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 absolute 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. rules of Cytotoxic T telephone services via a GPI-anchored Ecto-ADP-ribosyltransferase; J. Wang, et al.Mono-ADP-ribosylation inOther Animal Tissues. An ADP-Ribosyltransferase from Bovine Erythrocytes it appears 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 studies. Index.
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Additional resources for ADP-Ribosylation in Animal Tissues: Structure, Function, and Biology of Mono (ADP-ribosyl) Transferases and Related Enzymes
1 reversibly proceeding in intact rat lymphocytes. 1. Bioi. Chern. 270: 22747-22751. 4 CRYSTAL STRUCTURE OF DIPHTHERIA TOXIN BOUND TO NICOTINAMIDE ADENINE DINUCLEOTIDE * Charles E. 3"\ resolution. NAD binds to a cleft on the surface of the catalytic (C) domain of DT, interacting closely with the side chains of Tyr54, Tyr65, His21, Thr23, and Glu 48. The carboxylate group of Glu 148 of DT lies approximately 4"\ from the scissile, N-glycosidic bond ofNAD, suggesting a possible catalytic role for Glu 148 in stabilizing a positively charged oxocarbonium intermediate.
S. J. Stanley. 1981. Histone-dependent and histone-independent forms of an ADP-ribosyltransferase from human and turkey erythrocytes. Proc. Natl. Acad. Sci. USA. 78: 4809-4812. 32 J. Moss et al. 8. , S. J. Stanley, & J. C. Osborne Jr. 1981. Effect of self-association on activity of an ADP-ribosyltransferase from turkey erythrocytes. J. Bioi. Chern. 256: 11452-11456. 9. , J. C. Osborne Jr, & S. J. Stanley. 1984. Activation of an erythrocyte NAD:arginine ADP-ribosyltransferase by lysolecithin and nonionic and zwitterionic detergents.
1.. M. Molinete. G. Gradwoh!. F. Simonin, & G. de Murcia. 1989. Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA. Biol. 21(): 229-233 14. Chatterjee S.. F. Cheng. J. Berger. 1991. Alkylating agent hypersensitivity in poly(adenosine diphosphate-ribose)polymerase deficient cell lines. Cancer Commun. 3: 71-75; 15. , M. Miiller. K. Jacobson. J. L. Coyle. L. Jacobson, & A. Biirkle. 1995. Transdominant inhibition of poly-ADP-ribosylation sensitizes cells against g-irradiation and NMNG but does not limit DNA replication of a polyomavirus replicon.
ADP-Ribosylation in Animal Tissues: Structure, Function, and Biology of Mono (ADP-ribosyl) Transferases and Related Enzymes by Friedrich Haag, Friedrich Koch-Nolte