Results 201 to 210 of about 214,575 (242)

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, P, Adamietz, R, Bredehorst, K, Wielckens   +3 more
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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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ADP-Ribosylating Microbial Toxins

CRC Critical Reviews in Microbiology, 1984
(1984). ADP-Ribosylating Microbial Toxins. CRC Critical Reviews in Microbiology: Vol. 11, No. 4, pp. 273-298.
John W. Foster, Dennis Michael Kinney, Barbara H. Iglewski   +2 more
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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, M, Miwa, H, Saitô, Y, Kanai, M, Ikejima, M, Terada, M, Yamada, T, Utakoji   +7 more
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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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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, J, Plante, G, Beaumont, G G, Poirier   +3 more
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ADP-ribosylation reactions in plants

Biochimie, 1995
Poly ADP-ribosylation is a post-translational modification of protein structure and function that occurs in the nucleus of most eukaryotic cells. Although its function has not been fully elucidated it is thought to have a role in the processing DNA strand breaks.
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Mono ADP-ribosylation and poly ADP-ribosylation of proteins in normal and malignant tissues

Advances in Enzyme Regulation, 1982
Three subclasses of (ADPR)n protein conjugates were quantified from intact tissue; proteins carrying poly(ADPR) and two types of mono(ADPR) protein conjugates, one susceptible, the other resistant to neutral hydroxylamine. Mono(ADPR) conjugates were found in all major compartments of the liver cell although the two subfractions were unevenly ...
K, Wielckens, R, Bredehorst, P, Adamietz, H, Hilz   +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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