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Poly (ADP-Ribose) and ADP-Ribosylation of Proteins
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Description
Publisher Summary This chapter analyzes poly(ADP-ribose) and ADP-ribosylation of proteins. Poly(ADP-ribose) and the ADP-ribosylation of proteins constitute a novel type of covalent modification of proteins. They are ubiquitously distributed in nature and are implicated in the regulation of cell proliferation, protein synthesis, and DNA as well as RNA metabolism. This type of post-translational modification is unique because NAD, nicotinamide adenine dinucleotide, whose primary function is an electron carrier in biological oxidation, invariably provides the ADP-ribosyl moiety, which is transferred on to a protein molecule. The ADP-ribosyl unit thus, covalently attached to a protein acceptor is present as either a monomer or a polymer as in the case of the nuclear system. This chapter also summarizes developments in this field of research and some experimental results. It reviews briefly, mono ADP-ribosylation of proteins, in which only a single ADP-ribosyl moiety is transferred to a protein acceptor. It also covers a more complex reaction, poly(ADP-ribose) in nuclei, in which the ADP-ribosyl units are polymerized.
Journal
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- Annual Review of Biochemistry
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Annual Review of Biochemistry 46 (1), 95-116, 1977-06
Annual Reviews
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Keywords
- DNA Replication
- Poly Adenosine Diphosphate Ribose
- Glycoside Hydrolases
- Nucleoside Diphosphate Sugars
- Phosphoric Diester Hydrolases
- Bacterial Toxins
- Proteins
- Adenosine Diphosphate Sugars
- DNA-Directed RNA Polymerases
- Peptide Elongation Factors
- Coliphages
- Mitochondria
- Isomerism
- Pseudomonas
- Escherichia coli
- Animals
- Diphtheria Toxin
- Poly(ADP-ribose) Polymerases
Details 詳細情報について
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- CRID
- 1363670321194387712
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- ISSN
- 15454509
- 00664154
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- PubMed
- 197884
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- Data Source
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- Crossref
- OpenAIRE