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18 results on '"Nevins, B."'

1. Horizons: Nuclear Astrophysics in the 2020s and Beyond

Author

Schatz, H., Reyes, A. D. Becerril, Best, A., Brown, E. F., Chatziioannou, K., Chipps, K. A., Deibel, C. M., Ezzeddine, R., Galloway, D. K., Hansen, C. J., Herwig, F., Ji, A. P., Lugaro, M., Meisel, Z., Norman, D., Read, J. S., Roberts, L. F., Spyrou, A., Tews, I., Timmes, F. X., Travaglio, C., Vassh, N., Abia, C., Adsley, P., Agarwal, S., Aliotta, M., Aoki, W., Arcones, A., Aryan, A., Bandyopadhyay, A., Banu, A., Bardayan, D. W., Barnes, J., Bauswein, A., Beers, T. C., Bishop, J., Boztepe, T., Côté, B., Caplan, M. E., Champagne, A. E., Clark, J. A., Couder, M., Couture, A., de Mink, S. E., Debnath, S., deBoer, R. J., Hartogh, J. den, Denissenkov, P., Dexheimer, V., Dillmann, I., Escher, J. E., Famiano, M. A., Farmer, R., Fisher, R., Fröhlich, C., Frebel, A., Fryer, C., Fuller, G., Ganguly, A. K., Ghosh, S., Gibson, B. K., Gorda, T., Gourgouliatos, K. N., Graber, V., Gupta, M., Haxton, W., Heger, A., Hix, W. R., Ho, W C. G., Holmbeck, E. M., Hood, A. A., Huth, S., Imbriani, G., Izzard, R. G., Jain, R., Jayatissa, H., Johnston, Z., Kajino, T., Kankainen, A., Kiss, G. G., Kwiatkowski, A., La Cognata, M., Laird, A. M., Lamia, L., Landry, P., Laplace, E., Launey, K. D., Leahy, D., Leckenby, G., Lennarz, A., Longfellow, B., Lovell, A. E., Lynch, W. G., Lyons, S. M., Maeda, K., Masha, E., Matei, C., Merc, J., Messer, B., Montes, F., Mukherjee, A., Mumpower, M., Neto, D., Nevins, B., Newton, W. G., Nguyen, L. Q., Nishikawa, K., Nishimura, N., Nunes, F. M., O'Connor, E., O'Shea, B. W., Ong, W-J., Pain, S. D., Pajkos, M. A., Pignatari, M., Pizzone, R. G., Placco, V. M., Plewa, T., Pritychenko, B., Psaltis, A., Puentes, D., Qian, Y-Z., Radice, D., Rapagnani, D., Rebeiro, B. M., Reifarth, R., Richard, A. L., Rijal, N., Roederer, I. U., Rojo, J. S., K, J. S, Saito, Y., Schwenk, A., Sergi, M. L., Sidhu, R. S., Simon, A., Sivarani, T., Skúladóttir, Á., Smith, M. S., Spiridon, A., Sprouse, T. M., Starrfield, S., Steiner, A. W., Strieder, F., Sultana, I., Surman, R., Szücs, T., Tawfik, A., Thielemann, F., Trache, L., Trappitsch, R., Tsang, M. B., Tumino, A., Upadhyayula, S., Martínez, J. O. Valle, Van der Swaelmen, M., Vázquez, C. Viscasillas, Watts, A., Wehmeyer, B., Wiescher, M., Wrede, C., Yoon, J., Zegers, R G. T., Zermane, M. A., and Zingale, M.

Subjects
Nuclear Experiment, Astrophysics - High Energy Astrophysical Phenomena, Astrophysics - Solar and Stellar Astrophysics, Nuclear Theory
Abstract

Nuclear Astrophysics is a field at the intersection of nuclear physics and astrophysics, which seeks to understand the nuclear engines of astronomical objects and the origin of the chemical elements. This white paper summarizes progress and status of the field, the new open questions that have emerged, and the tremendous scientific opportunities that have opened up with major advances in capabilities across an ever growing number of disciplines and subfields that need to be integrated. We take a holistic view of the field discussing the unique challenges and opportunities in nuclear astrophysics in regards to science, diversity, education, and the interdisciplinarity and breadth of the field. Clearly nuclear astrophysics is a dynamic field with a bright future that is entering a new era of discovery opportunities., Comment: 96 pages. Submitted to Journal of Physics G

