Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Hanumant S. Tanwar"'
Autor:
Hanumant S Tanwar, Keith K Khoo, Megan Garvey, Lynne Waddington, Andrew Leis, Marcel Hijnen, Tony Velkov, Geoff J Dumsday, William J McKinstry, Johnson Mak
Publikováno v:
PLoS Pathogens, Vol 13, Iss 2, p e1006221 (2017)
The interactions that occur during HIV Pr55Gag oligomerization and genomic RNA packaging are essential elements that facilitate HIV assembly. However, mechanistic details of these interactions are not clearly defined. Here, we overcome previous limit
Externí odkaz:
https://doaj.org/article/958df98a5bb8424bb081bb2b7192b201
Autor:
Johnson Mak, Marcel Hijnen, Sureshbabu Nagarajan, Hanumant S. Tanwar, William J. McKinstry, Lindsay G. Sparrow, Son T. Pham
Publikováno v:
Protein Expression and Purification. 100:10-18
The HIV-1 Gag precursor protein, Pr55(Gag), is a multi-domain polyprotein that drives HIV-1 assembly. The morphological features of HIV-1 suggested Pr55(Gag) assumes a variety of different conformations during virion assembly and maturation, yet stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f1a4e74b6617d921cb34f9a08d5ca25
https://doi.org/10.1016/j.pep.2014.04.013
https://doi.org/10.1016/j.pep.2014.04.013
Autor:
Naresh, Yandrapalli, Quentin, Lubart, Hanumant S, Tanwar, Catherine, Picart, Johnson, Mak, Delphine, Muriaux, Cyril, Favard
Publikováno v:
Scientific Reports
The self-assembly of HIV-1 Gag polyprotein at the inner leaflet of the cell host plasma membrane is the key orchestrator of virus assembly. The binding between Gag and the plasma membrane is mediated by specific interaction of the Gag matrix domain a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ae163f8442aa03c84aa71e6d5415f6cc
https://pubmed.ncbi.nlm.nih.gov/28008947
https://pubmed.ncbi.nlm.nih.gov/28008947
Autor:
Cyril Favard, Hanumant S. Tanwar, Catherine Picart, Delphine Muriaux, Quentin Lubart, Johnson Mak, Naresh Yandrapalli
Publikováno v:
Scientific Reports
Scientific Reports, Nature Publishing Group, 2016, 6, ⟨10.1038/srep39332⟩
Scientific Reports, Nature Publishing Group, 2016, 6 (1), ⟨10.1038/srep39332⟩
Scientific Reports, Nature Publishing Group, 2016, 6, pp.39332. ⟨10.1038/srep39332⟩
Scientific Reports, 2016, 6, pp.39332. ⟨10.1038/srep39332⟩
Scientific Reports, Nature Publishing Group, 2016, 6, ⟨10.1038/srep39332⟩
Scientific Reports, Nature Publishing Group, 2016, 6 (1), ⟨10.1038/srep39332⟩
Scientific Reports, Nature Publishing Group, 2016, 6, pp.39332. ⟨10.1038/srep39332⟩
Scientific Reports, 2016, 6, pp.39332. ⟨10.1038/srep39332⟩
The self-assembly of HIV-1 Gag polyprotein at the inner leaflet of the cell host plasma membrane is the key orchestrator of virus assembly. The binding between Gag and the plasma membrane is mediated by specific interaction of the Gag matrix domain a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9101d7acc3fef7247c50c45c0efb5a37
https://hal.archives-ouvertes.fr/hal-01465578
https://hal.archives-ouvertes.fr/hal-01465578
