메뉴 건너뛰기




Volumn 7, Issue 4, 2004, Pages 243-249

The pathology of cellular anti-stress mechanisms: A new frontier

Author keywords

Anti stress mechanisms; Chaperonopathies; Heat shock proteins (Hsp); Molecular chaperones; Protein folding; Stress

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 10; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

EID: 17844398768     PISSN: 10253890     EISSN: None     Source Type: Journal    
DOI: 10.1080/10253890400019706     Document Type: Short Survey
Times cited : (29)

References (95)
  • 1
    • 0344443774 scopus 로고    scopus 로고
    • BAG-1 - A nucleotide exchange factor of Hsc70 with multiple cellular functions
    • Alberti, S., Esser, C. and Hoehfeld, J. (2003) BAG-1-a nucleotide exchange factor of Hsc70 with multiple cellular functions, Cell Stress Chaperones 8, 225-231.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 225-231
    • Alberti, S.1    Esser, C.2    Hoehfeld, J.3
  • 3
    • 0037177814 scopus 로고    scopus 로고
    • Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C
    • Bartolini, F., Bhamidipatis, A., Thomas, S., Schwahn, U., Lewis, S.A. and Cowan, N.J. (2002) Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C, J. Biol. Chem. 277, 14629-14634.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14629-14634
    • Bartolini, F.1    Bhamidipatis, A.2    Thomas, S.3    Schwahn, U.4    Lewis, S.A.5    Cowan, N.J.6
  • 4
    • 0037175395 scopus 로고    scopus 로고
    • Missense mutation in the tubulin-specific chaperone e (Tcbe) gene in the mouse mutant progressive motor neuronophathy, a model of human motoneuron disease
    • Boemmel, H., Xie, G., Rossoll, W., Wiese, S., Jablonka, S., Boehm, T. and Sendtner, M. (2002) Missense mutation in the tubulin-specific chaperone E (Tcbe) gene in the mouse mutant progressive motor neuronophathy, a model of human motoneuron disease, J. Cell Biol. 159, 563-569.
    • (2002) J. Cell Biol. , vol.159 , pp. 563-569
    • Boemmel, H.1    Xie, G.2    Rossoll, W.3    Wiese, S.4    Jablonka, S.5    Boehm, T.6    Sendtner, M.7
  • 5
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in alpha-beta-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova, M.P., Yaron, O., Huang, Q., Ding, L., Haley, D.A., Stewart, P.L. and Horwitz, J. (1999) Mutation R120G in alpha-beta-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function, Proc. Natl Acad. Sci. USA 96, 6137-6142.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7
  • 6
    • 1342271074 scopus 로고    scopus 로고
    • Some properties of human small heat shock protein Hsp20 (HspB6)
    • Bukach, O.V., Seit-Nebi, A.S., Marston, S.B. and Gusev, N.B. (2004) Some properties of human small heat shock protein Hsp20 (HspB6), Eur. J. Biochem. 271, 291-302.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 291-302
    • Bukach, O.V.1    Seit-Nebi, A.S.2    Marston, S.B.3    Gusev, N.B.4
  • 7
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • Bukau, B., Deuerling, E., Pfund, C. and Craig, E.A. (2000) Getting newly synthesized proteins into shape, Cell 101, 119-122.
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 8
    • 0043028205 scopus 로고    scopus 로고
    • What is a co-chaperone
    • Caplan, A.J. (2003) What is a co-chaperone, Cell Stress Chaperones 8, 105-107.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 105-107
    • Caplan, A.J.1
  • 10
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaptation of chaperone function
    • Cheetham, M.E. and Caplan, A.J. (1998) Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function, Cell Stress and Chaperones 3, 28-36.
    • (1998) Cell Stress and Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 11
    • 0028899440 scopus 로고
    • Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications
    • Cherian, M. and Abraham, E.C. (1995) Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications, Biochem. Biophys. Res. Commun. 208, 675-679.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 675-679
    • Cherian, M.1    Abraham, E.C.2
  • 12
    • 3242776825 scopus 로고    scopus 로고
    • Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
    • Chowdary, T.K., Raman, B., Ramakrishna, T. and Rao, C.M. (2004) Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity, Biochem. J. 381, 379-387.