Published
2022
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3. Efficacy and safety of alirocumab in reducing lipids and cardiovascular events

Author

Robinson, Jg, Farnier, M, Krempf, M, Bergeron, J, Luc, G, Averna, M, Stroes, Es, Langslet, G, Raal, Fj, El Shahawy, M, Koren, Mj, Lepor, Ne, Lorenzato, C, Pordy, R, Chaudhari, U, Kastelein, Jj, Caccavo, A, Codutti, O, Gelersztein, E, Vico, M, Zaidman, C, Majul, C, Balthazar, Y, Capiau, L, Vrolix, M, Vermeersch, P, Gotchev, D, Todorov, G, Tumbev, H, Tzekova, M, Gronkova, N, Dimov, B, Nikolaeva, A, Devedzhiev, T, Mincheva, V, D'Ignazio, G, Dzongowski, P, Elliott, T, Hart, R, Hoag, G, Martinho, V, O'Mahony, M, Tellier, G, Pandey, S, Heaton, K, Constance, C, Phaneuf, Dc, Shu, D, Narvaez, Nc, Cañon, Co, Cardenas, Sp, Loayza, Ms, de Salazar, Dm, Lopez, Rb, Gomez, Ji, Mendoza, Ja, Cure, Cc, Ceska, R, Zidkova, E, Jansky, P, Egstrup, K, Klausen, Ib, Lomholdt, J, Gislason, G, Torp Pedersen, C, Poulsen, S, Kuusela, M, Kekki, S, Nieminen, S, Tuomilehto, J, Boye, A, Bruckert, E, Cadinot, D, Lejay, D, Revol, T, Schaupp, T, Bonnet, J, Paillard, F, Moulin, P, Junggeburth, J, Isermann, B, Zühlke, M, Züchner, D, Theis, E, Stößel, J, König, Hj, Rinke, A, Piechatzek, R, Contzen, C, Lappo, M, Himpel Boenninghoff, Aa, Meissner, G, Maus, O, Degtyareva, E, Schulze, Ed, Horacek, T, Marten, I, Becher, P, Matoltsy, A, Nyirati, G, Paragh, G, Zilahi, Z, Nagy, K, Kanakaridisz, N, Beke, E, Biro, J, Schnabel, R, Elias, M, Gavish, D, Francis, A, Nseir, W, Zimlichman, R, Pozzi, C, Lembo, G, Bucci, M, Mezzetti, A, De Pellegrin, Am, Salvioni, A, De Cesare, N, Briones, Ir, Campos, Pf, Rosas, El, Espinosa, Ev, Salazar, Ma, Ruiz, Ab, Furusho, Lc, Olvera, I, Stroes, E, van den Berg, R, Basart, D, Köse, V, Kentgens, S, Peeters, M, Hoogendijk, J, Voors Pette, C, Agous, I, van Kempen, W, Lingan, Gr, Kooy, A, Troquay, R, Herrman, J, Hoivik, H, Norheim, P, Risberg, K, Høivik, Ho, Elle, S, Derezinski, T, Miekus, P, Ogorek, M, Szymkowiak, K, Cesar, M, Gawron, A, Dabrowska, M, Blach, E, Konieczny, M, Sidor, M, Matias, F, da Silva, Pm, Carvalho, D, Mendonca, I, Andor, M, Andrei, L, Podoleanu, C, Pop, C, Chizhov, P, Chumakova, G, Goloschekin, B, Libov, I, Paltsman, Z, Strutinskiy, A, Koziolova, N, Breedt, J, Ebrahim, I, Ellis, G, Fulat, M, van Rensburg, Dj, Raal, F, van Dyk, C, Vally, T, van der Walt, E, Kotzé, H, Landman, C, Tayob, M, Caixas, A, García, Lr, Fernandez Cruz, A, Gil Extremera, B, Grijalvo, Om, Plana, N, Fuentes, F, Valdivielso, P, Fraile, B, Borgencrantz, B, Larnefeldt, H, Tengmark, Bo, Eriksson, M, Olsson Önerud, Å, Amalyan, W, Dyadyk, O, Koval, O, Kushnir, M, Svintsitskiy, A, Kovalyov, O, Bondarchuk, O, Tashchuk, V, Barna, O, Prokhorov, O, Karpenko, O, Stanciu, D, Pawa, R, Balaji, H, Doig, F, Harvey, P, Ranganath, L, Massalski, W, Hassanin, H, Timmis, H, Pavel