Abstracts of the XVIII European Conference on Muscle and Motility

Autor: V. P. Nesterov, U. Peiper, J. Hiller, B. Krienke, K. Schüttler, C. Szymanski, R. Bottinelli, V. Cappelli, R. Minelli, C. Reggiani, S. Schiaffino, D. Carlhoff, J. D'Haese, R. Dabrowska, E. Nowak, Y. S. Borovikov, P. Cummins, G. Russell, D. McLoughlin, B. Cummins, A. Bonet, M. C. Harricane, E. Audemard, D. Mornet, S. Ropert, F. Cavaillé, C. S. Redwood, J. Bryan, R. A. Cross, J. Kendrick-Jones, S. B. Marston, M. Taggart, S. Marston, R. Makuch, G. Stokarska, G. Cecchi, F. Colomo, C. Poggesi, C. Tesi, M. Puceat, O. Clement, P. Lechene, J. -M. Pelosin, R. Ventura-Clapter, G. Vassort, W. Fischer, G. Pfitzer, R. J. Ankrett, A. J. Rowe, C. R. Bagshaw, S. V. Perry, S. Hebisch, B. Levine, A. J. G. Moir, J. Leszyk, J. Derancourt, V. Patcheil, C. Cavadore, J. H. Collins, K. Swiderek, K. Jaquet, K. Mittmann, H. E. Meyer, L. M. J. Heilmeyer, F. Travers, T. Barman, M. Duvert, X. Grandier-Vazeille, A. Verna, M. Dan-Goor, A. Mühlrad, A. Muhlrad, B. Polzar, P. Kießling, H. G. Mannherz, S. Lehmann-Klose, U. Gröschel-Stewart, N. Bettache, R. Bertrand, R. Kassab, A. Roulet, R. Cardinaud, J. J. Harford, J. M. Squire, Y. Maeda, M. W. K. Chew, Pia Huber, Marcus C. Schaub, S. Pierobon-Bormioli, R. Betto, S. Ceoldo, G. Salviati, I. Martinez, R. Ofstad, R. L. Olsen, J. Trinick, D. Barlow, M. Gautel, T. Gibson, S. Labeit, K. Leonard, J. Wardale, A. Whiting, A. Draeger, M. Barth, M. Herzog, M. Gimona, J. V. Small, E. Stelzer, B. Amos, M. Ikebe, J. C. Bernengo, Bettina Rinne, John S. Wray, K. J. V. Poole, R. S. Goody, Daniel Thomas, Arthur Rowe, R. R. Schröder, W. Hofmann, U. C. Müller, J. -F. Menetret, J. S. Wray, A. Lakey, W. Tichelaar, C. Ferguson, B. Bullard, W. Kabsch, E. F. Pai, D. Suck, K. C. Holmes, Robert Jarosch, R. van Mastrigt, Gerald H. Pollack, Arie Horowitz, R. Anderl, H. J. Kuhn, K. Burton, D. W. G. Jung, T. Blangé, B. W. Treijtel, M. A. Bagni, P. Garzella, A. F. Huxley, G. Beckers-Bleukx, G. Maréchal, S. Y. Bershitsky, A. K. Tsaturyan, S. K. A. Woodward, J. F. Eccleston, M. A. Geeves, Peter Knight, Neil Fortune, Mike Geeves, A. Arner, H. Arheden, V. Lombardi, G. Piazzesi, G. J. M. Stienen, G. Elzinga, E. L. de Beer, K. J. H. van Buuren, Y. J. ten Kate, R. L. F. Grundeman, P. Schiereck, K. Trombitas, P. G. A. Versteeg, Arthur J. Rowe, Paul Bolger, W. J. van der Laarse, P. C. Diegenbach, F. W. Flitney, D. A. Jones, S. Hatfaludy, J. Shansky, B. Smiley, H. H. Vandenburgh, A. de Haan, M. A. N. Lodder, A. Berquin, J. Lebacq, N. A. Curtin, R. C. Woledge, P. Hellstrand, P. Lönnbro, I. Wadsö, T. S. Lammertse, R. Zaremba, J. Daut, M. J. Kushmerick, E. McFarland, G. E. Lyons, D. Sassoon, M. Ontell, M. E. Buckingham

Publikováno v: Journal of Muscle Research & Cell Motility. 11:56-78

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2ecf46487b6ce71ab7f7822aad4a6048
https://doi.org/10.1007/bf01833326

Fluorescence methods for monitoring interactions of Rab proteins with nucleotides, Rab escort protein, and geranylgeranyltransferase

Autor: K, Alexandrov, A J, Scheidig, R S, Goody

Publikováno v: Methods in enzymology. 329

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ac2448c740798352bfc5e1f559b14804
https://pubmed.ncbi.nlm.nih.gov/11210530

Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP

Autor: N, Ostermann, A, Lavie, S, Padiyar, R, Brundiers, T, Veit, J, Reinstein, R S, Goody, M, Konrad, I, Schlichting

Publikováno v: Journal of molecular biology. 304(1)

The 60-fold reduced phosphorylation rate of azidothymidine (AZT) monophosphate (AZTMP), the partially activated AZT metabolite, by human thymidylate kinase (TMPK) severely limits the efficacy of this anti-HIV prodrug. Crystal structures of different

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4ce04e7cb7fe33c210e4be160be111f5
https://pubmed.ncbi.nlm.nih.gov/11071809

A new potent HIV-1 reverse transcriptase inhibitor. A synthetic peptide derived from the interface subunit domains

Autor: M C, Morris, V, Robert-Hebmann, L, Chaloin, J, Mery, F, Heitz, C, Devaux, R S, Goody, G, Divita

Publikováno v: The Journal of biological chemistry. 274(35)

The biologically relevant and active forms of human immunodeficiency viruses type 1 and 2 reverse transcriptase found in infectious virions are heterodimers produced in a two-step dimerization process. Dimerization involves first the rapid associatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6303d6f06e3c5e904e180bbddc9f350b
https://pubmed.ncbi.nlm.nih.gov/31075755

Equine infectious anemia virus transactivator is a homeodomain-type protein

Autor: D, Willbold, A U, Metzger, H, Sticht, K C, Gallert, R, Voit, N, Dank, P, Bayer, G, Krauss, R S, Goody, P, Rösch

Publikováno v: Journal of molecular biology. 277(4)

Lentiviral transactivator (Tat) proteins are essential for viral replication. Tat proteins of human immunodeficiency virus type 1 and bovine immunodeficiency virus form complexes with their respective RNA targets (Tat responsive element, TAR), and sp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fb7a9c1c9645f1d391bc28028f166016
https://pubmed.ncbi.nlm.nih.gov/9545368