Results 31 to 40 of about 1,256,081 (297)

The structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex reveals the protein-membrane and lateral protein-protein interaction [PDF]

open access: yes, 2013
Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex.
Topf, Maya   +41 more
core   +2 more sources

Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity.

open access: yesPLoS Pathogens, 2023
Many enveloped viruses enter host cells by fusing with acidic endosomes. The fusion activity of multiple viral envelope glycoproteins does not generally affect viral membrane permeability.
You Zhang   +4 more
doaj   +1 more source

Membrane curvature regulates the spatial distribution of bulky glycoproteins

open access: yesNature Communications, 2022
MUC1 is a heavily glycosylated protein on the cell surface. Here the authors show that MUC1 prefers negative over positive membrane curvature due to its bulky size, enabling MUC1 to avoid endocytosis and surface removal based on curvature preference.
Chih-Hao Lu   +7 more
doaj   +1 more source

Paramyxovirus Glycoprotein Incorporation, Assembly and Budding: A Three Way Dance for Infectious Particle Production

open access: yesViruses, 2014
Paramyxoviruses are a family of negative sense RNA viruses whose members cause serious diseases in humans, such as measles virus, mumps virus and respiratory syncytial virus; and in animals, such as Newcastle disease virus and rinderpest virus ...
Farah El Najjar   +2 more
doaj   +1 more source

Recognition of viral glycoproteins by influenza A-specific cross- reactive cytolytic T lymphocytes [PDF]

open access: yes, 1980
Two populations of cytolytic T lymphocytes (CTL) generated after influenza A virus infection can be distinguished into one with specificity for the sensitizing hemagglutinin type and a second with cross-reactivity for antigens induced by other type-A ...
Klenk, H   +17 more
core   +1 more source

Protein glycosylation in the gram-negative gamma proteobacterium photorhabdus luminescens [PDF]

open access: yes, 2011
The objective of this research was to investigate the possibility that Photorhabdus luminescens produces glycoproteins and thus contains a protein glycosylation system. P. luminescens is a pathogen of insects and a symbiont of soil nematodes.
Fox, Mary
core   +2 more sources

Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells

open access: yesAdvances in Virology, 2011
Human respiratory syncytial virus (HRSV) is an enveloped RNA virus that assembles and buds from the plasma membrane of infected cells. The ribonucleoprotein complex (RNP) must associate with the viral matrix protein and glycoproteins to form newly ...
Melissa Batonick, Gail W. Wertz
doaj   +1 more source

Biosynthesis and expression of zona pellucida glycoproteins in mammals [PDF]

open access: yes, 2001
The zona pellucida (ZP) is an extracellular matrix surrounding the oocyte and the early embryo that exerts several important functions during fertilization and early embryonic development.
Töpfer-Petersen, E.   +2 more
core   +1 more source

Dynamic organization of Herpesvirus glycoproteins on the viral envelope revealed by super-resolution microscopy.

open access: yesPLoS Pathogens, 2019
The processes of cell attachment and membrane fusion of Herpes Simplex Virus 1 involve many different envelope glycoproteins. Viral proteins gC and gD bind to cellular receptors.
Frauke Beilstein   +5 more
doaj   +1 more source

Super-resolution microscopy reveals specific recruitment of HIV-1 envelope proteins to viral assembly sites dependent on the envelope C-terminal tail [PDF]

open access: yes, 2013
The inner structural Gag proteins and the envelope (Env) glycoproteins of human immunodeficiency virus (HIV-1) traffic independently to the plasma membrane, where they assemble the nascent virion. HIV-1 carries a relatively low number of glycoproteins in
Mike Heilemann   +14 more
core   +2 more sources

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