Knox, I, Abdulhakim, E, Oyesile, B, Horvathova, V, Donnachie, H, Kondagunta, V, Shaw, H, Thomas, H, Kadr, H, Gunstone, A, Lip, G, Ellery, A, Kerrane, J, Sarker, A, Wong, Yk, Soran, H, Maw, K, Andersen, J, Blair Britt, L, Huffman, C, Kivitz, A, Marple, R, Patron, A, Schear, M, Allegar, N, Awasty, V, Casanova, R, Chaykin, L, Cohen, L, Collins, H, Collins, G, Elkin, G, Reyes, H, Feld, L, Fuller, G, Glover, R, Greenwald, J, Herrod, J, Kaye, W, Kimmel, M, Kolettis, E, Lakin, G, Lorch, D, Palatnik, M, Patel, R, Reichman, A, Rohlf, J, Shockey, G, Shore, K, Radin, D, Alvarado, O, Bellingar, B, Egelhof, R, Mcknight, T, Plevin, S, Pritchard, J, Reddy, R, Velazquez, F, Bolster, E, Broker, R, Butuk, D, Cheung, D, Cohen, K, Golden, G, Murray, A, Naccarato, T, Uusinarkaus, K, Pudi, K, Graff, A, Blumberg, V, Dunn, F, Toth, P, Anspach, R, Chuang, R, Meli, J, Nevins, B, Wayne, J, Schmidt, L, Levinsky, D, Rubino, J, Shealy, N, Torres, D, West, J, Jain, R, Vardi, G, Singh, N, Thew, S, Lo, E, Heitner, J, Gerber, J, Malik, A, Weinstein, D, Prashad, R, Koren, M, Ghitis, A, David, W, Reis, G, Kinzfogl, G, Haught, H, Kantaros, L, O'Dea, D, Weiss, D, Kassas, S, Hunter, J, Mollod, M, Khan, N, Henderson, D, Gatien, L, Schramm, R, Madder, R, Voyce, S, Nadar, V, Stich, M, Kumar, M, Black, R, Treasure, C, Lebeis, M, Mccullough, P, Lepor, N, Moriarty, P, Waxler, A, Talreja, D, Gen, M, Dohad, S, East, C, Conrad, G, Asbill, B, Roberts, J, Robinson, J, Zarich, S, Davis, B, Krolick, M, Sherman, H, Thompson, P., RUBBA, PAOLO OSVALDO FEDERICO, Robinson, Jg, Farnier, M, Krempf, M, Bergeron, J, Luc, G, Averna, M, Stroes, E, Langslet, G, Raal, Fj, El Shahawy, M, Koren, Mj, Lepor, Ne, Lorenzato, C, Pordy, R, Chaudhari, U, Kastelein, Jj, Caccavo, A, Codutti, O, Gelersztein, E, Vico, M, Zaidman, C, Majul, C, Balthazar, Y, Capiau, L, Vrolix, M, Vermeersch, P, Gotchev, D, Todorov, G, Tumbev, H, Tzekova, M, Gronkova, N, Dimov, B, Nikolaeva, A, Devedzhiev, T, Mincheva, V, D'Ignazio, G, Dzongowski, P, Elliott, T, Hart, R, Hoag, G, Martinho, V, O'Mahony, M, Tellier, G, Pandey, S, Heaton, K, Constance, C, Phaneuf, Dc, Shu, D, Narvaez, Nc, Cañon, Co, Cardenas, Sp, Loayza, M, de Salazar, Dm, Lopez, Rb, Gomez, Ji, Mendoza, Ja, Cure, Cc, Ceska, R, Zidkova, E, Jansky, P, Egstrup, K, Klausen, Ib, Lomholdt, J, Gislason, G, Torp Pedersen, C, Poulsen, S, Kuusela, M, Kekki, S, Nieminen, S, Tuomilehto, J, Boye, A, Bruckert, E, Cadinot, D, Lejay, D, Revol, T, Schaupp, T, Bonnet, J, Paillard, F, Moulin, P, Junggeburth, J, Isermann, B, Zühlke, M, Züchner, D, Theis, E, Stößel, J, König, Hj, Rinke, A, Piechatzek, R, Contzen, C, Lappo, M, Himpel Boenninghoff, Aa, Meissner, G, Maus, O, Degtyareva, E, Schulze, Ed, Horacek, T, Marten, I, Becher, P, Matoltsy, A, Nyirati, G, Paragh, G, Zilahi, Z, Nagy, K, Kanakaridisz, N, Beke, E, Biro, J, Schnabel, R, Elias, M, Gavish, D, Francis, A, Nseir, W, Zimlichman, R, Pozzi, C, Lembo, G, Bucci, M, Mezzetti, A, Rubba, PAOLO