Protein glycation in vivo: Functional and structural effects on yeast enolase

Biochemical Journal

Volumn 416, Issue 3, 2008, Pages 317-325

  Gomes, Ricardo A ^a   Oliveira, Luis M A ^a,b   Silva, Mariana ^a   Ascenso, Carla ^b   Quintas, Alexandre ^b   Costa, Gonçalo ^c   Coelho, Ana V ^c,d   Sousa Silva, Marta ^a   Ferreira, António E N ^a   Ponces Freire, Ana ^a   Cordeiro, Carlos ^a  

^a UNIVERSITY OF LISBON   (Portugal)

^b INSTITUTO SUPERIOR DE CIÊNCIAS DA SAÚDE EGAS MONIZ   (Portugal)

^c INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^d UNIVERSITY OF ÉVORA   (Portugal)

Author keywords

Enolase; Mass spectrometry (MS); Methylglyoxal; Methylglyoxal derived advanced glycation end product (MAGE); Protein glycation; Protein structure

Indexed keywords

ENZYME ACTIVITY; MASS SPECTROMETRY; NEURODEGENERATIVE DISEASES; PHYSIOLOGY; YEAST;

ADVANCED GLYCATION END PRODUCTS; ENOLASE; GLYCATION; METHYLGLYOXAL; PROTEIN STRUCTURES;

GLYCOSYLATION;

ENOLASE; METHYLGLYOXAL; ADVANCED GLYCATION END PRODUCT; ARGININE; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME STABILITY; IN VIVO STUDY; ION CYCLOTRON RESONANCE MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; GLYCOSYLATION; HUMAN; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SEQUENCE; ARGININE; ENZYME STABILITY; GLYCOSYLATION; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOPYRUVATE HYDRATASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 58949095221     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080632     Document Type: Article

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