Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: Studies on the structure and chaperone function using mutant mimics

PLoS ONE

Volumn 7, Issue 1, 2012, Pages

  Nagaraj, Ram H ^a   Panda, Alok Kumar ^b   Shanthakumar, Shilpa ^a   Santhoshkumar, Puttur ^c   Pasupuleti, NagaRekha ^a   Wang, Benlian ^a   Biswas, Ashis ^b  

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

^b INDIAN INSTITUTE OF TECHNOLOGY BHUBANESWAR   (India)

^c University of Missouri   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ALANINE; ALPHA CRYSTALLIN; ARGININE; BETA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN 27; HYDROIMIDAZOLONE; METHYLGLYOXAL; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG; IMIDAZOLE DERIVATIVE; IMIDAZOLONE; RECOMBINANT PROTEIN;

AGING; AMINO ACID SUBSTITUTION; ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; BINDING SITE; CATARACT; CONTROLLED STUDY; MOLECULAR WEIGHT; OLIGOMERIZATION; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; QUANTITATIVE ANALYSIS; THERMODYNAMICS; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; DRUG EFFECT; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; SPECTROFLUOROMETRY;

ALPHA-CRYSTALLIN A CHAIN; ALPHA-CRYSTALLIN B CHAIN; AMINO ACID SEQUENCE; ARGININE; BINDING SITES; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HSP27 HEAT-SHOCK PROTEINS; IMIDAZOLES; KINETICS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRUVALDEHYDE; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 84855826057     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030257     Document Type: Article

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