OSVALDO FEDERICO, De Pellegrin, Am, Salvioni, A, De Cesare, N, Briones, Ir, Campos, Pf, Rosas, El, Espinosa, Ev, Salazar, Ma, Ruiz, Ab, Furusho, Lc, Olvera, I, van den Berg, R, Basart, D, Köse, V, Kentgens, S, Peeters, M, Hoogendijk, J, Voors Pette, C, Agous, I, van Kempen, W, Lingan, Gr, Kooy, A, Troquay, R, Herrman, J, Hoivik, H, Norheim, P, Risberg, K, Høivik, Ho, Elle, S, Derezinski, T, Miekus, P, Ogorek, M, Szymkowiak, K, Cesar, M, Gawron, A, Dabrowska, M, Blach, E, Konieczny, M, Sidor, M, Matias, F, da Silva, Pm, Carvalho, D, Mendonca, I, Andor, M, Andrei, L, Podoleanu, C, Pop, C, Chizhov, P, Chumakova, G, Goloschekin, B, Libov, I, Paltsman, Z, Strutinskiy, A, Koziolova, N, Breedt, J, Ebrahim, I, Ellis, G, Fulat, M, van Rensburg, Dj, Raal, F, van Dyk, C, Vally, T, van der Walt, E, Kotzé, H, Landman, C, Tayob, M, Caixas, A, García, Lr, Fernandez Cruz, A, Gil Extremera, B, Grijalvo, Om, Plana, N, Fuentes, F, Valdivielso, P, Fraile, B, Borgencrantz, B, Larnefeldt, H, Tengmark, Bo, Eriksson, M, Olsson Önerud, Å, Amalyan, W, Dyadyk, O, Koval, O, Kushnir, M, Svintsitskiy, A, Kovalyov, O, Bondarchuk, O, Tashchuk, V, Barna, O, Prokhorov, O, Karpenko, O, Stanciu, D, Pawa, R, Balaji, H, Doig, F, Harvey, P, Ranganath, L, Massalski, W, Hassanin, H, Timmis, H, Pavel Knox, I, Abdulhakim, E, Oyesile, B, Horvathova, V, Donnachie, H, Kondagunta, V, Shaw, H, Thomas, H, Kadr, H, Gunstone, A, Lip, G, Ellery, A, Kerrane, J, Sarker, A, Wong, Yk, Soran, H, Maw, K, Andersen, J, Blair Britt, L, Huffman, C, Kivitz, A, Marple, R, Patron, A, Schear, M, Allegar, N, Awasty, V, Casanova, R, Chaykin, L, Cohen, L, Collins, H, Collins, G, Elkin, G, Reyes, H, Feld, L, Fuller, G, Glover, R, Greenwald, J, Herrod, J, Kaye, W, Kimmel, M, Kolettis, E, Lakin, G, Lorch, D, Palatnik, M, Patel, R, Reichman, A, Rohlf, J, Shockey, G, Shore, K, Radin, D, Alvarado, O, Bellingar, B, Egelhof, R, Mcknight, T, Plevin, S, Pritchard, J, Reddy, R, Velazquez, F, Bolster, E, Broker, R, Butuk, D, Cheung, D, Cohen, K, Golden, G, Murray, A, Naccarato, T, Uusinarkaus, K, Pudi, K, Graff, A, Blumberg, V, Dunn, F, Toth, P, Anspach, R, Chuang, R, Meli, J, Nevins, B, Wayne, J, Schmidt, L, Levinsky, D, Rubino, J, Shealy, N, Torres, D, West, J, Jain, R, Vardi, G, Singh, N, Thew, S, Lo, E, Heitner, J, Gerber, J, Malik, A, Weinstein, D, Prashad, R, Koren, M, Ghitis, A, David, W, Reis, G, Kinzfogl, G, Haught, H, Kantaros, L, O'Dea, D, Weiss, D, Kassas, S, Hunter, J, Mollod, M, Khan, N, Henderson, D, Gatien, L, Schramm, R, Madder, R, Voyce, S, Nadar, V, Stich, M, Kumar, M, Black, R, Treasure, C, Lebeis, M, Mccullough, P, Lepor, N, Moriarty, P, Waxler, A, Talreja, D, Gen, M, Dohad, S, East, C, Conrad, G, Asbill, B, Roberts, J, Robinson, J, Zarich, S, Davis, B, Krolick, M, Sherman, H, and Thompson, P.

