Cystathionine β-synthase mutations: Effect of mutation topology on folding and activity

Human Mutation

Volumn 31, Issue 7, 2010, Pages 809-819

  Kožich, Viktor ^a   Sokolová, Jitka ^a   Klatovská, Veronika ^a   Krijt, Jakub ^a   Janošík, Miroslav ^a   Jelínek, Karel ^b   Kraus, Jan P ^c  

^a General Teaching Hospital and 1st Medical Faculty of Charles University   (Czech Republic)

^b CHARLES UNIVERSITY   (Czech Republic)

^c Nutrition Obesity Research Center at the University of Colorado   (United States)

Author keywords

CBS; Cystathionine synthase deficiency; E. coli; Folding; Homocysteine; Homocystinuria; Misfolding; Topology

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; TETRAMER; MUTANT PROTEIN;

ALLELE; ARTICLE; CATALYSIS; CONTROLLED STUDY; ESCHERICHIA COLI; GENE ACTIVITY; GENE EXPRESSION; GENE MUTATION; GENE STRUCTURE; GENETIC VARIABILITY; HOMOCYSTINURIA; LOW TEMPERATURE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN QUATERNARY STRUCTURE; CHEMICAL STRUCTURE; CHEMISTRY; COLD; DEFICIENCY; ENZYME ACTIVE SITE; ENZYME STABILITY; ENZYMOLOGY; GENETICS; HUMAN; METABOLISM; MUTATION; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SOLUBILITY; WESTERN BLOTTING;

BLOTTING, WESTERN; CATALYSIS; CATALYTIC DOMAIN; COLD TEMPERATURE; CYSTATHIONINE BETA-SYNTHASE; ENZYME STABILITY; ESCHERICHIA COLI; HOMOCYSTINURIA; HUMANS; MODELS, MOLECULAR; MUTANT PROTEINS; MUTATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SOLUBILITY;

BACTERIA (MICROORGANISMS);

EID: 77954109889     PISSN: 10597794     EISSN: 10981004     Source Type: Journal    
DOI: 10.1002/humu.21273     Document Type: Article

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