Results 1 to 10 of about 40,918 (202)

Ubiquitin pathway blockade reveals endogenous ADP-ribosylation marking PARP7 and AHR for degradation [PDF]

The EMBO Journal
ADP-ribosylation is an important protein post-translational modification catalysed by a family of PARP enzymes in humans and is involved in DNA damage and immunity among other processes.
Andrii Gorelik, Nina Đukić, Rebecca Smith, Chatrin Chatrin, Osamu Suyari, Jason Matthews, Ivan Ahel   +6 more
doaj   +2 more sources

Global remodeling of ADP-ribosylation by PARP1 suppresses influenza A virus infection [PDF]

Nature Communications
ADP-ribosylation is a highly dynamic and fully reversible post-translational modification performed by PARP enzymes that modulates protein function, abundance, localization, and turnover. Here we show that PARPs mount an antiviral response to influenza A
Zhenyu Zhang, Isabel Uribe, Kaitlin A. Davis, Robert L. McPherson, Gloria P. Larson, Mohsen Badiee, Vy Tran, Mitchell P. Ledwith, Elizabeth M. Feltman, Shuǐqìng Yú, Yíngyún Caì, Che-Yuan Chang, Xingyi Yang, Zhuo Ma, Paul Chang, Jens H. Kuhn, Anthony K. L. Leung, Andrew Mehle   +17 more
doaj   +2 more sources

ADP-ribosylation of NuMA promotes DNA single-strand break repair and transcription

Cell Reports
Summary: Single-strand breaks (SSBs) are prevalent DNA lesions implicated in genome instability. The nuclear mitotic apparatus protein (NuMA) has been reported to promote SSB repair (SSBR) and regulate transcription following oxidative stress.
Arwa A. Abugable, Chunyan Liao, Sarah Antar, Matthew Dowson, Sherif F. El-Khamisy   +4 more
doaj   +2 more sources

Control of replication and gene expression by ADP-ribosylation of DNA in Mycobacterium tuberculosis [PDF]

The EMBO Journal
Mycobacterium tuberculosis maintains long-term infections characterised by the need to regulate growth and adapt to contrasting in vivo environments. Here we show that M.
Rachel E Butler, Marion Schuller, Ritu Jaiswal, Jayanta Mukhopadhyay, Jim Barber, Suzie Hingley-Wilson, Emily Wasson, Alexassander Couto Alves, Ivan Ahel, Graham R Stewart   +9 more
doaj   +2 more sources

Reversing ADP-ribosylation

eLife, 2017
The modification of serines by molecules of ADP-ribose plays an important role in signaling that the DNA in a cell has been damaged and needs to be repaired.
Giuliana Katharina Moeller, Gyula Timinszky   +1 more
doaj   +3 more sources

Roles of Asp179 and Glu270 in ADP-Ribosylation of Actin by Clostridium perfringens Iota Toxin. [PDF]

PLoS ONE, 2015
Clostridium perfringens iota toxin is a binary toxin composed of the enzymatically active component Ia and receptor binding component Ib. Ia is an ADP-ribosyltransferase, which modifies Arg177 of actin.
Alexander Belyy, Irina Tabakova, Alexander E Lang, Thomas Jank, Yury Belyi, Klaus Aktories   +5 more
doaj   +3 more sources

Ayurvedic Phytochemicals in Oncology: ADP-Ribosylation as a Molecular Nexus. [PDF]

Cells
Reddy GSVSR, Nandy SK, Cherukuri P, Samanta K, Kar P.   +4 more
europepmc   +3 more sources

Sequential ADP‐ribosylation pattern of nucleosomal histones [PDF]

European Journal of Biochemistry, 1985
The pattern of nucleosomal histones poly(ADP‐ribosyl)ation is changed under conditions which affect the poly(ADP‐ribosyl)ation state of the enzyme. At low NAD concentrations the enzyme can poly(ADP‐ribosyl)ate histones H1 and H1°, H2A, A2A, and H2B. However at NAD concentrations above 10 μM the enzyme preferentially poly(ADP‐ribosyl)ates histone H1 to ...
Ann Huletsky, Claude Niedergang, André Fréchette, Rémy A. Aubin, Alain Gaudreau, Guy G. Poirier   +5 more
openalex   +4 more sources

Specificity of DNA ADP-Ribosylation Reversal by NADARs [PDF]

Toxins
Recent discoveries establish DNA and RNA as bona fide substrates for ADP-ribosylation. NADAR (“NAD- and ADP-ribose”-associated) enzymes reverse guanine ADP-ribosylation and serve as antitoxins in the DarT-NADAR operon.
Bara Cihlova, Yang Lu, Andreja Mikoč, Marion Schuller, Ivan Ahel   +4 more
doaj   +2 more sources

Poly-ADP-ribosylation modulated by poly(ADP-ribose) polymerase 1 is associated with glucose metabolism in colorectal cancer cells. [PDF]

Transl Oncol
Zhang C, Wang P, Yu J, Yuan J, Zhang L, Li M.   +5 more
europepmc   +2 more sources