Effect of methylglyoxal modification on stress-induced aggregation of client proteins and their chaperoning by human αA-crystallin

Biochemical Journal

Volumn 409, Issue 3, 2008, Pages 771-777

  Biswas, Ashis ^a,c   Wang, Benlian ^a,b   Miyagi, Masaru ^a,b   Nagaraj, Ram H ^a,b  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b CASE WESTERN RESERVE UNIVERSITY   (United States)

^c LERNER RESEARCH INSTITUTE   (United States)

Author keywords

A crystallin; Argpyrimidine; Chaperone; Client protein aggregation; Human lens; Hydroimidazolone

Indexed keywords

ARGPYRIMIDINE; CHAPERONE; CLIENT PROTEIN AGGREGATION; HUMAN LENS; HYDROIMIDAZOLONE;

AGGLOMERATION; ALCOHOLS; CHEMICAL MODIFICATION; MAMMALS;

PROTEINS;

ALCOHOL DEHYDROGENASE; ALPHA CRYSTALLIN; ALPHA LACTALBUMIN; ARGPYRIMIDINE; GAMMA CRYSTALLIN; HYDROIMIDAZOLONE; INSULIN; METHYLGLYOXAL; PHOSALONE; PYRIMIDINE DERIVATIVE; UNCLASSIFIED DRUG;

AGING; ARTICLE; CHEMICAL MODIFICATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HYDROPHOBICITY; LENS; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; STRESS; TEMPERATURE;

ALPHA-CRYSTALLIN A CHAIN; AMINO ACID SEQUENCE; ANIMALS; CATTLE; HUMANS; INSULIN; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PYRUVALDEHYDE; TEMPERATURE;

EID: 38949167689     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071006     Document Type: Article

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