Structure-based mutational analysis of the bovine papillomavirus E1 helicase domain identifies residues involved in the nonspecific DNA binding activity required for double trimer formation.
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Nuclear export of human papillomavirus type 31 E1 is regulated by Cdk2 phosphorylation and required for viral genome maintenance.The inhibitory action of P56 on select functions of E1 mediates interferon's effect on human papillomavirus DNA replication.Novel Bovine Papillomavirus Type Discovered by Rolling-Circle Amplification Coupled with Next-Generation SequencingCK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins.Mutations in DNA binding and transactivation domains affect the dynamics of parvovirus NS1 protein.The E1 proteins.Characterization of human papillomavirus type 154 and tissue tropism of gammapapillomavirusesComplete genome sequences of three novel human papillomavirus types, 175, 178, and 180.A conserved regulatory module at the C terminus of the papillomavirus E1 helicase domain controls E1 helicase assembly.Characterization of human papillomavirus subtype 72b
P2860
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P2860
Structure-based mutational analysis of the bovine papillomavirus E1 helicase domain identifies residues involved in the nonspecific DNA binding activity required for double trimer formation.
description
2010 nî lūn-bûn
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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
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2010年論文
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2010年论文
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name
Structure-based mutational ana ...... d for double trimer formation.
@en
type
label
Structure-based mutational ana ...... d for double trimer formation.
@en
prefLabel
Structure-based mutational ana ...... d for double trimer formation.
@en
P2093
P2860
P356
P1433
P1476
Structure-based mutational ana ...... d for double trimer formation.
@en
P2093
Arne Stenlund
Stephen Schuck
Xiaofei Liu
P2860
P304
P356
10.1128/JVI.02214-09
P407
P577
2010-02-10T00:00:00Z