Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes - Wikidata - awgldk - TriplyDB

Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

http://www.wikidata.org/entity/Q36294865

about

Accessing DNA damage in chromatin: Preparing the chromatin landscape for base excision repair Post-translational modifications of histones that influence nucleosome dynamics ADP-ribosyltransferases and poly ADP-ribosylation Suicidal cross-linking of PARP-1 to AP site intermediates in cells undergoing base excision repair.Automodification switches PARP-1 function from chromatin architectural protein to histone chaperone.Reptin and Pontin oligomerization and activity are modulated through histone H3 N-terminal tail interaction Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation.Genome-Wide Profiling of PARP1 Reveals an Interplay with Gene Regulatory Regions and DNA Methylation.Characterization of the interactions of PARP-1 with UV-damaged DNA in vivo and in vitro Coordinated Regulation of TIP60 and Poly(ADP-Ribose) Polymerase 1 in Damaged-Chromatin Dynamics.In Vitro Chromatin Assembly: Strategies and Quality Control.Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro.Fluorescent sensors of PARP-1 structural dynamics and allosteric regulation in response to DNA damage.PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis.Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response.The rise and fall of poly(ADP-ribose): An enzymatic perspective.TRF1 and TRF2 binding to telomeres is modulated by nucleosomal organization.Unfolding of core nucleosomes by PARP-1 revealed by spFRET microscopy.Poly(ADP-ribose) polymerase 1 escorts XPC to UV-induced DNA lesions during nucleotide excision repair.Biochemical and Biophysical Methods for Analysis of Poly(ADP-Ribose) Polymerase 1 and Its Interactions with Chromatin.Identification of Protein Substrates of Specific PARP Enzymes Using Analog-Sensitive PARP Mutants and a "Clickable" NAD+ Analog.Catalytic-Independent Functions of PARP-1 Determine Sox2 Pioneer Activity at Intractable Genomic Loci.Origins of cancer symposium 2015: posttranslational modifications and cancer.Poly(ADP-ribose) polymerase 1 searches DNA via a 'monkey bar' mechanism

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P2860

Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

http://www.wikidata.org/entity/Q36294865

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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name

Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

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Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

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type

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Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

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Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

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prefLabel

Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

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Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

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P356

JBC.M112.397067

P1433

Journal of Biological Chemistry

P1476

Alternative modes of binding of poly(ADP-ribose) polymerase 1 to free DNA and nucleosomes

@en

P2093

Michael Kramer

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Nicholas J Clark

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Uma M Muthurajan

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P2860

The roles of PARP1 in gene control and cell differentiation

The role of PARP in DNA repair and its therapeutic exploitation

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

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 Basis for DNA Damage-Dependent Poly(ADP-ribosyl)ation by Human PARP-1

The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks

Biophysical analysis and small-angle X-ray scattering-derived structures of MeCP2-nucleosome complexes.

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.

The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity.

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32430-32439

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3463355

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