    • (2004) Biochem. J. , vol.381 , pp. 379-387
    • Chowdary, T.K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 13
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover, A. and Brundin, P. (2003) The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg, Neuron 40, 427-446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 14
    • 3042538418 scopus 로고    scopus 로고
    • The ubiquitin system: From basic mechanisms to the patient bed
    • Ciechanover, A. and Iwai, K. (2004) The ubiquitin system: from basic mechanisms to the patient bed, IUBMB Life 56, 193-201.
    • (2004) IUBMB Life , vol.56 , pp. 193-201
    • Ciechanover, A.1    Iwai, K.2
  • 15
    • 0034719154 scopus 로고    scopus 로고
    • Structural and functional changes in the alpha-A-crystallin R11C mutant in hereditary cataracts
    • Cobb, B.A. and Petrash, J.M. (2000) Structural and functional changes in the alpha-A-crystallin R11C mutant in hereditary cataracts, Biochemistry 39, 15791-15798.
    • (2000) Biochemistry , vol.39 , pp. 15791-15798
    • Cobb, B.A.1    Petrash, J.M.2
  • 16
    • 0035576876 scopus 로고    scopus 로고
    • Chaperone overload is a possible contributor to civilization disease
    • Csermely, P. (2001) Chaperone overload is a possible contributor to civilization disease, Trends Genet. 17, 701-704.
    • (2001) Trends Genet. , vol.17 , pp. 701-704
    • Csermely, P.1
  • 17
    • 0031873752 scopus 로고    scopus 로고
    • The 90 kDa molecular chaperone family: Structure, function and clinical applications
    • Csermely, P., Schnaider, T., Soeti, C., Prohaszka, Z. and Nardai, G. (1998) The 90 kDa molecular chaperone family: structure, function and clinical applications, Pharmacol. Ther. 79, 129-168.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soeti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 18
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M. (2003) Protein folding and misfolding, Nature 426, 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 19
    • 0033625965 scopus 로고    scopus 로고
    • The Hsp110 and Grp170 stress proteins: Newly recognized relatives of the Hsp70s
    • Easton, D.P., Kaneko, Y. and Subjeck, J.R. (2000) The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s, Cell Stress Chaperones 5, 276-290.
    • (2000) Cell Stress Chaperones , vol.5 , pp. 276-290
    • Easton, D.P.1    Kaneko, Y.2    Subjeck, J.R.3
  • 22
    • 0030755096 scopus 로고    scopus 로고
    • Variation in hsp gene expression and Hsp polymorphism: Do they contribute to differential disease susceptibility and stress tolerance?
    • Favatier, F., Bornman, L., Hightower, L.E., Guenther, E. and Polla, B.S. (1997) Variation in hsp gene expression and Hsp polymorphism: do they contribute to differential disease susceptibility and stress tolerance? Cell Stress Chaperones 2, 141-155.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 141-155
    • Favatier, F.1    Bornman, L.2    Hightower, L.E.3    Guenther, E.4    Polla, B.S.5
  • 24
    • 1642392035 scopus 로고    scopus 로고
    • Retrograde transport of the glucocortoid receptor in neurites requires dynamic assembly of complexes with the protein chaperon hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation
    • Galigniana, M.D., Harrel, J.M., Housley, P.R., Patterson, C., Fisher, S.K. and Pratt, W.B. (2004) Retrograde transport of the glucocortoid receptor in neurites requires dynamic assembly of complexes with the protein chaperon hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation, Mol. Brain Res. 123, 27-36.
    • (2004) Mol. Brain Res. , vol.123 , pp. 27-36
    • Galigniana, M.D.1    Harrel, J.M.2    Housley, P.R.3    Patterson, C.4    Fisher, S.K.5    Pratt, W.B.6
  • 25
    • 9844222252 scopus 로고
    • Heat shock response in Escherichia coli
    • Drilica, K. and Riley, M., eds, (American Society for Microbiology, Washington, D.C.)
    • Georgopoulos, C., Ang, D., Maddock, A., Raina, S., Lipinska, B. and Zylicz, M. (1990) Heat shock response in Escherichia coli, In: Drilica, K. and Riley, M., eds, The Bacterial Chromosome (American Society for Microbiology, Washington, D.C.), pp 405-419.
