Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion. - Wikidata - wikimedia - TriplyDB

Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion.

Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion.

http://www.wikidata.org/entity/Q34713747

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Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm Herpes simplex virus glycoprotein B associates with target membranes via its fusion loops Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B Blocking antibody access to neutralizing domains on glycoproteins involved in entry as a novel mechanism of immune evasion by herpes simplex virus type 1 glycoproteins C and E Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry Virion Glycoprotein-Mediated Immune Evasion by Human Cytomegalovirus: a Sticky Virus Makes a Slick Getaway Herpesvirus gB: A Finely Tuned Fusion Machine Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme Crystal structure of the conserved herpesvirus fusion regulator complex gH–gL Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody Extensive Mutagenesis of the HSV-1 gB Ectodomain Reveals Remarkable Stability of Its Postfusion Form Structural basis for the antibody neutralization ofHerpes simplex virus Interaction domain of glycoproteins gB and gH of Marek's disease virus and identification of an antiviral peptide with dual functions Reevaluating herpes simplex virus hemifusion.Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry.The Murid Herpesvirus-4 gL regulates an entry-associated conformation change in gH.The herpevac trial for women: Sequence analysis of glycoproteins from viruses obtained from infected subjects.Insertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry.Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.Glycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entry Low pH-induced conformational change in herpes simplex virus glycoprotein B.Herpes simplex virus glycoproteins H/L bind to cells independently of {alpha}V{beta}3 integrin and inhibit virus entry, and their constitutive expression restricts infection Glycoprotein L sets the neutralization profile of murid herpesvirus 4.Bimolecular Fluorescence Complementation analysis to reveal protein interactions in herpes virus infected cells.The herpes simplex virus type 1 UL20 protein and the amino terminus of glycoprotein K (gK) physically interact with gB.Herpes simplex virus type 2 glycoprotein H interacts with integrin αvβ3 to facilitate viral entry and calcium signaling in human genital tract epithelial cells.Herpesvirus glycoproteins undergo multiple antigenic changes before membrane fusion.Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.Antibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization.Herpes simplex virus glycoproteins gH/gL and gB bind Toll-like receptor 2, and soluble gH/gL is sufficient to activate NF-κB Herpes virus fusion and entry: a story with many characters.The amino terminus of herpes simplex virus 1 glycoprotein K is required for virion entry via the paired immunoglobulin-like type-2 receptor alpha HSV activates Akt to trigger calcium release and promote viral entry: novel candidate target for treatment and suppression.PDGF receptor-α does not promote HCMV entry into epithelial and endothelial cells but increased quantities stimulate entry by an abnormal pathway.Impact of valency of a glycoprotein B-specific monoclonal antibody on neutralization of herpes simplex virus Dissection of the antibody response against herpes simplex virus glycoproteins in naturally infected humans

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Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion.

http://www.wikidata.org/entity/Q34713747

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2007 nî lūn-bûn

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2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2007 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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Bimolecular complementation re ...... each other during cell fusion.

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Bimolecular complementation re ...... each other during cell fusion.

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Bimolecular complementation re ...... each other during cell fusion.

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Bimolecular complementation re ...... each other during cell fusion.

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Bimolecular complementation re ...... each other during cell fusion.

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Bimolecular complementation re ...... each other during cell fusion.

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Proceedings of the National Academy of Sciences of the United States of America

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Bimolecular complementation re ...... each other during cell fusion.

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Brigid Reilly

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Doina Atanasiu

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Gary H Cohen

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J Charles Whitbeck

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Tina M Cairns

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P2860

Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor

Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM).

Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted

Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions

Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B

A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications

Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation

The avian retrovirus avian sarcoma/leukosis virus subtype A reaches the lipid mixing stage of fusion at neutral pH.

Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism.

The gH-gL complex of herpes simplex virus (HSV) stimulates neutralizing antibody and protects mice against HSV type 1 challenge

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47

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104

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Roselyn J. Eisenberg

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2007-11-14T00:00:00Z

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5842932

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18003913

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membrane fusion involved in viral entry into host cell

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2141843

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