ADP-Ribosylation: Metabolic Effects and Regulatory Functions
(Sprache: Englisch)
Considering the current interest in cellular regulation and intracellular signalling systems, it is surprising that the contribution of ADP-ribosylation reactions to the modulation of a variety of specific cell processes, in parallel with other...
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Klappentext zu „ADP-Ribosylation: Metabolic Effects and Regulatory Functions “
Considering the current interest in cellular regulation and intracellular signalling systems, it is surprising that the contribution of ADP-ribosylation reactions to the modulation of a variety of specific cell processes, in parallel with other post-translational modifications such as phosphorylation, has not been generally recognized. While it is not feasible to cover all aspects of ADP-ribosylation, the thirty-one articles contained in this volume provide a valuable overview of recent progress in the field within the context of cell control mechanisms. For the convenience of the reader, the various topics have been grouped into several sections: (a) poly(ADP-ribosyl)ation; (b) mono-ADP-ribosylation; (c) toxin mono-ADP-ribosylation; (d) inhibitors and activators; (e) protein modification with ADP-ribose and its analogues; and (f) non-modification forms of ADP-ribose. The contents of the individual chapters reflect the ideas of the contributors, many of whom have spent their careers attempting to resolve the biological functions of ADP-ribosylation. We hope that this publication will serve as a useful reference for those investigators that are new to the area as well as those who are actively studying ADP-ribosylation. Inhaltsverzeichnis zu „ADP-Ribosylation: Metabolic Effects and Regulatory Functions “
I: Historical perspective.- Poly(ADP-ribose): Historical perspective.- II: Poly(ADP-ribosyl)ation A. Structure and enzymology of poly(ADP-ribose) polymerase.- Structure and function of poly(ADP-ribose) polymerase.- Poly(ADP-ribose) polymerase: Structural conservation among different classes of animals and its implications.- Enzymology of ADP-ribose polymer synthesis.- Interaction of poly(ADP-ribose)polymerase with DNA polymerase ?.- Poly(ADP-ribose) catabolism in mammalian cells.- Histone shuttling by poly ADP-ribosylation.- Growth-phase-dependent response to DNA damage in poly(ADP-ribose) polymerase deficient cell lines: basis for a new hypothesis describing the role of poly(ADP-ribose) polymerase in DNA replication and repair.- The function of poly (ADP-ribosylation) in DNA breakage and rejoining.- Poly(ADP-ribose) polymerase gene on chromosome 1q: Early role in differentiation linked replication; gene on human chromosome 13q: Marker of carcinogenesis.- Poly(ADP-ribose) polymerase activity in intact or permeabilized leukocytes from mammalian species of different longevity.- ADP-ribosylation and gene expression.- Transcriptional regulation and autoregulation of the human gene for ADP-ribosyltransferase.- III: Mono(ADP-ribosylation).- Vertebrate mono-ADP-ribosyltransferases.- Target protein for eucaryotic arginine-specific ADP-ribosyltransferase.- ADP-ribosylarginine hydrolases.- Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes.- Cellular ADP-ribosylation of Elongation Factor 2.- Characterization of botulinum C3-catalyzed ADP- ribosylation of rho proteins and identification of mammalian C3-like ADP-ribosyltransferase.- ADP-rybosylation of the molecular chaperone GRP78/BiP.- IV: Toxin mono-ADP-ribosylation.- Diphtheria toxin-relatedcytokine fusion proteins: Elongation factor 2 as a target for the threatment of neoplastic disease.- ADP-ribosylation factors: a family of ?20-kDa guanine nucleotide-binding proteins that activate cholera
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toxin.- Clostridial ADP-ribosylating toxins: effects on ATP and GTP-binding proteins.- Common structure of the catalytic sites of mammalian and bacterial toxin ADP- ribosyltransferases.- V: Inhibitors and activators of ADP-ribosylation.- Inhibitors and activators of ADP-ribosylation reactions.- VI: Derivation of proteins with ADP-ribose, NAD and their analogues.- Nitric oxide and NAD-dependent protein modification.- Glycation of proteins by ADP-ribose.- DeoxyNAD and deoxyADP-ribosylation of proteins.- Enzymatic and nonenzymatic ADP-ribosylation of cysteine.- VII: Cyclic ADP-ribose, NAD hydrologis and ADP-ribose synthesis.- Cyclic ADP-ribose: A calcium mobilizing metabolite of NAD+.- NAD glycohydrolases: A possible function in calcium homeostasis.- NAD hydrolysis: Chemical and enzymatic mechanisms.- Index to Volume 138.
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Bibliographische Angaben
- 2012, Softcover reprint of the original 1st ed. 1994, VI, 255 Seiten, Maße: 21 x 28 cm, Kartoniert (TB), Englisch
- Herausgegeben: Joel Moss, Peter Zahradka
- Verlag: Springer, Berlin
- ISBN-10: 1461361206
- ISBN-13: 9781461361206
Sprache:
Englisch
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