Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry. - Wikidata - thesis-toulmin - TriplyDB

Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.

Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.

http://www.wikidata.org/entity/Q34324896

about

PILRalpha is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B Bimolecular complementation defines functional regions of Herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion Analysis of a neutralizing antibody for human herpesvirus 6B reveals a role for glycoprotein Q1 in viral entry Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B 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 Viruses Utilize Cellular Cues in Distinct Combination to Undergo Systematic Priming and Uncoating Retargeting Strategies for Oncolytic Herpes Simplex Viruses Herpesvirus gB: A Finely Tuned Fusion Machine Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme Structure of Epstein-Barr Virus Glycoprotein 42 Suggests a Mechanism for Triggering Receptor-Activated Virus Entry Crystal Structure of the cis-Dimer of Nectin-1: IMPLICATIONS FOR THE ARCHITECTURE OF CELL-CELL JUNCTIONS Structure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1 Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion Structural basis for the antibody neutralization ofHerpes simplex virus Viral membrane fusion.Reevaluating herpes simplex virus hemifusion.Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion.Glycosaminoglycan interactions in murine gammaherpesvirus-68 infection Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection 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 Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein D 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 Global sensing of the antigenic structure of herpes simplex virus gD using high-throughput array-based SPR imaging.Repertoire of epitopes recognized by serum IgG from humans vaccinated with herpes simplex virus 2 glycoprotein D Glycoprotein B switches conformation during murid herpesvirus 4 entry Herpes B virus gD interaction with its human receptor--an in silico analysis approach.Herpesvirus glycoproteins undergo multiple antigenic changes before membrane fusion.Antibody-induced conformational changes in herpes simplex virus glycoprotein gD reveal new targets for virus neutralization.Herpes virus fusion and entry: a story with many characters.Herpes simplex virus glycoprotein D interferes with binding of herpesvirus entry mediator to its ligands through downregulation and direct competition Impact of valency of a glycoprotein B-specific monoclonal antibody on neutralization of herpes simplex virus Crystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.Construction and properties of a herpes simplex virus 1 designed to enter cells solely via the IL-13alpha2 receptor A herpes simplex virus recombinant that exhibits a single-chain antibody to HER2/neu enters cells through the mammary tumor receptor, independently of the gD receptors.Computational repositioning of ethno medicine elucidated gB-gH-gL complex as novel anti herpes drug target.

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P2860

Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.

http://www.wikidata.org/entity/Q34324896

description

2005 nî lūn-bûn

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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Structure of unliganded HSV gD ...... ted activation of virus entry.

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SJ.EMBOJ.7600875

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The EMBO Journal

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Structure of unliganded HSV gD ...... ated activation of virus entry

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Andrea Carfí

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Don C Wiley

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Gary H Cohen

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J Charles Whitbeck

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Sarah A Connolly

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Vinit M Supekar

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P2860

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

Improved methods for building protein models in electron density maps and the location of errors in these models

Herpes simplex virus glycoprotein D bound to the human receptor HveA

Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1

Automated protein model building combined with iterative structure refinement

The CCP4 suite: programs for protein crystallography

The atomic structure of protein-protein recognition sites

Crystallization and preliminary diffraction studies of the ectodomain of the envelope glycoprotein D from herpes simplex virus 1 alone and in complex with the ectodomain of the human receptor HveA

The antigenic structure of the HIV gp120 envelope glycoprotein

Identification of functional regions of herpes simplex virus glycoprotein gD by using linker-insertion mutagenesis.

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4144-4153

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scholarly article

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10.1038/SJ.EMBOJ.7600875

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23

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24

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Roselyn J. Eisenberg

Claude Krummenacher

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2005-11-17T00:00:00Z

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7476851

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1356314

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