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Volumn 37, Issue 10-11, 2002, Pages 1257-1262

Chaperone function and chaperone overload in the aged. A preliminary analysis

Author keywords

Chaperone overload; Heat shock proteins; Hsc70; Hsp70; Hsp90; Luciferase; Molecular chaperones; Protein aggregation; Protein denaturation; Stress proteins

Indexed keywords

CHAPERONE; HEAT SHOCK COGNATE PROTEIN 70; LIVER PROTEIN; PROTEIN; PROTEIN HSP90; UNCLASSIFIED DRUG; LUCIFERASE;

EID: 0036814834     PISSN: 05315565     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0531-5565(02)00134-1     Document Type: Conference Paper
Times cited : (69)

References (19)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye-binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 3
    • 0035824663 scopus 로고    scopus 로고
    • Proteasome inhibition in glyoxal-treated fibroblasts and resistance of glycated glucose-6-phosphate dehydrogenase to 20S proteosome degradation in vitro
    • Bulteau A.-L., Verbeke P., Petropoulos I., Chaffotte A.-F., Friguet B. Proteasome inhibition in glyoxal-treated fibroblasts and resistance of glycated glucose-6-phosphate dehydrogenase to 20S proteosome degradation in vitro. J. Biol. Chem. 274:2001;45662-45668.
    • (2001) J. Biol. Chem. , vol.274 , pp. 45662-45668
    • Bulteau, A.-L.1    Verbeke, P.2    Petropoulos, I.3    Chaffotte, A.-F.4    Friguet, B.5
  • 4
    • 0028899440 scopus 로고
    • Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications
    • Cherian M., Abraham E.C. Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. Biochem. Biophys. Res. Commun. 208:1995;675-679.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 675-679
    • Cherian, M.1    Abraham, E.C.2
  • 5
    • 0030586350 scopus 로고    scopus 로고
    • Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat shock protein 90
    • Conconi M., Szweda L.I., Levine R.L., Stadtman E.R., Friguet B. Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat shock protein 90. Arch. Biochem. Biophys. 331:1996;232-240.
    • (1996) Arch. Biochem. Biophys. , vol.331 , pp. 232-240
    • Conconi, M.1    Szweda, L.I.2    Levine, R.L.3    Stadtman, E.R.4    Friguet, B.5
  • 6
    • 0035354581 scopus 로고    scopus 로고
    • A nonconventional role of molecular chaperones: Involvement in the cytoarchitecture
    • Csermely P. A nonconventional role of molecular chaperones: involvement in the cytoarchitecture. News Physiol. Sci. 15:2001;123-126.
    • (2001) News Physiol. Sci. , vol.15 , pp. 123-126
    • Csermely, P.1
  • 7
    • 0035576876 scopus 로고    scopus 로고
    • Chaperone-overload as a possible contributor to 'civilization diseases': Atherosclerosis, cancer, diabetes
    • Csermely P. Chaperone-overload as a possible contributor to 'civilization diseases': atherosclerosis, cancer, diabetes. Trends Genet. 17:2001;701-704.
    • (2001) Trends Genet. , vol.17 , pp. 701-704
    • Csermely, P.1
  • 8
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo A.M., Dice J.F. Age-related decline in chaperone-mediated autophagy. J. Biol. Chem. 275:2000;31505-31513.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 10
    • 0033648159 scopus 로고    scopus 로고
    • Analysis of molecular chaperone activities using in vitro and in vivo approaches
    • Freeman B.C., Michels A., Song J., Kampinga H., Morimoto R.I. Analysis of molecular chaperone activities using in vitro and in vivo approaches. Methods Mol. Biol. 99:2000;393-419.
    • (2000) Methods Mol. Biol. , vol.99 , pp. 393-419
    • Freeman, B.C.1    Michels, A.2    Song, J.3    Kampinga, H.4    Morimoto, R.I.5
  • 12
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.-U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.-U.1
  • 13
    • 0032837150 scopus 로고    scopus 로고
    • Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein
    • Kurucz I., Tombor B., Prechl J., Erdö F., Hegedũs E., Nagy Z., Vitai M., Korányi L., László L. Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein. Cell Stress Chaperones. 4:1999;139-152.
    • (1999) Cell Stress Chaperones , vol.4 , pp. 139-152
    • Kurucz, I.1    Tombor, B.2    Prechl, J.3    Erdö, F.4    Hegedũs, E.5    Nagy, Z.6    Vitai, M.7    Korányi, L.8    László, L.9
  • 16
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman E.R., Berlett B.S. Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab. Rev. 30:1998;225-243.
    • (1998) Drug Metab. Rev. , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 18
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • Wright H.T. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit. Rev. Biochem. Mol. Biol. 26:1991;1-52.
    • (1991) Crit. Rev. Biochem. Mol. Biol. , vol.26 , pp. 1-52
    • Wright, H.T.1
  • 19
    • 0027511556 scopus 로고
    • The effect of age on the synthesis of two heat shock proteins in the hsp70 family
    • Wu B., Gu M.J., Heydari A.R., Richardson A. The effect of age on the synthesis of two heat shock proteins in the hsp70 family. J. Gerontol. 48:1993;B50-B56.
    • (1993) J. Gerontol. , vol.48
    • Wu, B.1    Gu, M.J.2    Heydari, A.R.3    Richardson, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.