Membrane anchoring of Epstein-Barr virus gp42 inhibits fusion with B cells even with increased flexibility allowed by engineered spacers - sprookjes - yvandenbroek - TriplyDB

Membrane anchoring of Epstein-Barr virus gp42 inhibits fusion with B cells even with increased flexibility allowed by engineered spacers

Membrane anchoring of Epstein-Barr virus gp42 inhibits fusion with B cells even with increased flexibility allowed by engineered spacers

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Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus.EBV glycoproteins: where are we now?Functional relevance of the transmembrane domain and cytoplasmic tail of the pseudorabies virus glycoprotein H for membrane fusion.

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Membrane anchoring of Epstein-Barr virus gp42 inhibits fusion with B cells even with increased flexibility allowed by engineered spacers

http://www.wikidata.org/entity/Q35038210

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Membrane anchoring of Epstein- ...... allowed by engineered spacers

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Membrane anchoring of Epstein- ...... allowed by engineered spacers

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Membrane anchoring of Epstein- ...... allowed by engineered spacers

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Membrane anchoring of Epstein- ...... allowed by engineered spacers

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Membrane anchoring of Epstein- ...... allowed by engineered spacers

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Membrane anchoring of Epstein- ...... allowed by engineered spacers

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Membrane anchoring of Epstein- ...... allowed by engineered spacers

@en

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Cynthia L Rowe

http://www.w3.org/2001/XMLSchema#string

Jia Chen

http://www.w3.org/2001/XMLSchema#string

Richard Longnecker

http://www.w3.org/2001/XMLSchema#string

Theodore S Jardetzky

http://www.w3.org/2001/XMLSchema#string

P2860

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

A regular pattern of Ig super-motifs defines segmental flexibility as the elastic mechanism of the titin chain.

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

Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity

Assembly and architecture of the EBV B cell entry triggering complex

Epstein-Barr virus uses different complexes of glycoproteins gH and gL to infect B lymphocytes and epithelial cells.

Epstein-Barr virus entry utilizing HLA-DP or HLA-DQ as a coreceptor

Mapping the N-terminal residues of Epstein-Barr virus gp42 that bind gH/gL by using fluorescence polarization and cell-based fusion assays

Defining the geometry of the two-component proteasome degron

Investigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42).

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scholarly article

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10.1128/MBIO.02285-14

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1

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6

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2015-01-06T00:00:00Z

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25564465

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membrane fusion involved in viral entry into host cell

Epstein–Barr virus

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4313908

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