Mutational analysis of aspartoacylase: Implications for Canavan Disease

Brain Research

Volumn 1148, Issue 1, 2007, Pages 1-14

  Hershfield, Jeremy R ^a   Pattabiraman, Nagarajan ^b   Madhavarao, Chikkathur N ^a   Namboodiri, M A Aryan ^a  

^a UNIFORMED SERVICES UNIVERSITY OF THE HEALTH SCIENCES   (United States)

^b GEORGETOWN UNIVERSITY   (United States)

Author keywords

Aminoacylase; Aspartoacylase; Canavan Disease; Carboxypeptidase; Homology modeling; N acetyl aspartate; NAA; Zinc metalloprotease

Indexed keywords

ALANINE; ASPARTOACYLASE; CARBOXYL GROUP; CARBOXYPEPTIDASE A; CYSTEINE; DISULFIDE; ZINC;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CANAVAN DISEASE; CONTROLLED STUDY; DISEASE ASSOCIATION; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME SUBSTRATE; MOLECULAR MODEL; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FUNCTION; SEQUENCE HOMOLOGY; WILD TYPE;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; BRAIN CHEMISTRY; CANAVAN DISEASE; CARBOXYPEPTIDASES A; DNA MUTATIONAL ANALYSIS; ENZYME ACTIVATION; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENETIC PREDISPOSITION TO DISEASE; HUMANS; MODELS, MOLECULAR; MUTATION; PHYLOGENY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 34247157359     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2007.02.069     Document Type: Article

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