ADP-Ribosylation in Animal Tissues: Structure, Function, and by Friedrich Haag, Friedrich Koch-Nolte

By Friedrich Haag, Friedrich Koch-Nolte

Introduction. Mono(ADP-ribosyl)Transferases and comparable Enzymes: rising Gene households; F. Koch-Nolte, F. Haag.Mono-ADP-ribosylationin Prokaryotes. Crystal constitution of Diphtheria Toxin guaranteed to Nicotinamide Adenine Dinucleotide; C.E. Bell, D. Eisenberg.MolecularApproaches to Eukaryotic Mono(ADP-ribosyl)Transferases. series and Structural hyperlinks among far away ADp-ribosyltransferase households; F.Bazan, F. Koch-Nolte.Moni(ADP-ribosyl)Transferases within the ImmuneSystem. law of Cytotoxic T cellphone features through a GPI-anchored Ecto-ADP-ribosyltransferase; J. Wang, et al.Mono-ADP-ribosylation inOther Animal Tissues. An ADP-Ribosyltransferase from Bovine Erythrocytes it sounds as if particular for Cysteine Residues; S. vanHeyningen, B. Saxty.Physiology of GPI-Anchored Proteins. cellphone floor Dynamics of GPI-anchored Proteins; F.R. Maxfield, S. Mayor.Relationship of ADP-Ribosyltransferases to NAD+ Glycohydrolasesand ADP-ribosyl Cyclases. ADp-Ribose in Glycation and Glycoxidation Reactions; E.L. Jacobson, et al.Special Lecture Commemorating theRetirement of Professor Heinz-Gunter Thiele. Appendix. 28 extra Lectures. 24 Poster experiences. Index.

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Extra info for ADP-Ribosylation in Animal Tissues: Structure, Function, and Biology of Mono (ADP-ribosyl) Transferases and Related Enzymes

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Thoracic Soc. 608078. 19. , & J. Moss. 1993. Integrin a7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. 1. Bioi. Chem. 268: 25273-25276. 20. Wang. 1.. E. Nemoto. & G. Dennert. 1996. Regulation of CTL by ecto-nicotinamide adenine dinucleotide H (NAD) involves ADP-ribosylation of a p56 -associated protein. 1. Immunol. 156: 2819-2827. 21. Moss, J.. & M. Vaughan. 1988. ADP-ribosylation of guanyl nucleotide-binding proteins by bacterial toxins.

Apparently primed by the detection of the poly-ADP-ribosylating system in cell nuclei, the Hayaishi group made a good guess in assuming that the NAD+ requirement for the toxin's action was due to an ADP-ribosyltransferase reaction modifying elongation factor 2 (19). Additional examples are listed in Tab II. Complexity of mono-ADP-ribosylation systems increases further, when the covalent modification requires reversibility. It is the merit of Paul Ludden to have provided the first example of a truly regulatory mono-ADP-ribosylation cycle, involving the regulated enzyme, dinitrogenase reductase, an ADP-ribosyltransferase inducing inhibition, and a reactivating glycohydrolase (8).

Lee et a1. Hellmich et a1. Takasawa et a1. Kim et a!. Zocchi et a1. Takasawa et a1. Zhanget a1. Jacobson et a1. Guse et a1. Grimaldi et a1. Pub!. Y Ref. a ) 1989 (25) 1993 (26) 1989/1994 (25,27) 199111992 (27) 1993 (26,27) 1993 (26) 1993 1993 1995 1995 1996 1995 (26,27) (26,27) (28) (29) (30) a) see authors in corresponding sections of cited reviews lyzes a reaction which comes to a halt long before the substrate is used up. It seems strange that a reaction producing a messenger-like metabolite should not go to completion.

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