Complete pathway for protein disulfide bond formation encoded by poxviruses
about
Archaeal virus with exceptional virion architecture and the largest single-stranded DNA genomeHuman quiescin-sulfhydryl oxidase, QSOX1: probing internal redox steps by mutagenesisIntermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347Using purine skews to predict genes in AT-rich poxvirusesImportance of disulphide bonds for vaccinia virus L1R protein function.Poxvirus cell entry: how many proteins does it take?Multiple phosphatidylinositol 3-kinases regulate vaccinia virus morphogenesisThe three-dimensional structure of two redox states of cyclophilin A from Schistosoma mansoni. Evidence for redox regulation of peptidyl-prolyl cis-trans isomerase activityStructural basis for the binding of the neutralizing antibody, 7D11, to the poxvirus L1 proteinVaccinia virus L2 protein associates with the endoplasmic reticulum near the growing edge of crescent precursors of immature virions and stabilizes a subset of viral membrane proteinsOrthopoxvirus genome evolution: the role of gene lossGenomic sequence of Spodoptera frugiperda Ascovirus 1a, an enveloped, double-stranded DNA insect virus that manipulates apoptosis for viral reproductionDiscovery of antivirals against smallpoxRequirement for integrase during reverse transcription of human immunodeficiency virus type 1 and the effect of cysteine mutations of integrase on its interactions with reverse transcriptase.The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infectionFrom structure to redox: The diverse functional roles of disulfides and implications in disease.Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.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.Salmon Gill Poxvirus, the Deepest Representative of the Chordopoxvirinae.A bioinformatics pipeline to search functional motifs within whole-proteome data: a case study of poxviruses.Kinetics and intracellular location of intramolecular disulfide bond formation mediated by the cytoplasmic redox system encoded by vaccinia virus.Disulfide bond formation in prokaryotes: history, diversity and designVaccinia virus H2 protein is an essential component of a complex involved in virus entry and cell-cell fusionHigh expression of 23 kDa protein of augmenter of liver regeneration (ALR) in human hepatocellular carcinomaTumorigenic poxviruses up-regulate intracellular superoxide to inhibit apoptosis and promote cell proliferationMaturation of papillomavirus capsids.Vaccinia virus A21 virion membrane protein is required for cell entry and fusionIn silico survey of the mitochondrial protein uptake and maturation systems in the brown alga Ectocarpus siliculosus.The product of the vaccinia virus L5R gene is a fourth membrane protein encoded by all poxviruses that is required for cell entry and cell-cell fusion.The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies.Structure/Function analysis of the vaccinia virus F18 phosphoprotein, an abundant core component required for virion maturation and infectivity.A small molecule inhibitor of redox-regulated protein translocation into mitochondriaCombinations of polyclonal or monoclonal antibodies to proteins of the outer membranes of the two infectious forms of vaccinia virus protect mice against a lethal respiratory challengeFormation and transfer of disulphide bonds in living cells.Molecular dating in the evolution of vertebrate poxviruses.Entry of vaccinia virus and cell-cell fusion require a highly conserved cysteine-rich membrane protein encoded by the A16L gene.The myristate moiety and amino terminus of vaccinia virus l1 constitute a bipartite functional region needed for entryLiver regeneration associated protein (ALR) exhibits antimetastatic potential in hepatocellular carcinoma.Interactions of the vaccinia virus A19 proteinThe structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity.
P2860
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P2860
Complete pathway for protein disulfide bond formation encoded by poxviruses
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2002 թվականի ապրիլին հրատարակված գիտական հոդված
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2002年の論文
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2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年學術文章
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name
Complete pathway for protein disulfide bond formation encoded by poxviruses
@ast
Complete pathway for protein disulfide bond formation encoded by poxviruses
@en
Complete pathway for protein disulfide bond formation encoded by poxviruses
@nl
type
label
Complete pathway for protein disulfide bond formation encoded by poxviruses
@ast
Complete pathway for protein disulfide bond formation encoded by poxviruses
@en
Complete pathway for protein disulfide bond formation encoded by poxviruses
@nl
prefLabel
Complete pathway for protein disulfide bond formation encoded by poxviruses
@ast
Complete pathway for protein disulfide bond formation encoded by poxviruses
@en
Complete pathway for protein disulfide bond formation encoded by poxviruses
@nl
P2860
P356
P1476
Complete pathway for protein disulfide bond formation encoded by poxviruses
@en
P2093
Christine L White
Tatiana G Senkevich
P2860
P304
P356
10.1073/PNAS.062163799
P407
P577
2002-04-30T00:00:00Z