Published
2015

5. Review of D-T Results from TFTR

Author

Hawryluk, R.J., primary, Barnes, Cris W., additional, Batha, S., additional, Beer, M., additional, Bell, M.G., additional, Bell, R., additional, Berk, H., additional, Bitter, M., additional, Bretz, N.L., additional, Budny, R., additional, Bush, C.E., additional, Cauffman, S., additional, Chang, C. S., additional, Chang, Z., additional, Cheng, C.Z., additional, Darrow, D.S., additional, Dendy, R., additional, Dorland, W., additional, Dudek, L., additional, Duong, H., additional, Durst, R., additional, Efthimion, P.C., additional, Evenson, H., additional, Fisch, N., additional, Fisher, R., additional, Fonck, R.J., additional, Forrest, C., additional, Fredrickson, E., additional, Fu, G.Y., additional, Furth, H.P., additional, Gorelenkov, N., additional, Grek, B., additional, Grisham, L.R., additional, Hammett, G., additional, Heidbrink, W., additional, Herrmann, H.W., additional, Herrmann, M., additional, Hill, K.W., additional, Hooper, B., additional, Hosea, J., additional, Houlberg, W.A., additional, Hughes, M., additional, Jassby, D.L., additional, Jobes, F.C., additional, Johnson, D.W., additional, Kaita, R., additional, Kamperschroer, J., additional, Kesner, J., additional, Krazilniknov, A., additional, Kugel, H., additional, Kumar, A., additional, LaMarche, P.H., additional, LeBlanc, B., additional, Levine, J., additional, Levinton, F.M., additional, Lin, Z., additional, Machuzak, J., additional, Majeski, R., additional, Mansfield, D.K., additional, Mazzucato, E., additional, Mauel, M., additional, McChesney, J., additional, McGuire, K.M., additional, McKee, G., additional, Meade, D.M., additional, Medley, S.S., additional, Mikkelsen, D.R., additional, Mimov, S.V., additional, Mueller, D., additional, Navratil, G., additional, Nazikian, R., additional, Nevins, B., additional, Okabayashi, M., additional, Osakabe, M., additional, Owens, D.K., additional, Park, H., additional, Park, W., additional, Paul, S.F., additional, Petrov, M., additional, Phillips, C.K., additional, Phillips, M., additional, Phillips, P., additional, Ramsey, A., additional, Redi, M.H., additional, Rewoldt, G., additional, Rice, B., additional, Rogers, J., additional, Roquemore, A.L., additional, Ruskov, E., additional, Sabbagh, S.A., additional, Sasao, M., additional, Schilling, G., additional, Schmidt, G.L., additional, Scott, S.D., additional, Semenov, I., additional, Skinner, C.H., additional, Spong, D., additional, Strachan, J.D., additional, Strait, E.J., additional, Stratton, B.C., additional, Synakowski, E., additional, Takahashi, H., additional, Tang, W., additional, Taylor, G., additional, Goeler, S. von, additional, Halle, A. von, additional, White, R.B., additional, Williams, M.D., additional, Wilson, J.R., additional, Wong, K.L., additional, Wurden, G.A., additional, Young, K.M., additional, Zarnstorff, M.C., additional, and Zweben, S.J., additional

Published
1996
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8. Banana split.

Author

Taylor, N. and Nevins, B.

