Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Deborah S. Dauber"'
Autor:
Nicholas F. Endres, Charles S. Craik, Deborah S. Dauber, Robert M. Stroud, K. Kinkead Reiling
Publikováno v:
Biochemistry. 41:4582-4594
The structure of HIV protease (HIV Pr) bound to JE-2147 (also named AG1776 or KNI-764) is determined here to 1.09 A resolution. This highest-resolution structure for HIV Pr allows refinement of anisotropic displacement parameters (ADPs) for all atoms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1860fde10b6e6b5d5e8c1bf19e3d13d7
https://doi.org/10.1021/bi011781z
https://doi.org/10.1021/bi011781z
Publikováno v:
Journal of Biological Chemistry. 275:7080-7086
Defective variants of human immunodeficiency virus type 1 (HIV-1) protease (HIV PR) have been engineered to inhibit wild-type (wt) HIV PR activity. These variants were designed to promote the formation of heterodimers and to destabilize the formation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5e305e3ce691f5ad47a1dee830921ba6
https://doi.org/10.1074/jbc.275.10.7080
https://doi.org/10.1074/jbc.275.10.7080
Autor:
Deborah S. Dauber, Jonathan A. Ellman, Francesco Leonetti, Dustin J. Maly, Charles S. Craik, Jennifer L. Harris, Bradley J. Backes
Publikováno v:
The Journal of organic chemistry. 67(3)
A highly efficient solid-phase synthesis method for the preparation of fluorogenic protease substrates based upon the bifunctional leaving group 7-amino-4-carbamoylmethylcoumarin (ACC) is reported. Methods for the large-scale preparation of the novel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60e0de531baf0a73ecc77d518600bffb
https://pubmed.ncbi.nlm.nih.gov/11856036
https://pubmed.ncbi.nlm.nih.gov/11856036
Autor:
Sami Mahrus, Rainer Ziermann, Dustin J. Maly, Deborah S. Dauber, Jennifer L. Harris, Neil Parkin, Christos J. Petropoulos, Jon A. Ellman, Charles S. Craik
Publikováno v:
Journal of virology. 76(3)
Resistance to human immunodeficiency virus type 1 protease (HIV PR) inhibitors results primarily from the selection of multiple mutations in the protease region. Because many of these mutations are selected for the ability to decrease inhibitor bindi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2cd2e1d4f6f7edaad40a50718956b9f
https://pubmed.ncbi.nlm.nih.gov/11773410
https://pubmed.ncbi.nlm.nih.gov/11773410
Publikováno v:
Aspartic Proteinases ISBN: 9781461374527
The protease encoded in the HIV-1 genome plays a crucial role in the life cycle of the virus, cleaving the p55 gag and p160 gag-pol precursors into their mature and functional forms Since either genetic inactivation or chemical inhibition of the prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a4dd8aa95b4caacd6b5df11bae716fd9
https://doi.org/10.1007/978-1-4615-5373-1_4
https://doi.org/10.1007/978-1-4615-5373-1_4
Publikováno v:
Aspartic Proteinases ISBN: 9781461374527
HIV protease (HIV PR) has been identified as a key target in the treatment of HIV infection, and antiviral drugs that block its proteolytic activity have been developed. However, there are numerous ways in which a drug can lose effectiveness during l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd9b16ca826387e3ca135226a62f36b9
https://doi.org/10.1007/978-1-4615-5373-1_9
https://doi.org/10.1007/978-1-4615-5373-1_9