Glyoxalase I polymorphism rs2736654 causing the Ala111Glu substitution modulates enzyme activity-implications for autism

Autism Research

Volumn 4, Issue 4, 2011, Pages 262-270

  Barua, Madhabi ^a   Jenkins, Edmund C ^a   Chen, Wenqiang ^a   Kuizon, Salomon ^a   Pullarkat, Raju K ^a   Junaid, Mohammed A ^a  

^a NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

Author keywords

Advanced glycation endproducts (AGEs); Autism; Glyoxalase I; Methylglyoxal; Receptor for advanced glycation end products (RAGEs); SNP

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; LACTOYLGLUTATHIONE LYASE; METHYLGLYOXAL;

AMINO ACID SUBSTITUTION; ARTICLE; AUTISM; CELL MATURATION; ENZYME ACTIVITY; GENE FREQUENCY; GENETIC SUSCEPTIBILITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; LYMPHOBLASTOID CELL; NERVE CELL; PHOSPHORYLATION; PRIORITY JOURNAL; REGULATORY MECHANISM; RISK FACTOR; SINGLE NUCLEOTIDE POLYMORPHISM; TOXICITY; WESTERN BLOTTING;

ALLELES; ANIMALS; AUTISTIC DISORDER; BLOTTING, WESTERN; CELLS, CULTURED; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENETIC PREDISPOSITION TO DISEASE; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMANS; LACTOYLGLUTATHIONE LYASE; POLYMORPHISM, SINGLE NUCLEOTIDE; PYRUVALDEHYDE; RABBITS; RECEPTORS, IMMUNOLOGIC;

EID: 80052622673     PISSN: 19393792     EISSN: 19393806     Source Type: Journal    
DOI: 10.1002/aur.197     Document Type: Article

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