Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.
about
Herpes simplex virus 1 DNA polymerase processivity factor UL42 inhibits TNF-α-induced NF-κB activation by interacting with p65/RelA and p50/NF-κB1Identification of polymerase and processivity inhibitors of vaccinia DNA synthesis using a stepwise screening approachThe positively charged surface of herpes simplex virus UL42 mediates DNA binding.Processing of lagging-strand intermediates in vitro by herpes simplex virus type 1 DNA polymeraseEffects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesisBinding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism.3' to 5' exonuclease activity of herpes simplex virus type 1 DNA polymerase modulates its strand displacement activity.Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activityMechanisms by which herpes simplex virus DNA polymerase limits translesion synthesis through abasic sites.Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase.The herpes simplex virus type 1 DNA polymerase processivity factor increases fidelity without altering pre-steady-state rate constants for polymerization or excision.Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunitsHuman Kaposi's sarcoma herpesvirus processivity factor-8 functions as a dimer in DNA synthesis.Contribution of the 3'- to 5'-exonuclease activity of herpes simplex virus type 1 DNA polymerase to the fidelity of DNA synthesis.Enzymatic therapeutic index of acyclovir. Viral versus human polymerase gamma specificity.
P2860
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P2860
Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.
description
2002 nî lūn-bûn
@nan
2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
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name
Evidence against a simple teth ...... ity by accessory protein UL42.
@ast
Evidence against a simple teth ...... ity by accessory protein UL42.
@en
Evidence against a simple teth ...... ity by accessory protein UL42.
@nl
type
label
Evidence against a simple teth ...... ity by accessory protein UL42.
@ast
Evidence against a simple teth ...... ity by accessory protein UL42.
@en
Evidence against a simple teth ...... ity by accessory protein UL42.
@nl
prefLabel
Evidence against a simple teth ...... ity by accessory protein UL42.
@ast
Evidence against a simple teth ...... ity by accessory protein UL42.
@en
Evidence against a simple teth ...... ity by accessory protein UL42.
@nl
P2860
P1433
P1476
Evidence against a simple teth ...... ity by accessory protein UL42.
@en
P2093
Deborah S Parris
Murari Chaudhuri
P2860
P304
10270-10281
P356
10.1128/JVI.76.20.10270-10281.2002
P407
P577
2002-10-01T00:00:00Z