Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.

Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.

Item
http://www.wikidata.org/entity/Q30488301
Poxvirus cell entry: how many proteins does it take?A Turn-like Structure "KKPE" Segment Mediates the Specific Binding of Viral Protein A27 to Heparin and Heparan Sulfate on Cell SurfacesVaccinia viral protein A27 is anchored to the viral membrane via a cooperative interaction with viral membrane protein A17Formation of orthopoxvirus cytoplasmic A-type inclusion bodies and embedding of virions are dynamic processes requiring microtubules.Congregation of orthopoxvirus virions in cytoplasmic A-type inclusions is mediated by interactions of a bridging protein (A26p) with a matrix protein (ATIp) and a virion membrane-associated protein (A27p)Vaccinia virus A25 and A26 proteins are fusion suppressors for mature virions and determine strain-specific virus entry pathways into HeLa, CHO-K1, and L cells.Smallpox vaccines: targets of protective immunity.Crystal structure of vaccinia viral A27 protein reveals a novel structure critical for its function and complex formation with A26 proteinVaccinia mature virus fusion regulator A26 protein binds to A16 and G9 proteins of the viral entry fusion complex and dissociates from mature virions at low pHThe lipid raft-associated protein CD98 is required for vaccinia virus endocytosis.Orthopoxvirus species and strain differences in cell entry.Poxvirus proteomics and virus-host protein interactions.Elimination of A-type inclusion formation enhances cowpox virus replication in mice: implications for orthopoxvirus evolutionFine structure of the vaccinia virion determined by controlled degradation and immunolocalization.
P2860

Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.

Item
http://www.wikidata.org/entity/Q30488301
description
2009 nî lūn-bûn
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2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Disulfide bond formation at th ...... noglycan-mediated cell fusion.
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Disulfide bond formation at th ...... noglycan-mediated cell fusion.
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type
label
Disulfide bond formation at th ...... noglycan-mediated cell fusion.
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Disulfide bond formation at th ...... noglycan-mediated cell fusion.
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prefLabel
Disulfide bond formation at th ...... noglycan-mediated cell fusion.
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Disulfide bond formation at th ...... noglycan-mediated cell fusion.
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P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932
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P1433
P1476
Disulfide bond formation at th ...... noglycan-mediated cell fusion.
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P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932