The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection
about
From structure to redox: The diverse functional roles of disulfides and implications in disease.HVint: A Strategy for Identifying Novel Protein-Protein Interactions in Herpes Simplex Virus Type 1Herpesvirus Capsid Assembly and DNA Packaging.The Essential Human Cytomegalovirus Proteins pUL77 and pUL93 Are Structural Components Necessary for Viral Genome Encapsidation.A bovine herpesvirus 1 pUL51 deletion mutant shows impaired viral growth in vitro and reduced virulence in rabbitsThe exonuclease activity of HSV-1 UL12 is required for the production of viral DNA that can be packaged to produce infectious virus.Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.
P2860
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P2860
The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年學術文章
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name
The putative herpes simplex vi ...... ond formation during infection
@ast
The putative herpes simplex vi ...... ond formation during infection
@en
type
label
The putative herpes simplex vi ...... ond formation during infection
@ast
The putative herpes simplex vi ...... ond formation during infection
@en
prefLabel
The putative herpes simplex vi ...... ond formation during infection
@ast
The putative herpes simplex vi ...... ond formation during infection
@en
P2093
P2860
P356
P1433
P1476
The putative herpes simplex vi ...... ond formation during infection
@en
P2093
Athena Kosinski
Brandon S Albright
Elizabeth A Cook
Nigel D Stow
Renata Szczepaniak
P2860
P304
P356
10.1128/JVI.01913-14
P577
2014-10-15T00:00:00Z