The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 41, 2006, Pages 15026-15031

  Mueller Dieckmann, Christoph ^a   Kernstock, Stefan ^b   Lisurek, Michael ^c   Von Kries, Jens Peter ^c   Haag, Friedrich ^b   Weiss, Manfred S ^a   Koch Nolte, Friedrich ^b  

^a DESY   (Germany)

^b UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

^c LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

Author keywords

Docking; Glycohydrolase; Posttranslational modification; Protein structure

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE DIPHOSPHATE RIBOSYLHYDROLASE 3; MAGNESIUM ION; UNCLASSIFIED DRUG;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ALPHA HELIX; ANIMAL CELL; APOPTOSIS; ARTICLE; CHOLERA; CONTROLLED STUDY; DIPHTHERIA; DNA REPAIR; ENZYME ACTIVITY; ENZYME STRUCTURE; HUMAN; HUMAN CELL; NONHUMAN; PERTUSSIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STRUCTURE; REACTION ANALYSIS;

ADENOSINE DIPHOSPHATE RIBOSE; AMINO ACID SEQUENCE; BINDING SITES; COMPUTER SIMULATION; GLYCOSIDE HYDROLASES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN;

MAMMALIA;

EID: 33750065699     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0606762103     Document Type: Article

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