Results 41 to 50 of about 615,106 (215)

NAD+ analog reveals PARP-1 substrate-blocking mechanism and allosteric communication from catalytic center to DNA-binding domains

Nature Communications, 2018
Poly(ADP-ribose) polymerases (PARPs) catalyse ADP-ribose posttranslational modifications using NAD+ as a substrate. Here, the authors present the crystal structure of PARP-1 bound to the non-hydrolyzable NAD+ analog BAD and provide insights into the ...
Marie-France Langelier, Levani Zandarashvili, Pedro M. Aguiar, Ben E. Black, John M. Pascal   +4 more
doaj   +1 more source

VERO cells harbor a poly-ADP-ribose belt partnering their epithelial adhesion belt [PDF]

PeerJ, 2014
Poly-ADP-ribose (PAR) is a polymer of up to 400 ADP-ribose units synthesized by poly-ADP-ribose-polymerases (PARPs) and degraded by poly-ADP-ribose-glycohydrolase (PARG).
Laura Lafon-Hughes, Salomé C. Vilchez Larrea, Alejandra Kun, Silvia H. Fernández Villamil   +3 more
doaj   +2 more sources

Methods for Purification of Proteins Associated with Cellular Poly(ADP-Ribose) and PARP-Specific Poly(ADP-Ribose)

, 2011
available in PMC 2012 November 09Poly(ADP-ribose) (pADPr) is a posttranslational modification that regulates protein function through two major mechanisms: covalent modification of acceptor proteins and noncovalent binding of proteins to pADPr.
Leung, Anthony, Jennifer E. Rood, Rood, Jennifer E., Paul Chang, Anthony K. L. Leung, Chang, Paul   +5 more
core   +1 more source

Whole proteome analysis of human tankyrase knockout cells reveals targets of tankyrase-mediated degradation

Nature Communications, 2017
Tankyrase 1 and 2 are poly(ADP-ribose) polymerases that mark proteins for degradation, but there is a current lack of knowledge about their distinct functions and substrates.
Amit Bhardwaj, Yanling Yang, Beatrix Ueberheide, Susan Smith   +3 more
doaj   +1 more source

Poly(ADP-Ribose) Glycohydrolase (PARG) vs. Poly(ADP-Ribose) Polymerase (PARP) – Function in Genome Maintenance and Relevance of Inhibitors for Anti-cancer Therapy

Frontiers in Molecular Biosciences, 2020
Poly(ADP-ribose) polymerases (PARPs) are a family of enzymes that catalyze the addition of poly(ADP-ribose) (PAR) subunits onto themselves and other acceptor proteins.
Daniel Harrision, Polly Gravells, Ruth Thompson, Helen E. Bryant   +3 more
doaj   +1 more source

The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation

Viruses, 2020
Macrodomains, enzymes that remove ADP-ribose from proteins, are encoded by several families of RNA viruses and have recently been shown to counter innate immune responses to virus infection.
Yousef M. O. Alhammad, Anthony R. Fehr
doaj   +1 more source

An assay to measure poly(ADP ribose) glycohydrolase (PARG) activity in cells [version 2; referees: 2 approved]

F1000Research, 2016
After a DNA damage signal multiple polymers of ADP ribose attached to poly(ADP) ribose (PAR) polymerases (PARPs) are broken down by the enzyme poly(ADP) ribose glycohydrolase (PARG).
Dominic I. James, Stephen Durant, Kay Eckersley, Emma Fairweather, Louise A. Griffiths, Nicola Hamilton, Paul Kelly, Mark O'Connor, Kerry Shea, Ian D. Waddell, Donald J. Ogilvie   +10 more
doaj   +1 more source

Crocetin antagonizes parthanatos in ischemic stroke via inhibiting NOX2 and preserving mitochondrial hexokinase-I

Cell Death and Disease, 2023
Parthanatos is one of the major pathways of programmed cell death in ischemic stroke characterized by DNA damage, poly (ADP-ribose) polymerases (PARP) activation, and poly (ADP-ribose) (PAR) formation.
Hao Wu, Ying Li, Qian Zhang, Hanxun Wang, Wenyu Xiu, Pu Xu, Yujie Deng, Wanxu Huang, Dan Ohtan Wang   +8 more
doaj   +1 more source

PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome

Nature Communications, 2019
The poly(ADP-ribose) polymerases play a key role in maintaining genomic integrity by detecting DNA damage and mediating repair. Here the authors characterize the kinetics of PARP1 binding to a variety of nucleosomes harbouring DNA double-strand breaks.
Deepti Sharma, Louis De Falco, Sivaraman Padavattan, Chang Rao, Susana Geifman-Shochat, Chuan-Fa Liu, Curt A. Davey   +6 more
doaj   +1 more source

Loss of IGF‐1R impairs DNA‐PKcs recruitment to chromatin leading to defective end‐joining

Molecular Oncology, EarlyView.
IGF‐1R promotes radioresistance by facilitating DNA‐PKcs recruitment to chromatin, enabling non‐homologous end‐joining (NHEJ) repair of double‐strand breaks. Inhibition or loss of IGF‐1R disrupts this recruitment to damage sites, driving compensatory reliance on microhomology‐mediated end‐joining (MMEJ) repair.
Matthew O. Ellis, Jack V. Mills, Wojciech Niedzwiedz, Valentine M. Macaulay   +3 more
wiley   +1 more source