A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation - Wikidata - wikimedia - TriplyDB

A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation

A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation

http://www.wikidata.org/entity/Q27649201

about

PARPs and the DNA damage response A New Nanobody-Based Biosensor to Study Endogenous PARP1 In Vitro and in Live Human Cells Crystal Structures of Poly(ADP-ribose) Polymerase-1 (PARP-1) Zinc Fingers Bound to DNA: STRUCTURAL AND FUNCTIONAL INSIGHTS INTO DNA-DEPENDENT PARP-1 ACTIVITY The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger Structural studies of the PARP-1 BRCT domain Structural Basis for DNA Damage-Dependent Poly(ADP-ribosyl)ation by Human PARP-1 Understanding specific functions of PARP-2: new lessons for cancer therapy Arsenite interacts selectively with zinc finger proteins containing C3H1 or C4 motifs PARP inhibition: PARP1 and beyond Analyzing structure-function relationships of artificial and cancer-associated PARP1 variants by reconstituting TALEN-generated HeLa PARP1 knock-out cells.Poly(ADP-ribose) polymerase-1 and its cleavage products differentially modulate cellular protection through NF-kappaB-dependent signaling In Silico Investigation of Potential PARP-1 Inhibitors from Traditional Chinese Medicine.The BRCT domain of PARP-1 is required for immunoglobulin gene conversion.Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes.PARP-2 and PARP-3 are selectively activated by 5' phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1.Poly(ADP-ribose) polymerase-1 inhibition: preclinical and clinical development of synthetic lethality.The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction.PARP1 restricts Epstein Barr Virus lytic reactivation by binding the BZLF1 promoter Structural dynamics in DNA damage signaling and repair Identification of a regulatory segment of poly(ADP-ribose) glycohydrolase.Targeting poly(ADP-ribose) polymerase activity for cancer therapy.Signaling mechanism of poly(ADP-ribose) polymerase-1 (PARP-1) in inflammatory diseases.A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.Large-scale preparation and characterization of poly(ADP-ribose) and defined length polymers.Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes Binding kinetics and activity of human poly(ADP-ribose) polymerase-1 on oligo-deoxyribonucleotide substrates.PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damage Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes.Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites Arsenite binding-induced zinc loss from PARP-1 is equivalent to zinc deficiency in reducing PARP-1 activity, leading to inhibition of DNA repair.Human RECQ1 promotes restart of replication forks reversed by DNA topoisomerase I inhibition.The Sound of Silence: RNAi in Poly (ADP-Ribose) Research Targeting PARP-1 allosteric regulation offers therapeutic potential against cancer.Fluorescent sensors of PARP-1 structural dynamics and allosteric regulation in response to DNA damage.Potential biological role of poly (ADP-ribose) polymerase (PARP) in male gametes.Conformational activation of poly(ADP-ribose) polymerase-1 upon DNA binding revealed by small-angle X-ray scattering.The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets.PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration

P2860

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P2860

A third zinc-binding domain of human poly(ADP-ribose) polymerase-1 coordinates DNA-dependent enzyme activation

http://www.wikidata.org/entity/Q27649201

description

2008 nî lūn-bûn

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2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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A third zinc-binding domain of ...... NA-dependent enzyme activation

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Journal of Biological Chemistry

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A third zinc-binding domain of ...... NA-dependent enzyme activation

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Elizabeth E Rogers

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John M Pascal

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Kristin M Servent

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P2860

XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage

Structural classification of zinc fingers: survey and summary.

Processing of X-ray diffraction data collected in oscillation mode

Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken

Coot: model-building tools for molecular graphics

Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy

Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin

Refinement of macromolecular structures by the maximum-likelihood method

ARP/wARP and automatic interpretation of protein electron density maps

The CCP4 suite: programs for protein crystallography

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4105-14

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3267393

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10.1074/JBC.M708558200

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7

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283

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Marie-France Langelier

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2008-02-15T00:00:00Z

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18055453

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