Zobrazeno 1 - 7
of 7
pro vyhledávání: '"H L, Robbins"'
Autor:
J C Hastings, Robert L. Lafemina, Abigail Wolfe, Pia L. Graham, Emilio A. Emini, Daria J. Hazuda, H L Robbins
Publikováno v:
Journal of Biological Chemistry. 269:3999-4004
A DNA binding assay was developed for the human immunodeficiency virus type 1 (HIV-1) integrase. The assay was capable of defining discrete complexes between the enzyme and the viral long terminal repeat (LTR) substrate. DNA binding reflected the seq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::526a554cd34633ec28fc83569f5724d2
https://doi.org/10.1016/s0021-9258(17)41733-9
https://doi.org/10.1016/s0021-9258(17)41733-9
Autor:
A S Zeft, Mark W. Bruner, Gautam Sanyal, James A. Ryan, H L Robbins, C R Middaugh, C J Burke, Robert L. Lafemina, M G Cordingley
Publikováno v:
Journal of Biological Chemistry. 267:9639-9644
The N-terminal domain of human immunodeficiency virus (HIV-1) integrase (IN) contains the sequence motif His-Xaa3-His-Xaa23-Cys-Xaa2-Cys, which is strongly conserved in all retroviral and retrotransposon IN proteins. This structural motif constitutes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8b35d979b679b0461c64bc40faf2660a
https://doi.org/10.1016/s0021-9258(19)50138-7
https://doi.org/10.1016/s0021-9258(19)50138-7
Autor:
Lori J. Gabryelski, H L Robbins, D Laird, Donald J. Graham, R T Steigbigel, Daniel J. Holder, J A Chodakewitz, Malathi Shivaprakash, O M Blahy, F. E. Massari, Jon H. Condra, Robert M. Danovich, T Yang, Elizabeth Roth, Quintero Julio C, A Rhodes, William A. Schleif, Emilio A. Emini, K E Squires, Deutsch Paul J, Randi Y. Leavitt, J W Mellors, Hedy Teppler
Indinavir (IDV) (also called CRIXIVAN, MK-639, or L-735,524) is a potent and selective inhibitor of the human immunodeficiency virus type 1 (HIV-1) protease. During early clinical trials, in which patients initiated therapy with suboptimal dosages of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b7b97919b851dd2170bcead88bfc7e3
https://europepmc.org/articles/PMC190914/
https://europepmc.org/articles/PMC190914/
Publikováno v:
The Journal of biological chemistry. 269(6)
A DNA binding assay was developed for the human immunodeficiency virus type 1 (HIV-1) integrase. The assay was capable of defining discrete complexes between the enzyme and the viral long terminal repeat (LTR) substrate. DNA binding reflected the seq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5167974e15e7358498a5dae115a39c7c
https://pubmed.ncbi.nlm.nih.gov/8307956
https://pubmed.ncbi.nlm.nih.gov/8307956
Autor:
P L Callahan, K LeGrow, R L LaFemina, William A. Schleif, Emilio A. Emini, C L Schneider, Elizabeth Roth, H L Robbins
The human immunodeficiency virus type 1 (HIV-1) integrase enzyme exhibits significant amino acid sequence conservation with integrase proteins of other retroviruses. We introduced specific amino acid substitutions at a number of the conserved residue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a610463f1a14a8ef4011fbc83d620f4e
https://europepmc.org/articles/PMC240448/
https://europepmc.org/articles/PMC240448/
Autor:
C J, Burke, G, Sanyal, M W, Bruner, J A, Ryan, R L, LaFemina, H L, Robbins, A S, Zeft, C R, Middaugh, M G, Cordingley
Publikováno v:
The Journal of biological chemistry. 267(14)
The N-terminal domain of human immunodeficiency virus (HIV-1) integrase (IN) contains the sequence motif His-Xaa3-His-Xaa23-Cys-Xaa2-Cys, which is strongly conserved in all retroviral and retrotransposon IN proteins. This structural motif constitutes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::39abbc976e0b11f1d55167315c840a75
https://pubmed.ncbi.nlm.nih.gov/1577801
https://pubmed.ncbi.nlm.nih.gov/1577801
Publikováno v:
Academic Medicine. 46:1074-9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0baf9fd0c58e6c9b9246f7a132d09994
https://doi.org/10.1097/00001888-197112000-00008
https://doi.org/10.1097/00001888-197112000-00008