    • (1990) The Bacterial Chromosome , pp. 405-419
    • Georgopoulos, C.1    Ang, D.2    Maddock, A.3    Raina, S.4    Lipinska, B.5    Zylicz, M.6
  • 26
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos, C. and Welch, W.J. (1993) Role of the major heat shock proteins as molecular chaperones, Annu. Rev. Cell Biol. 9, 601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 27
    • 2442682934 scopus 로고    scopus 로고
    • Independent functions of hsp90 in neurotransmitter release and in the continuous synaptic cycling of AMPA receptors
    • Gerges, N.Z., Tran, I.C., Backos, D.S., Harrel, J.M., Chinkers, M., Pratt, W.B. and Esteban, J.A. (2004) Independent functions of hsp90 in neurotransmitter release and in the continuous synaptic cycling of AMPA receptors, J. Neurosci. 24, 4758-4766.
    • (2004) J. Neurosci. , vol.24 , pp. 4758-4766
    • Gerges, N.Z.1    Tran, I.C.2    Backos, D.S.3    Harrel, J.M.4    Chinkers, M.5    Pratt, W.B.6    Esteban, J.A.7
  • 28
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M.H. and Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction, Physiol. Rev. 82, 373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 29
    • 3142767444 scopus 로고    scopus 로고
    • Reversion of protein aggregation mediated by Sso7d in cell extracts of Sulfologus solfataricus
    • Guagliardi, A., Mancusi, L. and Rossi, M. (2004) Reversion of protein aggregation mediated by Sso7d in cell extracts of Sulfologus solfataricus, Biochem. J. 381, 249-255.
    • (2004) Biochem. J. , vol.381 , pp. 249-255
    • Guagliardi, A.1    Mancusi, L.2    Rossi, M.3
  • 31
    • 0037208893 scopus 로고    scopus 로고
    • Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter
    • Hansen, J.J., Bross, P., Westergaard, M., Nielsen, M., Eiberg, H., Borglum, A.D., Mogensen, J., Kristiansen, K., Bolund, L. and Gregersen, N. (2003) Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter, Hum. Genet. 112, 71-77.
    • (2003) Hum. Genet. , vol.112 , pp. 71-77
    • Hansen, J.J.1    Bross, P.2    Westergaard, M.3    Nielsen, M.4    Eiberg, H.5    Borglum, A.D.6    Mogensen, J.7    Kristiansen, K.8    Bolund, L.9    Gregersen, N.10
  • 32
    • 0344875614 scopus 로고    scopus 로고
    • GrpE, a nucleotide exchange factor for DnaK
    • Harrison, C. (2003) GrpE, a nucleotide exchange factor for DnaK, Cell Stress Chaperones 8, 218-224.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 218-224
    • Harrison, C.1
  • 33
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein, Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 34
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay, D.G., Sathasivam, K., Tobaben, S., Stahl, B., Marber, M., Mestril, R., Mahal, A., Smith, D.L., Woodman, B. and Bates, G.P. (2004) Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach, Hum. Mol. Genet. 13, 1389-1405.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 35
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Hayes, S.A. and Dice, J.F. (1996) Roles of molecular chaperones in protein degradation. Cell Biol. 132, 255-258.
    • (1996) Cell Biol. , vol.132 , pp. 255-258
    • Hayes, S.A.1    Dice, J.F.2
  • 36
    • 0035002568 scopus 로고    scopus 로고
    • Role of chaperones in nuclear translocation and transactivation of steroid receptors
    • Heinlein, C.A. and Chang, C. (2001) Role of chaperones in nuclear translocation and transactivation of steroid receptors. Endocrine 14, 143-149.
    • (2001) Endocrine , vol.14 , pp. 143-149
    • Heinlein, C.A.1    Chang, C.2
  • 37
    • 1542365215 scopus 로고    scopus 로고
    • The molecular chaperone Atp12p, Homo sapiens
    • Hinton, A., Gatti, D.L. and Ackerman, S.H. (2004) The molecular chaperone Atp12p, Homo sapiens, J. Biol. Chem. 279, 9016-9022.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9016-9022
    • Hinton, A.1    Gatti, D.L.2    Ackerman, S.H.3
  • 38
    • 0034756104 scopus 로고    scopus 로고
    • From the cradle to the grave: Molecular chaperones may choose between folding and degradation
    • Hoehfeld, J., Cyr, D.M. and Patterson, C. (2001) From the cradle to the grave: molecular chaperones may choose between folding and degradation, EMBO Rep. 21, 885-890.
