Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Alexandra B, Samal"'
Autor:
R. Elliot Murphy, Alexandra B. Samal, Gunnar Eastep, Ruba H. Ghanam, Peter E. Prevelige, Jamil S. Saad
Publikováno v:
Proceedings, Vol 50, Iss 1, p 114 (2020)
During the late phase of the HIV-1 replication cycle, the Gag polyproteins are transported to the plasma membrane (PM) for assembly. Gag targeting and assembly on the PM is dependent on interactions between its matrix (MA) domain and phosphatidylinos
Externí odkaz:
https://doaj.org/article/0e7bae4d392b4dafbcb13e85f3a223d3
Publikováno v:
Proceedings of the National Academy of Sciences. 119
During the late phase of HIV type 1 (HIV-1) infection cycle, the virally encoded Gag polyproteins are targeted to the inner leaflet of the plasma membrane (PM) for assembly, formation of immature particles, and virus release. Gag binding to the PM is
Autor:
Bliss J Chang, Alexandra B Samal, Jiri Vlach, Timothy F Fernandez, Dewey Brooke, Peter E Prevelige, Jamil S Saad
Publikováno v:
PLoS ONE, Vol 11, Iss 1, p e0146493 (2016)
The extrinsic apoptotic pathway is initiated by binding of a Fas ligand to the ectodomain of the surface death receptor Fas protein. Subsequently, the intracellular death domain of Fas (FasDD) and that of the Fas-associated protein (FADD) interact to
Externí odkaz:
https://doaj.org/article/16fb252c2f12402884702fd84dad4583
Autor:
Jiri Vlach, Alexandra B. Samal, Anita Niedziela-Majka, Michael V. Lee, Giuseppe A. Papalia, Melanie H. Wong, Katherine M. Brendza, Brian E. Schultz, Dmitry O. Koltun, Hyock Joo Kwon, Joy Y. Feng, Roman Sakowicz, Nikolai Novikov, Jamil S. Saad
Publikováno v:
Journal of Molecular Biology. 431:1440-1459
Calcium/calmodulin-dependent protein kinase II (CaMKII) is a multifunctional serine/threonine protein kinase that transmits calcium signals in various cellular processes. CaMKII is activated by calcium-bound calmodulin (Ca2+/CaM) through a direct bin
Publikováno v:
Frontiers in Microbiology, Vol 3 (2012)
Human immunodeficiency virus type-1 (HIV-1) encodes a polypeptide called Gag that is able to form virus-like particles (VLPs) in vitro in the absence of any cellular or viral constituents. During the late phase of the HIV-1 infection, Gag polyprotein
Externí odkaz:
https://doaj.org/article/4ee8cdbc1eec4c888ebed541eebe1182
Autor:
Jamil S. Saad, Jiri Vlach, Peter E. Prevelige, Vicente Mas, R. Elliot Murphy, Alexandra B. Samal
Publikováno v:
J Biol Chem
Repisalud
Instituto de Salud Carlos III (ISCIII)
Repisalud
Instituto de Salud Carlos III (ISCIII)
During the late phase of the HIV-1 replication cycle, the viral Gag polyproteins are targeted to the plasma membrane for assembly. The Gag-membrane interaction is mediated by binding of Gag's N-terminal myristoylated matrix (MA) domain to phosphatidy
Autor:
Melanie H, Wong, Alexandra B, Samal, Mike, Lee, Jiri, Vlach, Nikolai, Novikov, Anita, Niedziela-Majka, Joy Y, Feng, Dmitry O, Koltun, Katherine M, Brendza, Hyock Joo, Kwon, Brian E, Schultz, Roman, Sakowicz, Jamil S, Saad, Giuseppe A, Papalia
Publikováno v:
Journal of molecular biology. 431(7)
Calcium/calmodulin-dependent protein kinase II (CaMKII) is a multifunctional serine/threonine protein kinase that transmits calcium signals in various cellular processes. CaMKII is activated by calcium-bound calmodulin (Ca
Publikováno v:
Journal of Biological Chemistry. 289:8697-8705
Subcellular distribution of calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1)-infected cells is distinct from that observed in uninfected cells. CaM co-localizes and interacts with the HIV-1 Gag protein in the cytosol of infected cells.
Publikováno v:
Journal of Biological Chemistry. 286:33533-33543
Subcellular distribution of Calmodulin (CaM) in human immunodeficiency virus type-1 (HIV-1)-infected cells is distinct from that observed in uninfected cells. CaM has been shown to interact and co-localize with the HIV-1 Gag protein in infected cells
Autor:
William J. Cook, Lawrence J. DeLucas, Alexandra B. Samal, Debasish Chattopadhyay, Norbert Schormann
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 63:571-580
Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate in the presence of Mg(2+) ions. The enzyme plays multiple cellular roles by maintaining a low dUTP:dTTP ratio and by synthesizing the s