Subjects
*TRAVEL, SAINT Lucia description & travel
Abstract

Describes the authors' stay on St. Lucia, a relatively undeveloped Caribbean island. Explains why the banana industry can no longer support the island's economy. Impact of the European Economic Community; Coming of development; Les Pitons, twin volcanic peaks; The Cunard Hotel La Toc; History and culture; Castries, the capital city; Soufriere; Diamond Falls; The Maria Islands Nature Reserve. INSET: Right little island (hotels, restaurants, travel information)..

Published
1992

9. Luxury and simplicity.

Author

Geser, G. and Nevins, B.

Subjects
*TRAVEL
Abstract

Gives a description of the accommodations and activities available on Kiawah Island, S.C. Island's history; Golf courses; West Village; East Village; Food and restaurants.

Published
1991

10. Identification of the raland rac1 Gene Products, Low Molecular Mass GTP-binding Proteins from Human Platelets*

Author

Polakis, P G, Weber, R F, Nevins, B, Didsbury, J R, Evans, T, and Snyderman, R

Abstract

Identification of the GTP-binding proteins from human platelet particulate fractions was attained by their purification via successive column chromatography steps followed by amino acid sequencing. To enhance the likelihood of identifying the GTP-binding proteins, two assays were employed to monitor GTP-binding activities: (i) guanosine 5′-(3-O-[35S]thio)triphosphate (GTP γ S)-binding followed by rapid filtration and ii) [α-32P]GTP-binding following sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electroblotting onto nitrocellulose membranes. The latter assay permitted the isolation of a 28-kDa GTP-binding protein that bound [α-32P]GTP prominently but was only poorly detected with the GTP γ S-binding assay. The amino acid sequences of three peptide fragments derived from the 28-kDa protein were identical to regions of the amino acid sequence deduced from a simian ral cDNA with the exception of one conservative substitution (Asp147→Glu). A full length human ralcDNA was isolated from a placental cDNA library, and its deduced amino acid sequence, compared with simian ral, also contained the Asp→Glu substitution along with two other substitutions and an additional three NH2-terminal amino acids. In addition to the 28-kDa protein, two distinct 25-kDa GTP-binding proteins were purified from platelets. One of these proteins has been previously characterized as G25K, an abundant low molecular mass GTP-binding protein. Partial amino acid sequence obtained from the second unidentified 25-kDa protein indicates that it is the product of the rac1 gene; a member of a newly identified gene family which encode for low molecular mass GTP-binding proteins (Didsbury, J., Weber, R.F., Bokoch, G. M., Evans, T., and Snyderman, R. (1989) J. Biol. Chem. 264, 16378-16382). These results identify two new GTP-binding proteins in human platelets, ral, the major protein that binds [α-32P]GTP on nitrocellulose transfers, and rac1, a substrate for botulinum C3 ADP-ribosyltransferase.

Published
1989
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11. Decorsin. A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora

Author

Jl, Seymour, William Henzel, Nevins B, Jt, Stults, and Ra, Lazarus

Subjects
Molecular Sequence Data, Proteins, Enzyme-Linked Immunosorbent Assay, Platelet Membrane Glycoproteins, Chromatography, Affinity, Mass Spectrometry, Molecular Weight, Leeches, Sequence Homology, Nucleic Acid, Animals, Amino Acid Sequence, Saliva, Cell Adhesion Molecules, Chromatography, High Pressure Liquid, Platelet Aggregation Inhibitors
Abstract

The discovery, purification, and characterization of decorsin, a protein isolated from the North American leech Macrobdella decora, are described. Decorsin acts as an antagonist of platelet glycoprotein IIb-IIIa (GPIIb-IIIa), and is a potent inhibitor of platelet aggregation. The protein was purified to apparent homogeneity from crude whole leech extracts by treatment with trifluoroacetic acid followed by GPIIb-IIIa affinity chromatography and C18 reverse-phase high performance liquid chromatography. Decorsin was also isolated from a solution of leech ingestate by treatment with trifluoroacetic acid followed by C18 reverse-phase high performance liquid chromatography. The primary sequence of decorsin indicates that the protein is 39 amino acids long and contains 6 cysteine and 6 proline residues, as well as the sequence Arg-Gly-Asp, (RGD), a proposed recognition site of many adhesion proteins. A molecular mass of 4379 was obtained by fast atom bombardment mass spectrometry and is consistent with the mass calculated from the observed sequence. Evidence for an N-3 isoform, lacking the first 3 amino-terminal residues is also presented. Both decorsin and the N-3 isoform inhibit GP IIb-IIIa binding to immobilized fibrinogen with an IC50 of approximately 1.5 nM. Human platelet aggregation induced by ADP is inhibited by decorsin with an IC50 of approximately 500 nM; complete inhibition was observed at less than or equal to 1 microM. Based on overall sequence homology, decorsin does not belong to the family of GPIIb-IIIa protein antagonists that is found in snake venoms (Dennis, M. S., Henzel, W. J., Pitti, R. M., Lipari, M. T., Napier, M. A., Deisher, T. A., Bunting, S., and Lazarus, R. A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 2471-2475); however the carboxyl-terminal RGD-containing region from residues 27 to 38 of decorsin is approximately 60% homologous with the corresponding region of the snake venom proteins, suggesting that high affinity binding of these proteins to GPIIb-IIIa is defined by this epitope.

