منابع مشابه
A new facet of ADP-ribosylation reactions: SIRTs and PARPs interplay.
Nicotinamide Adenine Dinucleotide (NAD⁺) is known mainly as coenzyme of redox reactions for energy transduction and is consumed as substrate in regulatory reactions removing nicotinamide and producing ADP-ribose. Several families of ADP-ribose synthesizing enzymes use NAD⁺ as substrate and control processes like DNA repair, replication and transcription, chromatin structure, the activity of G-p...
متن کاملReversing ADP-ribosylation
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.
متن کاملSerine ADP-Ribosylation Depends on HPF1
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 the DNA damage response. However, the biochemical basis underlying this serine modification remained unknown. Here we report that serine ADPr is strict...
متن کاملADP-ribosylation of nuclear proteins.
ADP-ribosylation can be defined as the postsynthetic modification of protein by the covalent attachment of the ADP-ribose moiety of NAD+. ADP-ribosylation of elongation-factor Tu is responsible for the inhibition of protein synthesis by both diptheria and Pseudomonas aeroginosa toxins (Hilz & Stone, 1976). The activation of membrane adenylate cyclase by cholera toxin is thought to occur by ADP-...
متن کاملProteasome Regulation by ADP-Ribosylation
Protein degradation by the ubiquitin-proteasome system is central to cell homeostasis and survival. Defects in this process are associated with diseases such as cancer and neurodegenerative disorders. The 26S proteasome is a large protease complex that degrades ubiquitinated proteins. Here, we show that ADP-ribosylation promotes 26S proteasome activity in both Drosophila and human cells. We ide...
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ژورنال
عنوان ژورنال: Genes & Development
سال: 2020
ISSN: 0890-9369,1549-5477
DOI: 10.1101/gad.336420.120