    • (2001) EMBO Rep. , vol.21 , pp. 885-890
    • Hoehfeld, J.1    Cyr, D.M.2    Patterson, C.3
  • 40
    • 17844386773 scopus 로고    scopus 로고
    • Posttranslational control and ubiquination
    • Epstein, C.J., Erickson, R.P. and Wynshaw-Boris, A., eds, (Oxford University Press, Oxford, UK)
    • Jackson, P.K. (2004) Posttranslational control and ubiquination, In: Epstein, C.J., Erickson, R.P. and Wynshaw-Boris, A., eds, Inborn Errors of Development (Oxford University Press, Oxford, UK), pp 804-814.
    • (2004) Inborn Errors of Development , pp. 804-814
    • Jackson, P.K.1
  • 41
    • 0037036431 scopus 로고    scopus 로고
    • Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP
    • Kang, S.G., Onega, J., Singh, S.K., Wang, N., Huang, N.N., Steven, A.C. and Maurizi, M.R. (2002) Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP, J. Biol. Chem. 277, 21095-21102.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21095-21102
    • Kang, S.G.1    Onega, J.2    Singh, S.K.3    Wang, N.4    Huang, N.N.5    Steven, A.C.6    Maurizi, M.R.7
  • 43
    • 0346963154 scopus 로고    scopus 로고
    • Modified alpha-A crystallin in the retina: Altered expression and truncation with aging
    • Kapphan, R.J., Ethen, C.M., Peters, E.A., Higgins, L.A. and Ferrington, D.A. (2003) Modified alpha-A crystallin in the retina: altered expression and truncation with aging, Biochemistry 42, 15310-15325.
    • (2003) Biochemistry , vol.42 , pp. 15310-15325
    • Kapphan, R.J.1    Ethen, C.M.2    Peters, E.A.3    Higgins, L.A.4    Ferrington, D.A.5
  • 44
    • 0033594405 scopus 로고    scopus 로고
    • Molecular chaperones: How J domains turn on Hsp70s
    • Kelley, W.L. (1999) Molecular chaperones: how J domains turn on Hsp70s, Curr. Biol. 9, R305-R308.
    • (1999) Curr. Biol. , vol.9
    • Kelley, W.L.1
  • 45
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen, B. and Braakman, I. (2004) Protein folding and quality control in the endoplasmic reticulum, Curr. Opin. Cell Biol. 16, 343-349.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 46
    • 0032560551 scopus 로고    scopus 로고
    • The thermosome: Archetype of group II chaperonins
    • Klumpp, M. and Baumeister, W. (1998) The thermosome: archetype of group II chaperonins, FEBS Lett. 430, 73-77.
    • (1998) FEBS Lett. , vol.430 , pp. 73-77
    • Klumpp, M.1    Baumeister, W.2
  • 47
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R.R. (2000) Aggresomes, inclusion bodies and protein aggregation, Trends Cell Biol. 10, 524-530.
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 48
    • 1442335996 scopus 로고    scopus 로고
    • The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase
    • Kozany, C., Mokranjac, D., Sichting, M., Neupert, W. and Hell, K. (2004) The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase, Struct. Mol. Biol. 11, 234-241.
    • (2004) Struct. Mol. Biol. , vol.11 , pp. 234-241
    • Kozany, C.1    Mokranjac, D.2    Sichting, M.3    Neupert, W.4    Hell, K.5
  • 49
    • 0035951385 scopus 로고    scopus 로고
    • Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding
    • Krzewska, J., Langer, T. and Liberek, K. (2001) Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding, FEBS Lett. 489, 92-96.
