Aprataxin forms a discrete branch in the HIT (Histidine Triad) superfamily of proteins with both DNA/RNA binding and nucleotide hydrolase activities

Journal of Biological Chemistry

Volumn 281, Issue 20, 2006, Pages 13939-13948

  Kijas, Amanda W ^a   Harris, Janelle L ^a,b   Harris, Jonathan M ^b   Lavin, Martin F ^a,c  

^a ROYAL BRISBANE AND WOMEN'S HOSPITAL   (Australia)

^b QUEENSLAND UNIVERSITY OF TECHNOLOGY   (Australia)

^c UNIVERSITY OF QUEENSLAND   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENZYMES; HYDROLYSIS; MOLECULAR BIOLOGY; RNA; ZINC;

APRATAXIN; HAIRPIN; HISTIDINE TRIAD (HIT); SPINOCEREBELLAR ATAXIA;

GENETIC ENGINEERING;

DOUBLE STRANDED DNA; DOUBLE STRANDED RNA; HISTIDINE; HYDROLASE; NUCLEIC ACID BINDING PROTEIN; PROTEIN APRATAXIN; RECOMBINANT PROTEIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; ZINC;

ARTICLE; DNA DAMAGE; DNA PROTEIN COMPLEX; DNA REPAIR; DNA STRUCTURE; ENZYME ACTIVITY; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN EXPRESSION; PROTEIN RNA BINDING; SEQUENCE ANALYSIS;

DINUCLEOSIDE PHOSPHATES; DNA; DNA REPAIR; DNA, SINGLE-STRANDED; DNA-BINDING PROTEINS; HISTIDINE; HUMANS; HYDROLASES; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; RNA; RNA, DOUBLE-STRANDED; SACCHAROMYCES CEREVISIAE;

ATAXIA;

EID: 33744937625     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M507946200     Document Type: Article

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