Glycerol stimulates innate chaperoning, proteasomal and stress-resistance functions: Implications for geronto-manipulation

Biogerontology

Volumn 9, Issue 4, 2008, Pages 269-282

  Deocaris, Custer C ^a,b   Takano, Syuichi ^c   Priyandoko, Didik ^a   Kaul, Zeenia ^a   Yaguchi, Tomoko ^a   Kraft, David C ^d   Yamasaki, Kazuhiko ^a   Kaul, Sunil C ^a   Wadhwa, Renu ^a  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

^c Mays Cancer Center at UT Health San Antonio   (United States)

^d AARHUS UNIVERSITY   (Denmark)

Author keywords

Chaperone; Geronto modulation; Glycerol; Homeostasis; Mortalin; Proteasome; Protein misfolding; Stress protection

Indexed keywords

CELL PROTEIN; CHAPERONE; GLYCEROL; HEAT SHOCK PROTEIN; PROTEASOME; PROTEIN P53;

AGING; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; AUTOFLUORESCENCE; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVITY; HEAT STRESS; HEAT TOLERANCE; HUMAN; HUMAN CELL; LIFESPAN; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; STRESS; SURVIVAL; WORM;

ANIMALS; CAENORHABDITIS ELEGANS; CELL LINE; CELL PROLIFERATION; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME STABILITY; FIBROBLASTS; GLYCEROL; HEAT; HSP70 HEAT-SHOCK PROTEINS; HUMANS; LONGEVITY; MOLECULAR CHAPERONES; OXIDATIVE STRESS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN DENATURATION; PROTEIN FOLDING; TUMOR SUPPRESSOR PROTEIN P53;

EID: 46749136068     PISSN: 13895729     EISSN: 15736768     Source Type: Journal    
DOI: 10.1007/s10522-008-9136-8     Document Type: Article

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