mg of α2uglobulin per day, no physiological role of this protein has yet been established. The close parallel between the male reproductive capability and the production of α2uglobulin4,5prompted us to look into the possible reproductive role of this protein. The discovery of the oestrogen-mediated lag period in the mature male rats also provided an opportunity to look into the spermatogenic abnormalities within this lag period and any reparative effects which α2uglobulin may have on such damage. The results reported here demonstrate considerable protection of spermatogenesis by α2uglobulin against potential damage by oestrogen.

Published
1976
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33. Heat of Dissociation of Nitrogen

Author

Arun K. Datta

Subjects
Multidisciplinary, Materials science, Absorption spectroscopy, chemistry, chemistry.chemical_element, Atomic physics, Nitrogen, Dissociation (chemistry)
Abstract

THE value of the heat of dissociation of nitrogen has formed a lively subject of controversy in the past few years. All values from 19 to 7 volts have been given by various workers for the dissociation potential. I have recently determined this value by examining the absorption spectrum of N2O in a manner which has already been explained in my note on the spectrum of SO3.1 The value comes out to be 8.8 volts or 203 kcal.

Published
1932

34. Surface-active Characteristics of Sodium Salts of Anacardic Acids of Varying Unsaturation

Author

Arun K. Biswas and Anil B. Ray

Subjects
chemistry.chemical_classification, Degree of unsaturation, Multidisciplinary, Double bond, biology, Anacardium, chemistry.chemical_element, biology.organism_classification, Anacardic acids, chemistry.chemical_compound, chemistry, Organic chemistry, Molecule, Phenol, Carbon, Alkyl
Abstract

CASHEW nut (Anacardium occidentale Linn.) shell liquid chiefly consists of anacardic acid, an ortho-carboxymeta-alkyl phenol. Earlier workers1–3 have shown that the unsaturated alkyl side-chain in the acid consists of 15 carbon atoms and that the acid is a mixture of saturated and mono-, di-, and tri-olefinic compounds, in proportions that give, on average, about two double bonds per molecule. Properties of the sodium salt of the whole anacardic acid have been reported earlier4–6. However, considerable interest remains in the examination of surface-activity unsaturation relationship in the anacardic acid series. The work recorded here is an extension of previous work5 on whole anacardic acid.

Published
1963

35. Heat of Dissociation of Oxygen

Author

Arun K. Dutta

Subjects
Multidisciplinary, Chemistry, Excited state, Atom, chemistry.chemical_element, Molecule, Atomic physics, Oxygen, Dissociation (chemistry), Excitation, Spectral line, Standard enthalpy of formation
Abstract

THE heat of dissociation of oxygen has given rise to some lively controversies in recent years. Mecke1 concluded from the photochemical work of Norrish on NO2 that DO2=128 kcal., a view which was supported by V. Henri2 from the interpretation of the predissociation spectra of NO2 and SO2. Birge and Sponer,3 on the other hand, conclude, from the analysis of the Runge-Schumann bands, that the heat of dissociation in the excited state amounts to 162 kcal. Herzberg 4 was of opinion that the molecule in the excited state was made up of a (3P) oxygen atom and a (1D2) atom, hence subtracting from Birge's figures the heat of excitation to the 1D2 state, namely, 45 kcal., he gets the heat of dissociation of O2 into two 3P atoms as 117 kcal. This view seems to have been accepted by Franck, though Copeland5 supports Mecke's value of 128 kcal. from his study of the heat of formation of the molecule from the atomised state in the discharge tube.

Published
1932

36. Existence of Cupric Hexammino Sulphate

Author

Arun K. Dey

Subjects
Ammonia, chemistry.chemical_compound, Ammonium hydroxide, Multidisciplinary, Chemistry, Inorganic chemistry, Copper salt, Halide, chemistry.chemical_element, Molecule, Cupric sulphate, Copper
Abstract

WHILE the hexammino compounds of the halides, nitrates and other salts of copper are well known, nothing seems to be on record regarding the existence of cupric hexammino sulphate. In recent communications, Dey and Bhattacharya1 have described a new method for the isolation of cupric pentammino sulphate, from ammoniacal solutions of cupric sulphate. In other publications from this laboratory, Dey has recorded the results of the conductometric measurements of mixtures of cupric nitrate2 or chloride3, with ammonium hydroxide solutions, of various compositions. The conductometric curves gave breaks corresponding to three, four, five and six molecules of ammonia for one molecule of the copper salt, thus affording the evidence for the existence of tri-, tetra-, penta- and hexa-ammino cupric compounds. In the case of cupric ammino sulphates, however, the triammino compound is not found, whereas the three other compounds are formed. The changes in the extinction coefficients of mixtures have also been studied by means of a Nutting's spectrophotometer, and the results confirm those obtained by the electrical conductivity method. We thus find that these results indicate the definite existence of cupric hexammino sulphate, as well, in an ammoniacal solution of cupric sulphate.