    • (2001) FEBS Lett. , vol.489 , pp. 92-96
    • Krzewska, J.1    Langer, T.2    Liberek, K.3
  • 50
    • 2142806742 scopus 로고    scopus 로고
    • Minimal protein-folding systems in hyperthermophilic archaea
    • Laksanalmai, P., Whitehead, T.A. and Robb, F.T. (2004) Minimal protein-folding systems in hyperthermophilic archaea, Nat. Rev. Microbiol. 2, 315-324.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 315-324
    • Laksanalmai, P.1    Whitehead, T.A.2    Robb, F.T.3
  • 51
    • 3042811126 scopus 로고    scopus 로고
    • A single amino acid substitution in a proteasome subunit triggers aggregation of ubiquitinated proteins in stressed neuronal cells
    • Li, Z., Arnaud, L., Rockwell, P. and Figueiredo-Pereira, M.E. (2004) A single amino acid substitution in a proteasome subunit triggers aggregation of ubiquitinated proteins in stressed neuronal cells, J. Neurochem. 90, 19-28.
    • (2004) J. Neurochem. , vol.90 , pp. 19-28
    • Li, Z.1    Arnaud, L.2    Rockwell, P.3    Figueiredo-Pereira, M.E.4
  • 52
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • Litt, M., Kramer, P., LaMorticella, D.M., Murphey, W., Lovrien, E.W. and Weleber, R.G. (1998) Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA, Hum. Mol. Genet. 7, 471-474.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    Lamorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 53
    • 3142657524 scopus 로고    scopus 로고
    • Evidence for an unfolding/threading mechanism for protein pisaggregation by Saccharomyces cerevisiae Hsp104
    • Lum, R., Tkach, J.M., Vierling, E. and Glover, J.R. (2004) Evidence for an unfolding/threading mechanism for protein pisaggregation by Saccharomyces cerevisiae Hsp104, J. Biol. Chem. 279, 29139-29146.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29139-29146
    • Lum, R.1    Tkach, J.M.2    Vierling, E.3    Glover, J.R.4
  • 54
    • 0029188297 scopus 로고
    • Heat-shock proteins and molecular chaperones: Implications for pathogenesis, diagnostics, and therapeutics
    • Macario, A.J.L. (1995) Heat-shock proteins and molecular chaperones: implications for pathogenesis, diagnostics, and therapeutics, Int. J. Clin. Lab. Res. (Currently Clin. Exp. Med.) 25, 59-70.
    • (1995) Int. J. Clin. Lab. Res. (Currently Clin. Exp. Med.) , vol.25 , pp. 59-70
    • Macario, A.J.L.1
  • 56
    • 0005125363 scopus 로고    scopus 로고
    • Molecular chaperones and age-related degenerative disorders
    • Macario, A.J.L. and Conway de Macario, E. (2001a) Molecular chaperones and age-related degenerative disorders, Adv. Cell Aging Gerontol. 7, 131-162.
    • (2001) Adv. Cell Aging Gerontol. , vol.7 , pp. 131-162
    • Macario, A.J.L.1    Conway De Macario, E.2
  • 57
    • 0035260487 scopus 로고    scopus 로고
    • The molecular chaperone system and other anti-stress mechanisms in archaea
    • On line journal
    • Macario, A.J.L. and Conway de Macario, E. (2001b) The molecular chaperone system and other anti-stress mechanisms in archaea, Front. Biosci. 6, d262-d283, On line journal http://www.bioscience.org/2001/v6/d/macario/fulltext. htm
    • (2001) Front. Biosci. , vol.6
    • Macario, A.J.L.1    Conway De Macario, E.2
  • 60
    • 2442718034 scopus 로고    scopus 로고
    • Evolution of assisted protein folding: The distribution of the main chaperoning systems within the phylogenetic domain Archaea
    • On line journal
    • Macario, A.J.L., Malz, M. and Conway de Macario, E. (2004) Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain Archaea, Front. Biosci. 9, 1318-1332, On line journal http://www.bioscience.org/2004/v9/af/1328/fulltext.htm
    • (2004) Front. Biosci. , vol.9 , pp. 1318-1332
    • Macario, A.J.L.1    Malz, M.2    Conway De Macario, E.3
  • 62
    • 2442704477 scopus 로고    scopus 로고
    • Archaeal peptidyl prolyl cis-trans isomerases (PPIases), update 2004
    • On line journal
    • Maruyama, T., Suzuki, R. and Furutani, M. (2004) Archaeal peptidyl prolyl cis-trans isomerases (PPIases), update 2004 Front. Biosci. 9, 1680-1700, On line journal http://www.bioscience.org/2004/v9/af/1361/fulltext.htm
    • (2004) Front. Biosci. , vol.9 , pp. 1680-1700
    • Maruyama, T.1    Suzuki, R.2    Furutani, M.3
  • 63
    • 2542587655 scopus 로고    scopus 로고
    • Identification of chaperonin CCT-gamma subunit as a determinant of retinotectal development by whole-genome subtraction cloning from zebrafish no tectal neuron mutant
    • Matsuda, N. and Mishina, N. (2004) Identification of chaperonin CCT-gamma subunit as a determinant of retinotectal development by whole-genome subtraction cloning from zebrafish no tectal neuron mutant, Development 131, 1913-1925.
