Zobrazeno 1 - 10
of 766
pro vyhledávání: '"Gregory A. Voth"'
Autor:
Kun Wang, Chia-Wei Lee, Xuewu Sui, Siyoung Kim, Shuhui Wang, Aidan B. Higgs, Aaron J. Baublis, Gregory A. Voth, Maofu Liao, Tobias C. Walther, Robert V. Farese
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract Cells remodel glycerophospholipid acyl chains via the Lands cycle to adjust membrane properties. Membrane-bound O-acyltransferase (MBOAT) 7 acylates lyso-phosphatidylinositol (lyso-PI) with arachidonyl-CoA. MBOAT7 mutations cause brain devel
Externí odkaz:
https://doaj.org/article/68b75801fe374236b43a6404d4b29a01
Autor:
Guochao Wei, Naseer Iqbal, Valentine V. Courouble, Ashwanth C. Francis, Parmit K. Singh, Arpa Hudait, Arun S. Annamalai, Stephanie Bester, Szu-Wei Huang, Nikoloz Shkriabai, Lorenzo Briganti, Reed Haney, Vineet N. KewalRamani, Gregory A. Voth, Alan N. Engelman, Gregory B. Melikyan, Patrick R. Griffin, Francisco Asturias, Mamuka Kvaratskhelia
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-19 (2022)
Host proteins CPSF6, NUP153, and SEC24C are vital for HIV-1 infection. They bind to the viral capsid protein and contribute to shuttling of virions through the cytoplasm (SEC24C), import into the nucleus (NUP153 and CPSF6) and subsequent trafficking
Externí odkaz:
https://doaj.org/article/8104b0cb2298482ba5ea2e87aa234579
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Simulations reveal concerted interactions between the SARS-CoV-2 spike trimers and ACE2 receptors that result in cooperative spike binding and shedding, and further suggest that variant efficacy is promoted by increased RBD opening or S1/S2 cleavage
Externí odkaz:
https://doaj.org/article/b7971dbf743c4c2a9d686fef92340311
Autor:
Kimberly A Dolan, Mandira Dutta, David M Kern, Abhay Kotecha, Gregory A Voth, Stephen G Brohawn
Publikováno v:
eLife, Vol 11 (2022)
SARS-CoV-2 encodes four structural proteins incorporated into virions, spike (S), envelope (E), nucleocapsid (N), and membrane (M). M plays an essential role in viral assembly by organizing other structural proteins through physical interactions and
Externí odkaz:
https://doaj.org/article/e30b73ef0ebc4151b16b3ceff1fe0988
Autor:
Siyoung Kim, Jeeyun Chung, Henning Arlt, Alexander J Pak, Robert V Farese Jnr, Tobias C Walther, Gregory A Voth
Publikováno v:
eLife, Vol 11 (2022)
Lipid droplets (LDs) are organelles formed in the endoplasmic reticulum (ER) to store triacylglycerol (TG) and sterol esters. The ER protein seipin is key for LD biogenesis. Seipin forms a cage-like structure, with each seipin monomer containing a co
Externí odkaz:
https://doaj.org/article/45901e8cb1ba41fd93941bb6a40f02e9
Autor:
Alvin Yu, Katarzyna A. Skorupka, Alexander J. Pak, Barbie K. Ganser-Pornillos, Owen Pornillos, Gregory A. Voth
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
Tripartite-motif containing (TRIM) proteins modulate cellular responses to viral infection. Here the authors use molecular dynamics simulations to demonstrate that TRIM5α uses a two-dimensional lattice hopping mechanism to aggregate on the HIV capsi
Externí odkaz:
https://doaj.org/article/bd9cc94b90814f36bcde658814d9e443
Publikováno v:
The Journal of Physical Chemistry B. 127:3911-3918
Publikováno v:
The journal of physical chemistry. B. 126(38)
Classical molecular dynamics simulations are a versatile tool in the study of biomolecular systems, but they usually rely on a fixed bonding topology, precluding the explicit simulation of chemical reactivity. Certain modifications can permit the mod
Autor:
Viviana Monje-Galvan, Gregory A Voth
Publikováno v:
eLife, Vol 9 (2020)
Specific protein-lipid interactions are critical for viral assembly. We present a molecular dynamics simulation study on the binding mechanism of the membrane targeting domain of HIV-1 Gag protein. The matrix (MA) domain drives Gag onto the plasma me
Externí odkaz:
https://doaj.org/article/049b6f6f2f3e46b9a81b30c5838411f8
Publikováno v:
ACS Central Science, Vol 3, Iss 12, Pp 1246-1253 (2017)
Externí odkaz:
https://doaj.org/article/13eb23962c6043b1b48b043b97e9c234