Published
1947

37. Post-Dissociation Radiation from Sulphur Trioxide

Author

Arun K. Dutta

Subjects
chemistry.chemical_compound, Multidisciplinary, chemistry, Excited state, Halogen, Photodissociation, chemistry.chemical_element, Radiation, Photochemistry, Iodine, Sulfur, Trioxide, Dissociation (chemistry)
Abstract

ACCORDING to Franck's theory of photodissociation of the halogens, the effect of light absorption is to split I2 into a normal iodine and an excited iodine (2P½). No direct proof has yet been forthcoming that the metastable atoms are actually produced in the reaction.

Published
1932

38. Composition of Cupric Ammino Nitrates

Author

Arun K. Dey

Subjects
Multidisciplinary, Precipitation (chemistry), Chemistry, Cupric sulphate, Composition (visual arts), Nuclear chemistry
Abstract

IN a recent publication1 from this laboratory, we have described our results on the study of the composition of cupric ammino sulphates by the new electrical conductivity method2 of Dey and Bhattacharya. In other communications we have described the isolation of cupric pentammino sulphate by alcoholic precipitation from ammoniacal solutions of cupric sulphate.

Published
1946

40. Molecular basis of β-arrestin coupling to formoterol-bound β 1 -adrenoceptor.

Author

Lee Y, Warne T, Nehmé R, Pandey S, Dwivedi-Agnihotri H, Chaturvedi M, Edwards PC, García-Nafría J, Leslie AGW, Shukla AK, and Tate CG

Subjects
Amino Acid Sequence, Animals, Binding Sites, GTP-Binding Protein alpha Subunits, Gs chemistry, GTP-Binding Protein alpha Subunits, Gs metabolism, GTP-Binding Protein alpha Subunits, Gs ultrastructure, HEK293 Cells, Humans, Models, Molecular, Multiprotein Complexes, Receptors, Adrenergic, beta-1 metabolism, Single-Chain Antibodies chemistry, Single-Chain Antibodies metabolism, Single-Chain Antibodies ultrastructure, Zebrafish, beta-Arrestin 1 metabolism, Cryoelectron Microscopy, Formoterol Fumarate chemistry, Formoterol Fumarate metabolism, Receptors, Adrenergic, beta-1 chemistry, Receptors, Adrenergic, beta-1 ultrastructure, beta-Arrestin 1 chemistry, beta-Arrestin 1 ultrastructure
Abstract

The β 1 -adrenoceptor (β 1 AR) is a G-protein-coupled receptor (GPCR) that couples 1 to the heterotrimeric G protein G s . G-protein-mediated signalling is terminated by phosphorylation of the C terminus of the receptor by GPCR kinases (GRKs) and by coupling of β-arrestin 1 (βarr1, also known as arrestin 2), which displaces G s and induces signalling through the MAP kinase pathway 2 . The ability of synthetic agonists to induce signalling preferentially through either G proteins or arrestins-known as biased agonism 3 -is important in drug development, because the therapeutic effect may arise from only one signalling cascade, whereas the other pathway may mediate undesirable side effects 4 . To understand the molecular basis for arrestin coupling, here we determined the cryo-electron microscopy structure of the β 1 AR-βarr1 complex in lipid nanodiscs bound to the biased agonist formoterol 5 , and the crystal structure of formoterol-bound β 1 AR coupled to the G-protein-mimetic nanobody 6 Nb80. βarr1 couples to β 1 AR in a manner distinct to that 7 of G s coupling to β 2 AR-the finger loop of βarr1 occupies a narrower cleft on the intracellular surface, and is closer to transmembrane helix H7 of the receptor when compared with the C-terminal α5 helix of G s . The conformation of the finger loop in βarr1 is different from that adopted by the finger loop of visual arrestin when it couples to rhodopsin 8 . β 1 AR coupled to βarr1 shows considerable differences in structure compared with β 1 AR coupled to Nb80, including an inward movement of extracellular loop 3 and the cytoplasmic ends of H5 and H6. We observe weakened interactions between formoterol and two serine residues in H5 at the orthosteric binding site of β 1 AR, and find that formoterol has a lower affinity for the β 1 AR-βarr1 complex than for the β 1 AR-G s complex. The structural differences between these complexes of β 1 AR provide a foundation for the design of small molecules that could bias signalling in the β-adrenoceptors.

Published
2020
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