    • (2004) Development , vol.131 , pp. 1913-1925
    • Matsuda, N.1    Mishina, N.2
  • 64
    • 0033529033 scopus 로고    scopus 로고
    • Molecular chaperones: The busy life of Hsp90
    • Mayer, M.P. and Bukau, B. (1999) Molecular chaperones: the busy life of Hsp90, Curr. Biol. 9, R322-R325.
    • (1999) Curr. Biol. , vol.9
    • Mayer, M.P.1    Bukau, B.2
  • 65
    • 0035147404 scopus 로고    scopus 로고
    • Molecular chaperones and the art of recognizing a lost cause
    • McClellan, A.J. and Frydman, J. (2001) Molecular chaperones and the art of recognizing a lost cause, Nat. Cell Biol. 3, E1-E3.
    • (2001) Nat. Cell Biol. , vol.3
    • McClellan, A.J.1    Frydman, J.2
  • 66
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto, R.I. (1998) Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators, Genes Dev. 12, 3788-3796.
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 67
    • 0037014426 scopus 로고    scopus 로고
    • Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
    • Muchowski, P.J. (2002) Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron 35, 9-12.
    • (2002) Neuron , vol.35 , pp. 9-12
    • Muchowski, P.J.1
  • 68
    • 0036195722 scopus 로고    scopus 로고
    • Alpha-crystallin-type heat-shock proteins: Socializing minichaperones in the context of a multichaperone network
    • Narberhaus, F. (2002) Alpha-crystallin-type heat-shock proteins: socializing minichaperones in the context of a multichaperone network, Microbiol. Mol. Biol. Rev. 66, 64-93.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 69
    • 0036814834 scopus 로고    scopus 로고
    • Chaperone function and chaperone overload in the aged: A preliminary analysis
    • Nardai, G., Csermely, P. and Soti, C. (2002) Chaperone function and chaperone overload in the aged: a preliminary analysis, Exp. Gerontol. 37, 1257-1262.
    • (2002) Exp. Gerontol. , vol.37 , pp. 1257-1262
    • Nardai, G.1    Csermely, P.2    Soti, C.3
  • 71
    • 1042301417 scopus 로고    scopus 로고
    • S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complex
    • Okada, M., Hatakeyama, T., Itoh, H., Tokuta, N., Tokumitsu, H. and Kobayashi, R. (2004) S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complex, J. Biol. Chem. 279, 4221-4233.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4221-4233
    • Okada, M.1    Hatakeyama, T.2    Itoh, H.3    Tokuta, N.4    Tokumitsu, H.5    Kobayashi, R.6
  • 72
    • 0346365101 scopus 로고    scopus 로고
    • The chaperoning properties of mouse Grp170, a member of the third family of Hsp70 related proteins
    • Park, J., Easton, D.P., Chen, X., MacDonald, I.J., Wang, X.-Y. and Subjeck, J.R. (2003) The chaperoning properties of mouse Grp170, a member of the third family of Hsp70 related proteins, Biochemistry 42, 14893-14902.