13. The street kid and the reporter.

Author

Nevins, B.

Subjects
FOSTER home care
Abstract

Recounts how the author, a television news reporter, ended up becoming a foster mother to a child she met on the street during an assignment.

Published
1991

14. 3 bags full.

Author

Taylor, N. and Nevins, B.

Subjects
*COMMERCIAL products
Abstract

Gives advice on choosing good luggage. Tells how to pack luggage; Hard and soft luggage; Lark Luggage Company; Bags from Tumi; Ballistic fabric; Garment bags; Samsonite's Piggyback Carry-on; Brand names and prices.

Published
1991

15. Rapid Implementation and Adaptation of a Telehospitalist Service to Coordinate and Optimize Care for COVID-19 Patients.

Author

Becker CD, Forman L, Gollapudi L, Nevins B, and Scurlock C

Subjects
Humans, New York City, Pandemics, Prospective Studies, Tertiary Care Centers, COVID-19 therapy, Hospitalists, Patient Care, Telemedicine
Abstract

Background/Introduction: The COVID-19 pandemic poses enormous resource challenges to hospitals. Telemedicine is increasingly recognized as an attractive tool to alleviate resource strains. Herein we describe the rapid implementation and sequential process improvement (PI) of a centralized telehospitalist service to coordinate and optimize management of large number of COVID-19 patients in a tertiary and quaternary care hospital very close to the New York City epicenter. Methods: Prospective multidisciplinary PI meetings were held weekly between March 23 and May 10, 2020, and consensus service modifications were implemented for the following week. Inpatient census data, telehospitalist intervention volumes, and service utilization statistics were collected. Results/Discussion: Between March 23 and May 10, 2020, a total of 745 COVID-19 patients were admitted to the general medical wards. The telehospitalist service performed 1,136 audiovisual (AV) patient assessments, 379 best practice interventions, cohorted 108 patients, and conducted 170 remote family conversations. During the consecutive PI cycles, a number of adaptations in AV setup, care standardization, patient logistics, communication, and consultative functions were made to load balance the bedside hospitalist teams. As the COVID-19 hospital census increased to peak levels, the most value was added through facilitation of communication and collaboration between the bedside clinical teams, the infection prevention and control teams, and patient logistics team. Conclusions: A telehospitalist service can be rapidly implemented with basic telemedicine equipment. Processes/this functions can be sequentially adapted to quickly changing needs during conditions such as the COVID-19 pandemic that very quickly can place extraordinary strains on hospital resources.

Published
2021
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16. Affinity purification and sequence determination of equine relaxin.

Author

Stewart DR, Nevins B, Hadas E, and Vandlen R

Subjects
Amino Acid Sequence, Animals, Antibodies, Monoclonal, Chromatography, Affinity, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Female, Immunologic Techniques, Molecular Sequence Data, Pregnancy, Relaxin chemistry, Horses, Placenta chemistry, Relaxin isolation & purification
Abstract

