Zobrazeno 1 - 10
of 123
pro vyhledávání: '"Volker M Vogt"'
Autor:
Robert A Dick, Chaoyi Xu, Dustin R Morado, Vladyslav Kravchuk, Clifton L Ricana, Terri D Lyddon, Arianna M Broad, J Ryan Feathers, Marc C Johnson, Volker M Vogt, Juan R Perilla, John A G Briggs, Florian K M Schur
Publikováno v:
PLoS Pathogens, Vol 16, Iss 1, p e1008277 (2020)
Retrovirus assembly is driven by the multidomain structural protein Gag. Interactions between the capsid domains (CA) of Gag result in Gag multimerization, leading to an immature virus particle that is formed by a protein lattice based on dimeric, tr
Externí odkaz:
https://doaj.org/article/c3daa523b8f640e092a5ea59c68b3690
Autor:
Robert Alfred Dick, Volker M Vogt
Publikováno v:
Frontiers in Microbiology, Vol 5 (2014)
Assembly of an infectious retroviral particle relies on multimerization of the Gag polyprotein at the inner leaflet of the plasma membrane. The three domains of Gag common to all retroviruses-- MA, CA, and NC-- provide the signals for membrane bindin
Externí odkaz:
https://doaj.org/article/1d608ebd2d254f5280b5325ce88dfa4f
Publikováno v:
Annual Review of Biochemistry. 90:681-707
Located at the inner leaflet of the plasma membrane (PM), phosphatidyl-inositol 4,5-bisphosphate [PI(4,5)P2] composes only 1–2 mol% of total PM lipids. With its synthesis and turnover both spatially and temporally regulated, PI(4,5)P2 recruits and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da9da2b093f3e69a608185e800192382
https://doi.org/10.1146/annurev-biochem-070920-094827
https://doi.org/10.1146/annurev-biochem-070920-094827
Publikováno v:
Journal of molecular biology
Phosphatidylinositol 4,5-bisphosphate (PIP2) is critical for HIV-1 virus assembly. The viral membrane is enriched in PIP2, suggesting that the virus assembles at PIP2-rich microdomains. We showed previously that in model membranes PIP2 can form nanos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29d049954acf9309cbec4bf9c93b85d5
https://doi.org/10.1016/j.jmb.2020.07.018
https://doi.org/10.1016/j.jmb.2020.07.018
Publikováno v:
Annual review of biochemistry. 90
Located at the inner leaflet of the plasma membrane (PM), phosphatidyl-inositol 4,5-bisphosphate [PI(4,5)P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::60c7083e3c31442a311f3affb1e2d395
https://pubmed.ncbi.nlm.nih.gov/33441034
https://pubmed.ncbi.nlm.nih.gov/33441034
Autor:
Jon-Philip R. Feathers, Marc C. Johnson, Andreas Thader, Marco Klanschnig, Robert A. Dick, Martin Obr, Florian K. M. Schur, Volker M. Vogt, Clifton L. Ricana, Nadia Nikulin
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Inositol hexakisphosphate (IP6) is an assembly cofactor for HIV-1. We report here that IP6 is also used for assembly of Rous sarcoma virus (RSV), a retrovirus from a different genus. IP6 is ~100-fold more potent at promoting RSV mature capsid protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a39db804672be6c19213d5c10b3195d
https://doi.org/10.1101/2020.12.03.410175
https://doi.org/10.1101/2020.12.03.410175
Publikováno v:
Journal of Virology. 90:9518-9532
The retroviral structural protein Gag binds to the inner leaflet of the plasma membrane (PM), and many cellular proteins do so as well. We used Rous sarcoma virus (RSV) Gag together with membrane sensors to study the principles governing peripheral p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ca8b4e4edc7a8ce17810723e89e875a
https://doi.org/10.1128/jvi.01102-16
https://doi.org/10.1128/jvi.01102-16
Publikováno v:
Biophysical journal. 114(11)
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P 2 or PIP2), is a key component of the inner leaflet of the plasma membrane in eukaryotic cells. In model membranes, PIP2 has been reported to form clusters, but whether these locally different condition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::639d3e8dba5a24dd1ce0d0a686358ee7
https://pubmed.ncbi.nlm.nih.gov/29874599
https://pubmed.ncbi.nlm.nih.gov/29874599
Autor:
Florian K. M. Schur, Chaoyi Xu, Marc C. Johnson, Owen Pornillos, Juan R. Perilla, Volker M. Vogt, Clifton L. Ricana, Jonathan M. Wagner, Robert A. Dick, Barbie K. Ganser-Pornillos, Kaneil K. Zadrozny, Terri D. Lyddon
Publikováno v:
Nature. 560(7719)
A short, 14-amino-acid segment called SP1, located in the Gag structural protein1, has a critical role during the formation of the HIV-1 virus particle. During virus assembly, the SP1 peptide and seven preceding residues fold into a six-helix bundle,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de00a3f0bac5ccd173c04d1ab76640c6
https://pubmed.ncbi.nlm.nih.gov/30158708
https://pubmed.ncbi.nlm.nih.gov/30158708
Publikováno v:
Journal of Virology. 89:10294-10302
The polyprotein Gag is the primary structural component of retroviruses. Gag consists of independently folded domains connected by flexible linkers. Interactions between the conserved capsid (CA) domains of Gag mediate formation of hexameric protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b79477afbdfeef665c34140ad3008ae9
https://doi.org/10.1128/jvi.01502-15
https://doi.org/10.1128/jvi.01502-15