Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody - Wikidata - wikimedia - TriplyDB

Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody

Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody

http://www.wikidata.org/entity/Q27666356

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Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus Retargeting Strategies for Oncolytic Herpes Simplex Viruses Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex Mechanism for neutralizing activity by the anti-CMV gH/gL monoclonal antibody MSL-109 Assembly and architecture of the EBV B cell entry triggering complex Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.A wide extent of inter-strain diversity in virulent and vaccine strains of alphaherpesviruses.Herpesvirus glycoproteins undergo multiple antigenic changes before membrane fusion.Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Herpes virus fusion and entry: a story with many characters.The conserved disulfide bond within domain II of Epstein-Barr virus gH has divergent roles in membrane fusion with epithelial cells and B cells Structural and biochemical studies of HCMV gH/gL/gO and Pentamer reveal mutually exclusive cell entry complexes.Comparative analysis of glycoprotein B (gB) of equine herpesvirus type 1 and type 4 (EHV-1 and EHV-4) in cellular tropism and cell-to-cell transmission Structure-function analysis of varicella-zoster virus glycoprotein H identifies domain-specific roles for fusion and skin tropism.Fusion of Epstein-Barr virus with epithelial cells can be triggered by αvβ5 in addition to αvβ6 and αvβ8, and integrin binding triggers a conformational change in glycoproteins gHgL.A site of varicella-zoster virus vulnerability identified by structural studies of neutralizing antibodies bound to the glycoprotein complex gHgL.Fusing structure and function: a structural view of the herpesvirus entry machinery.The Engineering of a Novel Ligand in gH Confers to HSV an Expanded Tropism Independent of gD Activation by Its Receptors Scanning Mutagenesis of Human Cytomegalovirus Glycoprotein gH/gL.Dissociation of HSV gL from gH by αvβ6- or αvβ8-integrin promotes gH activation and virus entry.Patient-Specific Neutralizing Antibody Responses to Herpes Simplex Virus Are Attributed to Epitopes on gD, gB, or Both and Can Be Type Specific.Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Probing the interactions of CdTe quantum dots with pseudorabies virus.A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B.gH/gL supercomplexes at early stages of herpesvirus entry Regulation of HSV glycoprotein induced cascade of events governing cell-cell fusion.Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.Peptide inhibitors against herpes simplex virus infections.Epstein-Barr virus infection mechanisms Functional Relevance of the N-Terminal Domain of Pseudorabies Virus Envelope Glycoprotein H and Its Interaction with Glycoprotein L.Mutations in Pseudorabies Virus Glycoproteins gB, gD, and gH Functionally Compensate for the Absence of gL.Comparative Mutagenesis of Pseudorabies Virus and Epstein-Barr Virus gH Identifies a Structural Determinant within Domain III of gH Required for Surface Expression and Entry Function Functional Characterization of Glycoprotein H Chimeras Composed of Conserved Domains of the Pseudorabies Virus and Herpes Simplex Virus 1 Homologs.Structure-based functional analyses of domains II and III of pseudorabies virus glycoprotein H.The highly conserved proline at position 438 in pseudorabies virus gH is important for regulation of membrane fusion.Novel mutations in gB and gH circumvent the requirement for known gD Receptors in herpes simplex virus 1 entry and cell-to-cell spread.The fusion loops and membrane proximal region of Epstein-Barr virus glycoprotein B (gB) can function in the context of herpes simplex virus 1 gB when substituted individually but not in combination.Initial Contact: The First Steps in Herpesvirus Entry.

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Structure of a core fragment of glycoprotein H from pseudorabies virus in complex with antibody

http://www.wikidata.org/entity/Q27666356

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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Structure of a core fragment o ...... virus in complex with antibody

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Structure of a core fragment o ...... virus in complex with antibody

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Structure of a core fragment o ...... virus in complex with antibody

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Structure of a core fragment o ...... virus in complex with antibody

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Barbara G Klupp

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Harald Granzow

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Marija Backovic

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P2860

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

Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.

Three-dimensional structure of the amino-terminal domain of syntaxin 6, a SNAP-25 C homolog

Structure of a trimeric variant of the Epstein-Barr virus glycoprotein B

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

Crystal structure of the conserved herpesvirus fusion regulator complex gH–gL

Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex

The CCP4 suite: programs for protein crystallography

Analysis of membrane and surface protein sequences with the hydrophobic moment plot

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22635-40

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10.1073/PNAS.1011507107

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52

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107

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Thomas Mettenleiter

Gérard Bricogne

Marie-Christine Vaney

Rebecca M DuBois

Joseph Cockburn

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2010-12-28T00:00:00Z

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