Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA.
about
PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein responsecDNAs encoding the large subunit of human replication factor CDynamics of DNA damage response proteins at DNA breaks: a focus on protein modificationsTwo DNA-binding and nick recognition modules in human DNA ligase IIIConnecting the Dots: From DNA Damage and Repair to AgingDNA Damage and Pulmonary HypertensionA novel zinc snap motif conveys structural stability to 3-methyladenine DNA glycosylase IThe DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc FingerIdentification of a zinc finger domain in the human NEIL2 (Nei-like-2) proteinPoly(ADP-ribosyl)ation reactions in the regulation of nuclear functionsDNA ligase III is recruited to DNA strand breaks by a zinc finger motif homologous to that of poly(ADP-ribose) polymerase. Identification of two functionally distinct DNA binding regions within DNA ligase III.The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity.Overproduction of the poly(ADP-ribose) polymerase DNA-binding domain blocks alkylation-induced DNA repair synthesis in mammalian cells3'-5' phosphoadenosine phosphate is an inhibitor of PARP-1 and a potential mediator of the lithium-dependent inhibition of PARP-1 in vivoPoly(ADP-ribosyl)ation of p53 in vitro and in vivo modulates binding to its DNA consensus sequence.Inhibition of poly(ADP-ribose) synthetase (PARS) and protection against peroxynitrite-induced cytotoxicity by zinc chelation.A role for poly(ADP-ribosyl)ation in DNA methylation.New opportunities in chemosensitization and radiosensitization: modulating the DNA-damage response.Cloning of cDNA encoding Drosophila poly(ADP-ribose) polymerase: leucine zipper in the auto-modification domain.Normal telomere length and chromosomal end capping in poly(ADP-ribose) polymerase-deficient mice and primary cells despite increased chromosomal instability.Characterization of the interactions of PARP-1 with UV-damaged DNA in vivo and in vitroThe Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species.Requirement of poly(ADP-ribose) polymerase in recovery from DNA damage in mice and in cells.Mutations in the amino-terminal domain of the human poly(ADP-ribose) polymerase that affect its catalytic activity but not its DNA binding capacity.Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes.Poly(ADP-ribose) polymerase: molecular biological aspects.Structural recognition of DNA by poly(ADP-ribose)polymerase-like zinc finger families.Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sitesConformational activation of poly(ADP-ribose) polymerase-1 upon DNA binding revealed by small-angle X-ray scattering.The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.Poly(ADP-ribose) polymerase-2: emerging transcriptional roles of a DNA-repair protein.The potential of PARP inhibitors in neuro-oncology.Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins.Kin17, a mouse nuclear zinc finger protein that binds preferentially to curved DNA.Conformational transitions of proteins engaged in DNA double-strand break repair, analysed by tryptophan fluorescence emission and FRET.Destabilization of Zn2+ coordination in ADP-ribose transferase (polymerizing) by 6-nitroso-1,2-benzopyrone coincidental with inactivation of the polymerase but not the DNA binding function.Poly(adenosine diphosphate-ribose) polymerase as therapeutic target: lessons learned from its inhibitors.Visible light may directly induce nuclear DNA damage triggering the death pathway in RGC-5 cells.Expression of JP-8-induced inflammatory genes in AEII cells is mediated by NF-kappaB and PARP-1.PARP-mediated repair, homologous recombination, and back-up non-homologous end joining-like repair of single-strand nicks
P2860
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P2860
Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
Zinc-binding domain of poly(AD ...... f single strand breaks on DNA.
@en
type
label
Zinc-binding domain of poly(AD ...... f single strand breaks on DNA.
@en
prefLabel
Zinc-binding domain of poly(AD ...... f single strand breaks on DNA.
@en
P2093
P1476
Zinc-binding domain of poly(AD ...... f single strand breaks on DNA.
@en
P2093
Gradwohl G
Molinete M
Ménissier-de Murcia J
de Murcia G
P304
P356
10.1016/0022-2836(89)90302-1
P407
P577
1989-11-01T00:00:00Z