Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins.

Marsischky, G T; Wilson, B A; Collier, R J

Marsischky, G T; Wilson, B A; Collier, R J.

Affiliation

Marsischky GT; Department of Microbiology and Molecular Genetics, Harvard Medical School, Shipley Institute of Medicine, Boston, Massachusetts 02115.

J Biol Chem ; 270(7): 3247-54, 1995 Feb 17.

Article in En | MEDLINE | ID: mdl-7852410

Subject(s)

ADP Ribose Transferases; Diphtheria Toxin/chemistry; Glutamic Acid; Point Mutation; Poly(ADP-ribose) Polymerases/chemistry; Poly(ADP-ribose) Polymerases/metabolism; Adenosine Diphosphate Ribose/metabolism; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Carrier Proteins/chemistry; Cattle; Chickens; DNA Primers; Humans; Maltose-Binding Proteins; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Poly(ADP-ribose) Polymerases/biosynthesis; Rats; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Xenopus

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Collection: 01-internacional Database: MEDLINE Main subject: Poly(ADP-ribose) Polymerases / ADP Ribose Transferases / Point Mutation / Glutamic Acid / Diphtheria Toxin Limits: Animals / Humans Language: En Journal: J Biol Chem Year: 1995 Document type: Article Country of publication: United States

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