Natural dipeptides as mini-chaperones: Molecular mechanism of inhibition of lens βL-crystallin aggregation

Current Aging Science

Volumn 5, Issue 3, 2012, Pages 236-241

  Dizhevskaya, Antonina K ^a   Muranov, Konstantin O ^b   Boldyrev, Alexander A ^a,c   Ostrovsky, Mikhail A ^b  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b EMANUEL INSTITUTE OF BIOCHEMICAL PHYSICS   (Russian Federation)

^c RESEARCH CENTER OF NEUROLOGY   (Russian Federation)

Author keywords

L crystallin; Anserine; Carnosine related compounds (CRCs); Cataract; Lens; N acetylcarnosine; Protein aggregation

Indexed keywords

ANSERINE; BETA CRYSTALLIN; CARBONYL DERIVATIVE; CARNOSINE; DIPEPTIDE; HISTIDINE; N ACETYLCARNOSINE; UNCLASSIFIED DRUG;

ARTICLE; HYDROPHOBICITY; IN VITRO STUDY; INHIBITION KINETICS; PHOTOCHEMICAL EFFICIENCY; PHOTOCHEMISTRY; PRIORITY JOURNAL; PROTEIN AGGREGATION; SEPARATION TECHNIQUE; ULTRAVIOLET RADIATION;

ANIMALS; ANSERINE; BETA-CRYSTALLINS; CARNOSINE; CATARACT; CATTLE; DIPEPTIDES; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; LENS, CRYSTALLINE; MOLECULAR CHAPERONES; PROTEIN CARBONYLATION; PROTEIN CONFORMATION; ULTRAVIOLET RAYS;

EID: 84874844679     PISSN: 18746098     EISSN: 18746128     Source Type: Journal    
DOI: 10.2174/1874609811205030011     Document Type: Article

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