Relaxin, a polypeptide hormone normally associated with pregnancy, has been purified from many species, and the sequence determined for a growing number. Equine relaxin has been previously purified by acetone extraction, gel filtration, and ion exchange chromatographies. In an attempt to develop a more rapid and efficient method for relaxin purification, the use of affinity chromatography coupled with HPLC was explored. Monoclonal antibodies were raised against highly purified equine relaxin; large quantities of antibody were obtained by ascites production and attached to a solid phase support. An extract of term equine placentas was passed through the affinity column and washed, and relaxin was eluted by a change in pH. The isoforms of equine relaxin were separated by HPLC using a C18 (ODS) reverse phase column and a linear gradient of 25-30% acetonitrile. Four major and several minor isoforms of equine relaxin were obtained. The isoforms share similar mol wt by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), are composed of subunits (SDS-PAGE under reducing conditions), and have similar charges (native PAGE). Five isoforms tested positive for biological activity in the mouse interpubic ligament bioassay. Equine relaxin was sequenced by Edman degradation, and the sequence was confirmed by fast atom bombardment mass spectrometry. The isoforms of equine relaxin were found to be due to heterogeneity of the C-terminus of the B-chain. Equine relaxin appears to be the smallest relaxin sequenced. The A-chain consists of 20 residues, and the B-chain has 28 residues, with a total mol wt of 5253. Equine relaxin shares the greatest sequence homology with porcine relaxin (67% identity).

Published
1991
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17. Soluble and membrane-associated human low-affinity adenosine binding protein (adenotin): properties and homology with mammalian and avian stress proteins.

Author

Hutchison KA, Nevins B, Perini F, and Fox IH

Subjects
Amino Acid Sequence, Animals, Binding, Competitive, Birds, Carbohydrates analysis, Carrier Proteins genetics, Cell Membrane metabolism, Cricetinae, Heat-Shock Proteins genetics, Humans, Molecular Sequence Data, Molecular Weight, Placenta analysis, Sequence Homology, Nucleic Acid, Solubility, Carrier Proteins metabolism, Heat-Shock Proteins metabolism
Abstract

A low-affinity adenosine binding protein has recently been distinguished from the adenosine A2 receptor and purified from human placental membranes. Soluble human placental extracts contain an adenosine binding activity that has properties similar to those of the membrane low-affinity adenosine binding protein. The binding protein was purified from soluble human placental extracts 134-fold to 89% purity with a Bmax of 2.5 nmol/mg. It comprises 0.7-0.9% of the soluble protein. The major purified soluble protein has a subunit molecular mass of 98 kDa and a Stokes radius identical with that of the membrane-bound adenosine binding protein. Competition analysis of the soluble protein revealed similar affinities and an identical potency order for displacement of 5'-(N-ethylcarbamoyl)[2,8-3H]adenosine ([3H]NECA) as follows: NECA greater than 2-chloroadenosine greater than adenosine greater than (R)-N6-(2-phenylisopropyl)adenosine. The soluble binding protein was more acidic than the membrane binding protein as revealed by a comparison of the elution properties during ion exchange chromatography. A second form of soluble adenosine binding activity comprised 17% of the major form and had a charge similar to that of the membrane binding protein, a smaller Stokes radius, and a subunit molecular mass of 74 kDa. Carbohydrate composition analysis revealed that the major soluble form has 4.3% carbohydrate by weight as compared to the membrane-associated form, which has 5.5% carbohydrate by weight.(ABSTRACT TRUNCATED AT 250 WORDS)

Published
1990
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18. Preglomerular resistance and glomerular perfusion in the rat and dog.

Author

Chenitz WR, Nevins BA, and Hollenberg NK

Subjects
Animals, Body Weight, Cardiac Output, Microspheres, Regional Blood Flow, Vascular Resistance, Dogs physiology, Kidney Glomerulus blood supply, Rats physiology
Abstract

Glomerular blood flow in the rat, measured with radioactive microspheres, averaged 233 +/- 59 nl/min per glomerulus, significantly less than the glomerular flow rate in the dog (568 +/- 115; P less than 0.005). The difference in glomerular blood flow rate could not be attributed to differences in mean or cortical flow rates, the fraction of acrdiac output received, cardiac output normalized to body weight, or the fractional distribution of blood flow or glomeruli from outer to inner cortex in the two species. The size of microspheres reaching the glomerulus, however, was significantly larger in the dog than in the rat (P less than 0.0005) suggesting that afferent arterioles were larger in the dog than rat. The difference in afferent resistance calculated from the size of microspheres delivered to the glomeruli was larger than the difference in glomerular blood flow. With a similar arterial pressure, a lower afferent resistance suggests a higher glomerular capillary pressure in the dog, consistent with a number of suggestions that filtration equilibrium is less likely in this species.

Published
1976
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