Results 21 to 30 of about 214,575 (242)

Serine ADP-Ribosylation Depends on HPF1

Molecular Cell, 2017
Summary ADP-ribosylation (ADPr) regulates important patho-physiological processes through its attachment to different amino acids in proteins. Recently, by precision mapping on all possible amino acid residues, we identified histone serine ADPr marks in ...
Juan JOSÉ Bonfiglio, Pietro FONTANA, Thomas Colby   +2 more
exaly   +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

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

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

Interplay of Histone Marks with Serine ADP-Ribosylation

Cell Reports, 2018
Summary: Serine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1).
Juan JOSÉ Bonfiglio, Evgeniia Prokhorova, Thomas Colby   +2 more
exaly   +3 more sources

Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation

Nature Communications, 2019
ADP-ribose erasing enzymes are increasingly recognized as critical regulators of protein ADP-ribosylation dynamics in living systems. Here, the authors review recent advances in the discovery and characterization of ADP-ribose erasers and discuss their ...
Julia O’Sullivan, Maria Tedim Ferreira, Jean-Philippe Gagné, Ajit K. Sharma, Michael J. Hendzel, Jean-Yves Masson, Guy G. Poirier   +6 more
doaj   +2 more sources

Studying Catabolism of Protein ADP-Ribosylation [PDF]

, 2017
Protein ADP-ribosylation is a conserved posttranslational modification that regulates many major cellular functions, such as DNA repair, transcription, translation, signal transduction, stress response, cell division, aging, and cell death. Protein ADP-ribosyl transferases catalyze the transfer of an ADP-ribose (ADPr) group from the β-nicotinamide ...
Palazzo L., James D. I., Waddell I. D., Ahel I.   +3 more
core   +9 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

ADP Ribosylation [PDF]

Definitions, 2020

semanticscholar   +2 more sources

General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes [PDF]

Toxins
ADP-ribosylation is a ubiquitous modification of proteins and other targets, such as nucleic acids, that regulates various cellular functions in all kingdoms of life.
Hideaki Tsuge, Noriyuki Habuka, Toru Yoshida   +2 more
doaj   +2 more sources