PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.
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 cancerPoly(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' mechanismSynthesis, preliminarily biological evaluation and molecular docking study of new Olaparib analogues as multifunctional PARP-1 and cholinesterase inhibitors
P2860
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P2860
PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.
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
P2093
P2860
P1433
P1476
PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain.
@en
P2093
Amanda A Riccio
Ben E Black
Connie D Cao
Jamie E DeNizio
Jamin D Steffen
John M Pascal
Marie-France Langelier
Michael McCauley
P2860
P304
P356
10.1016/J.MOLCEL.2015.10.013
P577
2015-11-24T00:00:00Z