Zobrazeno 1 - 10
of 68
pro vyhledávání: '"Miriam Gochin"'
Autor:
Li He, Guangyan Zhou, Vladimir Sofiyev, Eddie Garcia, Newton Nguyen, Kathy H. Li, Miriam Gochin
Publikováno v:
Viruses, Vol 14, Iss 12, p 2703 (2022)
Human Immunodeficiency virus (HIV-1) fusion is mediated by glycoprotein-41, a protein that has not been widely exploited as a drug target. Small molecules directed at the gp41 ectodomain have proved to be poorly drug-like, having moderate efficacy, h
Externí odkaz:
https://doaj.org/article/5065a82cb7664402b470a0fa6f5244e5
Publikováno v:
Chem Commun (Camb)
We describe a low molecular weight covalent inhibitor targeting a conserved lysine residue within the hydrophobic pocket of HIV-1 glycoprotein-41. The inhibitor bound selectively to the hydrophobic pocket and exhibited an order of magnitude enhanceme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8741a79876866ebd2b3293172603ff1
https://doi.org/10.1039/d1cc01013a
https://doi.org/10.1039/d1cc01013a
Autor:
Ariana Nemati, Shidong Chu, Guangyan Zhou, Roger G. Ptak, Beth A. Snyder, Miriam Gochin, Chunsheng Huang
Publikováno v:
European Journal of Medicinal Chemistry. 161:533-542
In previous work, we described 6–6’-bisindole compounds targeting a hydrophobic pocket on the N-heptad repeat region of viral glycoprotein-41 as effective inhibitors of HIV-1 fusion. Two promising compounds with sub-micromolar IC(50)’s containe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d969d2672eb585471be5a7ae463525d
https://doi.org/10.1016/j.ejmech.2018.10.048
https://doi.org/10.1016/j.ejmech.2018.10.048
Publikováno v:
Organic & Biomolecular Chemistry. 15:5210-5219
Small molecule inhibitors of glycoprotein-41 (gp41) are able to prevent HIV infection by binding to a hydrophobic pocket (HP) contained within the gp41 ectodomain, and preventing progression of fusion. There is little structural information on gp41
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9fad0f237aa13bb26c27c6b02b9899d
https://doi.org/10.1039/c7ob00954b
https://doi.org/10.1039/c7ob00954b
Autor:
Peter H. Hwang, Hardeep Kaur, Miriam Gochin, Beth A. Snyder, Priscilla A. Hogan, Roger G. Ptak, Vladimir Sofiyev
Publikováno v:
Bioorganic & Medicinal Chemistry. 25:408-420
Low molecular weight peptidomimetic inhibitors with hydrophobic pocket binding properties and moderate fusion inhibitory activity against HIV-1 gp41-mediated cell fusion were elaborated by increasing the available surface area for interacting with th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::034d0b476ddeb0795d0fae36b274a36f
https://doi.org/10.1016/j.bmc.2016.11.010
https://doi.org/10.1016/j.bmc.2016.11.010
Publikováno v:
Biochim Biophys Acta Gen Subj
Background The hydrophobic pocket (HP) of HIV-1 glycoprotein-41 ectodomain is defined by two chains of the N-heptad repeat trimer, within the protein-protein interface that mediates 6HB formation. It is a potential target for inhibitors of viral fusi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93bec85cde95bd608025465e6b464dee
https://doi.org/10.1016/j.bbagen.2020.129724
https://doi.org/10.1016/j.bbagen.2020.129724
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 25:2853-2859
Identification of mechanistically novel anti-HIV fusion inhibitors was accomplished using a computer-aided structure-based design approach with the goal of blocking the formation of the N-heptad repeat (NHR) trimer of the viral protein gp41. A virtua
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de3cf05e750a4e00a0582198afd7f8ae
https://doi.org/10.1016/j.bmcl.2015.04.067
https://doi.org/10.1016/j.bmcl.2015.04.067
Publikováno v:
Protein Engineering, Design and Selection. 28:107-116
Four new swapped-domain constructs of the ectodomain of human immunodeficiency virus type 1 glycoprotein-41 (gp41) were prepared. The gp41 ectodomain consists of 50-residue N-heptad repeat (NHR), 36-residue disulfide-bonded loop and 39-residue C-hept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae9beb14ba3acea9f6dad46fedd598b0
https://doi.org/10.1093/protein/gzv006
https://doi.org/10.1093/protein/gzv006
Autor:
Shao-Qing Zhang, Hardeep Kaur, Shidong Chu, Miriam Gochin, Vivian Partida, Joseph D. Walsh, Ariana Nemati
Publikováno v:
ACS Chemical Biology. 10:1247-1257
The conformational rearrangement of N- and C-heptad repeats (NHR, CHR) of the HIV-1 glycoprotein-41 (gp41) ectodomain into a trimer of hairpins triggers virus-cell fusion by bringing together membrane-spanning N- and C-terminal domains. Peptides deri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d76e0fa4b47ac9cd53b117949a93b445
https://doi.org/10.1021/cb501021j
https://doi.org/10.1021/cb501021j
Autor:
Miriam Gochin
Publikováno v:
ASSAY and Drug Development Technologies. 10:407-416
Several different segments of the gp41 N-heptad repeat coiled coil have been constructed using N-terminal bipyridyl modification of composite peptides and inducing trimerization by adding ferrous ions. These metallopeptides act as receptors in fluore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c7b32d5568cbd003d7cb2cd6f698ac6
https://doi.org/10.1089/adt.2012.464
https://doi.org/10.1089/adt.2012.464