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Regulation by ADP-ribosylation

Trends in Cell Biology, 1995
78 41 KLINGENSMITH, 1.1 NOLL, E. and PERRIMON, N. (1989) Dev. 44 LOWE. 5. W., SCHMITT, E. M., SMITH, 5. W., Bid. 134, 130-14s OSBORNE, 8. A. and JACKS, T. (1993) Nature 362, 42 BONINI, N. M., LEISERON, W. M. and BENZER, 5. (1993) Celi 847-849 72, 3799395 45 CLARKE, A. R. et of. (1993) Nature 362, 849-852 43 BATE, M., GOODMAN, C. 5. and SPITZER, N.
Murcia, G, Jacobson, M, Shall, S
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ADP-ribosylation reactions

Biochimie, 1995
ADP-ribosylation reactions have been studied now for over 30 years. They came to light originally in studies of some bacterial toxins, which turned out to be mono-ADP-ribosyl transferases. Subsequently, endogenous mono-ADP-ribosyltransferases were discovered.
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Detecting ADP-Ribosylation in RNA

2021
ADP-ribosylation is a widespread reversible chemical modification of macromolecular targets. Protein ADP-ribosylation has been widely studied and plays a vital role in the regulation of several biological processes. In recent years there has been increasing interest in alternative ADP-ribosylation targets such as nucleic acids-DNA and RNA.
Deeksha, Munnur, Ivan, Ahel
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ADP-ribosylation of nuclear proteins

Advances in Enzyme Regulation, 1979
Covalent modification of nuclear proteins by mono ADP-ribosylation and poly ADP-ribosylation was studied in various tissues and under various growth conditions with the aid of a newly developed radioimmunoassay. Two types of (ADPR)n protein conjugates were found in vitro and in intact tissues which could be differentiated by their sensitivity towards ...
H, Hilz   +3 more
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ADP-ribosylation of rye histones

Canadian Journal of Biochemistry, 1980
Chromatin from etiolated rye seedlings synthesized protein-bound, acid-insoluble material from [3H]NAD, presumably poly(ADP-ribose). [3H]ADP-ribosylated histone fractions were isolated from crude chromatin and characterized by gel electrophoresis and exclusion chromatography.
A, Laroche   +3 more
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Poly ADP-Ribosylation of Protein

1983
Publisher Summary This chapter discusses poly ADP-ribosylation of protein. ADP-ribosylation is a postsynthetic modification of protein that involves the covalent attachment of the ADP-ribose moiety of NAD to specific amino-acid residues or to another ADP-ribose moiety to form a poly(ADP-ribose) molecule.
P H, Pekala, J, Moss
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Poly(ADP-ribosylation) and apoptosis

Molecular and Cellular Biochemistry, 1999
Poly(ADP-ribosylation) is a post-translational modification playing a relevant role in DNA damage recovery, DNA replication and viral integration. Several reports also suggest a modulation of this process during cell death by apoptosis. The aim of this review is to discuss the possible involvement of poly(ADP-ribosylation) during apoptosis, by dealing ...
A I, Scovassi, G G, Poirier
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Studies of nuclear ADP-ribosylation

Advances in Enzyme Regulation, 1980
Abstract Recent studies on poly(ADP-ribose) are reviewed. Poly(ADP-ribose) was shown to have α (1″ → 2′) ribose-ribose bonds. High molecular weight poly(ADP-ribose) with a branched structure was demonstrated. The structure of the branch linkage was determined as 2″-[1′-ribosyl-2″ (1‴-ribosyl)]-adenosine 5′,5″,5‴-tris(phosphate).
T, Sugimura   +7 more
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Deciphering ADP-ribosylation signalling

Nature Reviews Molecular Cell Biology, 2023
Edoardo José Longarini, Helen Dauben
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ADP-ribosylation and gene expression

Molecular and Cellular Biochemistry, 1994
Gene expression can be defined as the conversion of information existing in a molecule of DNA into a mature RNA or protein product and each step in the process, which requires the concerted action of several macromolecules for completion, may be perturbed by the post-translational modification of specific proteins with ADP-ribose.
P, Zahradka, L, Yau
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