Results 41 to 50 of about 136,075 (281)

HIV-1 buds predominantly at the plasma membrane of primary human macrophages.

open access: yesPLoS Pathogens, 2007
HIV-1 assembly and release are believed to occur at the plasma membrane in most host cells with the exception of primary macrophages, for which exclusive budding at late endosomes has been reported.
Sonja Welsch   +5 more
doaj   +1 more source

A Budding-Defective M2 Mutant Exhibits Reduced Membrane Interaction, Insensitivity To Cholesterol, And Perturbed Interdomain Coupling [PDF]

open access: yes, 2017
Influenza A M2 is a membrane-associated protein with a C-terminal amphipathic helix that plays a cholesterol-dependent role in viral budding. An M2 mutant with alanine substitutions in the C-terminal amphipathic helix is deficient in viral scission. With
Feix, J. B.   +5 more
core   +2 more sources

Virus Entry, Assembly, Budding, and Membrane Rafts [PDF]

open access: yesMicrobiology and Molecular Biology Reviews, 2003
SUMMARY As intracellular parasites, viruses rely heavily on the use of numerous cellular machineries for completion of their replication cycle. The recent discovery of the heterogeneous distribution of the various lipids within cell membranes has led to the proposal that sphingolipids and cholesterol tend to segregate in ...
Nathalie, Chazal, Denis, Gerlier
openaire   +2 more sources

The nuclear egress complex of Epstein-Barr virus buds membranes through an oligomerization-driven mechanism.

open access: yesPLoS Pathogens, 2022
During replication, herpesviral capsids are translocated from the nucleus into the cytoplasm by an unusual mechanism, termed nuclear egress, that involves capsid budding at the inner nuclear membrane.
Michael K Thorsen   +2 more
doaj   +1 more source

Budding of domains in mixed bilayer membranes [PDF]

open access: yesPhysical Review E, 2015
We propose a model that accounts for budding behavior of domains in lipid bilayers, where each of the bilayer leaflets has a coupling between its local curvature and local lipid composition. The compositional asymmetry between the two monolayers leads to an overall spontaneous curvature.
Wolff, Jean   +2 more
openaire   +3 more sources

Association of Influenza Virus Proteins with Membrane Rafts

open access: yesAdvances in Virology, 2011
Assembly and budding of influenza virus proceeds in the viral budozone, a domain in the plasma membrane with characteristics of cholesterol/sphingolipid-rich membrane rafts.
Michael Veit, Bastian Thaa
doaj   +1 more source

The Race against Protease Activation Defines the Role of ESCRTs in HIV Budding. [PDF]

open access: yesPLoS Pathogens, 2016
HIV virions assemble on the plasma membrane and bud out of infected cells using interactions with endosomal sorting complexes required for transport (ESCRTs). HIV protease activation is essential for maturation and infectivity of progeny virions, however,
Mourad Bendjennat, Saveez Saffarian
doaj   +1 more source

Membrane Remodeling by Arc/Arg3.1

open access: yesFrontiers in Molecular Biosciences, 2021
The activity-regulated cytoskeletal-associated protein (Arc, also known as Arg3.1) is an immediate early gene product induced by activity/experience and required for multiple modes of synaptic plasticity.
Per Niklas Hedde   +7 more
doaj   +1 more source

Human annexin A6 interacts with influenza a virus protein M2 and negatively modulates infection [PDF]

open access: yes, 2011
Copyright © 2012, American Society for Microbiology. All Rights ReservedThe influenza A virus M2 ion channel protein has the longest cytoplasmic tail (CT) among the three viral envelope proteins and is well conserved between different viral strains.
B. Nal   +69 more
core   +2 more sources

Why enveloped viruses need cores -- the contribution of a nucleocapsid core to viral budding

open access: yes, 2017
During the alphavirus lifecycle, a nucleocapsid core buds through the cell membrane to acquire an outer envelope of lipid membrane and viral glycoproteins. However, the presence of a nucleocapsid core is not required for assembly of infectious particles.
Hagan, Michael F.   +2 more
core   +1 more source

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