Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Susan M. Watanabe"'
Autor:
Susan M. Watanabe, David A. Nyenhuis, Mahfuz Khan, Lorna S. Ehrlich, Irene Ischenko, Michael D. Powell, Nico Tjandra, Carol A. Carter
Publikováno v:
Viruses, Vol 16, Iss 10, p 1566 (2024)
Tsg101, a component of the endosomal sorting complex required for transport (ESCRT), is responsible for recognition of events requiring the machinery, as signaled by cargo tagging with ubiquitin (Ub), and for recruitment of downstream acting subunits
Externí odkaz:
https://doaj.org/article/ef7af3353cf84ebe87004a4b3dd69d12
Publikováno v:
Viruses, Vol 13, Iss 6, p 1147 (2021)
Two decades ago, Tsg101, a component of the Endosomal Sorting Complexes Required for Transport (ESCRT) complex 1, was identified as a cellular factor recruited by the human immunodeficiency virus type 1 (HIV-1) to facilitate budding of viral particle
Externí odkaz:
https://doaj.org/article/5c181bb7926643de842a6fda8687ad90
Publikováno v:
Viruses, Vol 12, Iss 4, p 447 (2020)
The ESCRT-I factor Tsg101 is essential for sorting endocytic cargo and is exploited by viral pathogens to facilitate egress from cells. Both the nucleocapsid (NC) domain and p6 domain in HIV-1 Gag contribute to recruitment of the protein. However, th
Externí odkaz:
https://doaj.org/article/e07e2a9aa43c4f4382c93deb62d81496
Autor:
Jiri Vlach, Carol A. Carter, Gunnar N. Eastep, Jamil S. Saad, Ruba H. Ghanam, Gisselle N. Medina, Susan M. Watanabe
Publikováno v:
Journal of Biological Chemistry. 293:18841-18853
The Gag protein of avian sarcoma virus (ASV) lacks an N-myristoyl (myr) group, but contains structural domains similar to those of HIV-1 Gag. Similarly to HIV-1, ASV Gag accumulates on the plasma membrane (PM) before egress; however, it is unclear wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84236e7299f25ef6af5c5b244652b444
https://doi.org/10.1074/jbc.ra118.003947
https://doi.org/10.1074/jbc.ra118.003947
Publikováno v:
Viruses, Vol 13, Iss 1147, p 1147 (2021)
Viruses
Viruses
Two decades ago, Tsg101, a component of the Endosomal Sorting Complexes Required for Transport (ESCRT) complex 1, was identified as a cellular factor recruited by the human immunodeficiency virus type 1 (HIV-1) to facilitate budding of viral particle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e1458601147b63b6d1095c99013c3ac
https://pubmed.ncbi.nlm.nih.gov/34203832
https://pubmed.ncbi.nlm.nih.gov/34203832
Publikováno v:
Viruses
Volume 12
Issue 4
Viruses, Vol 12, Iss 447, p 447 (2020)
Volume 12
Issue 4
Viruses, Vol 12, Iss 447, p 447 (2020)
The ESCRT-I factor Tsg101 is essential for sorting endocytic cargo and is exploited by viral pathogens to facilitate egress from cells. Both the nucleocapsid (NC) domain and p6 domain in HIV-1 Gag contribute to recruitment of the protein. However, th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::498d1e586d4e24a68f2508e016bbfc0d
https://pubmed.ncbi.nlm.nih.gov/32326417
https://pubmed.ncbi.nlm.nih.gov/32326417
Autor:
Veronica Soloveva, Arthur J. Goff, Xiaofan Li, Lorna S. Ehrlich, Nico Tjandra, Charles B. Stauft, Madeleine Strickland, Carol A. Carter, Sumita Bhaduri-McIntosh, Susan M. Watanabe
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-15 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-15 (2020)
Two proton pump inhibitors, tenatoprazole and esomeprazole, were previously shown to inhibit HIV-1 egress by blocking the interaction between Tsg101, a member of the ESCRT-I complex, and ubiquitin. Here, we deepen our understanding of prazole budding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccd41ee608ca5bf199afca18345df204
http://europepmc.org/articles/PMC7055211
http://europepmc.org/articles/PMC7055211
Autor:
Ruba H. Ghanam, Gunnar N. Eastep, Jamil S. Saad, Carol A. Carter, Jiri Vlach, Susan M. Watanabe
Publikováno v:
The Journal of biological chemistry. 293(49)
For most retroviruses, including HIV-1, binding of the Gag polyprotein to the plasma membrane (PM) is mediated by interactions between Gag's N-terminal myristoylated matrix (MA) domain and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)) in the PM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbceb77055af8cdd8a8ad7e60591d559
https://pubmed.ncbi.nlm.nih.gov/30309983
https://pubmed.ncbi.nlm.nih.gov/30309983
Autor:
Susan M, Watanabe, Gisselle N, Medina, Gunnar N, Eastep, Ruba H, Ghanam, Jiri, Vlach, Jamil S, Saad, Carol A, Carter
Publikováno v:
The Journal of biological chemistry. 293(49)
The Gag protein of avian sarcoma virus (ASV) lacks an N-myristoyl (myr) group, but contains structural domains similar to those of HIV-1 Gag. Similarly to HIV-1, ASV Gag accumulates on the plasma membrane (PM) before egress; however, it is unclear wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::470fb5e8b17ff9a113fcb4a22f1a2ab0
https://pubmed.ncbi.nlm.nih.gov/30309982
https://pubmed.ncbi.nlm.nih.gov/30309982
Autor:
Jordan T. Speidel, Liangqun Huang, ChihFeng Tien, Carol A. Carter, Chaoping Chen, Susan M. Watanabe
Publikováno v:
PLoS ONE, Vol 13, Iss 1, p e0191372 (2018)
PLoS ONE
PLoS ONE
HIV-1 protease autoprocessing is responsible for liberation of free mature protease (PR) from the Gag-Pol polyprotein precursor. A cell-based model system was previously developed to examine the autoprocessing mechanism of fusion precursors carrying
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72dcadc0d57ebe181522f521193d305b
http://europepmc.org/articles/PMC5770051?pdf=render
http://europepmc.org/articles/PMC5770051?pdf=render