PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain. - Wikidata - awgldk - TriplyDB

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

http://www.wikidata.org/entity/Q42095016

about

Analyzing structure-function relationships of artificial and cancer-associated PARP1 variants by reconstituting TALEN-generated HeLa PARP1 knock-out cells.Emerging therapies for breast cancer 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.PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes.MEIS homeodomain proteins facilitate PARP1/ARTD1-mediated eviction of histone H1.At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair.What Combined Measurements From Structures and Imaging Tell Us About DNA Damage Responses.Unfolding of core nucleosomes by PARP-1 revealed by spFRET microscopy.Structural Basis of Detection and Signaling of DNA Single-Strand Breaks by Human PARP-1.BRCA Gene Mutations and Poly(ADP-Ribose) Polymerase Inhibitors in Triple-Negative Breast Cancer.Specificity of reversible ADP-ribosylation and regulation of cellular processes.Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation.Anticancer effects of 10-hydroxycamptothecin induce apoptosis of human osteosarcoma through activating caspase-3, p53 and cytochrome c pathways.Inhibited, trapped or adducted: the optimal selective synthetic lethal mix for BRCAness.NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains.Purification of DNA Damage-Dependent PARPs from E. coli for Structural and Biochemical Analysis.The multifunctional protein YB-1 potentiates PARP1 activity and decreases the efficiency of PARP1 inhibitors.Genome-wide and high-density CRISPR-Cas9 screens identify point mutations in PARP1 causing PARP inhibitor resistance.Poly(ADP-ribose) polymerase 1 searches DNA via a 'monkey bar' mechanism Synthesis, preliminarily biological evaluation and molecular docking study of new Olaparib analogues as multifunctional PARP-1 and cholinesterase inhibitors

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P2860

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

http://www.wikidata.org/entity/Q42095016

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

@en

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

@nl

type

label

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

@en

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

@nl

prefLabel

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

@en

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

@nl

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J.MOLCEL.2015.10.013

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P1476

PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.

@en

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Amanda A Riccio

http://www.w3.org/2001/XMLSchema#string

Ben E Black

http://www.w3.org/2001/XMLSchema#string

Connie D Cao

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Jamie E DeNizio

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Jamin D Steffen

http://www.w3.org/2001/XMLSchema#string

John M Pascal

http://www.w3.org/2001/XMLSchema#string

Marie-France Langelier

http://www.w3.org/2001/XMLSchema#string

Michael McCauley

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P2860

Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease

The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres

PHENIX: a comprehensive Python-based system for macromolecular structure solution

A novel endogenous inhibitor of the secreted streptococcal NAD-glycohydrolase.

ARTD1 (PARP1) activation and NAD(+) in DNA repair and cell death

A high-fat diet and NAD(+) activate Sirt1 to rescue premature aging in cockayne syndrome

Chromosomes. CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere.

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

Domain C of human poly(ADP-ribose) polymerase-1 is important for enzyme activity and contains a novel zinc-ribbon motif

Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens -toxin

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755-768

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10.1016/J.MOLCEL.2015.10.013

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5

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60

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Jennine M Dawicki McKenna

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2015-11-24T00:00:00Z

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26626480

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4712911

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