    • (2003) Biochemistry , vol.42 , pp. 14893-14902
    • Park, J.1    Easton, D.P.2    Chen, X.3    MacDonald, I.J.4    Wang, X.-Y.5    Subjeck, J.R.6
  • 73
    • 0036843239 scopus 로고    scopus 로고
    • Mutation of TBCE causes hypoparathyroidims retardation-dysmorphism and autosomal recessive Kenny-Caffey syndrome
    • Parvari, R. and HRD/Autosomal Recessive Kenny-Caffey Syndrome Consortium (2002) Mutation of TBCE causes hypoparathyroidims retardation-dysmorphism and autosomal recessive Kenny-Caffey syndrome, Nat. Genet. 32, 448-452.
    • (2002) Nat. Genet. , vol.32 , pp. 448-452
    • Parvari, R.1
  • 74
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in the regulation of the heat shock response and beyond
    • Pirkkala, L., Nykanen, P. and Sistonen, L. (2001) Roles of the heat shock transcription factors in the regulation of the heat shock response and beyond, FASEB J. 15, 1118-1131.
    • (2001) FASEB J. , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 75
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa, F. (1962) A new puffing pattern induced by temperature shock and DNP in Drosophila, Experientia 18, 571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 76
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C.P. and Poirier, M.A. (2004) Protein aggregation and neurodegenerative disease, Nat. Med. 10, S10-S17.
    • (2004) Nat. Med. , vol.10
    • Ross, C.P.1    Poirier, M.A.2
  • 79
    • 0035872885 scopus 로고    scopus 로고
    • Mutations in the X-linked RP2 gene cause intracellular misrouting and loss of the protein
    • Schwahn, U., Paland, N., Techritz, S., Lenzner, S. and Berger, W. (2001) Mutations in the X-linked RP2 gene cause intracellular misrouting and loss of the protein, Hum. Mol. Genet. 10, 1177-1183.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1177-1183
    • Schwahn, U.1    Paland, N.2    Techritz, S.3    Lenzner, S.4    Berger, W.5
  • 80
    • 34249007019 scopus 로고
    • A syndrome produced by diverse nocuous agents
    • Selye, H. (1936) A syndrome produced by diverse nocuous agents, Nature 138, 32.
    • (1936) Nature , vol.138 , pp. 32
    • Selye, H.1
  • 81
    • 0035451646 scopus 로고    scopus 로고
    • Unfolding the role of chaperones and chaperonins in human disease
    • Slavotinek, A.M. and Biesecker, L.G. (2001) Unfolding the role of chaperones and chaperonins in human disease, Trends Genet. 17, 528-535.
    • (2001) Trends Genet. , vol.17 , pp. 528-535
    • Slavotinek, A.M.1    Biesecker, L.G.2
  • 83
    • 0036883535 scopus 로고    scopus 로고
    • Chaperones and aging: Role in neurodegeneration and in other civilizational diseases
    • Soti, C. and Csermely, P. (2002) Chaperones and aging: role in neurodegeneration and in other civilizational diseases, Neurochem. Int. 41, 383-389.
    • (2002) Neurochem. Int. , vol.41 , pp. 383-389
    • Soti, C.1    Csermely, P.2
  • 84
    • 0142186172 scopus 로고    scopus 로고
    • Aging and molecular chaperones
    • Soti, C. and Csermely, P. (2003) Aging and molecular chaperones, Exp. Gerontol. 38, 1037-1040.
    • (2003) Exp. Gerontol. , vol.38 , pp. 1037-1040
    • Soti, C.1    Csermely, P.2
  • 86
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogasler: Relation to chromosome puffs
    • Tissieres, A., Mitchell, H.K. and Tracy, U.M. (1974) Protein synthesis in salivary glands of Drosophila melanogasler: relation to chromosome puffs, J. Mol. Biol. 84, 389-398.
    • (1974) J. Mol. Biol. , vol.84 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 87
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa, P. and Csermely, P. (2004) The role of structural disorder in the function of RNA and protein chaperones, FASEB J. 18, 1169-1175.
    • (2004) FASEB J. , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 88
    • 0037447049 scopus 로고    scopus 로고
    • Mechanism of protein import into mitochondria
    • Truscott, K.N., Brandner, K. and Pfanner, N. (2003) Mechanism of protein import into mitochondria, Curr. Biol. 13, R326-R337.
    • (2003) Curr. Biol. , vol.13
    • Truscott, K.N.1    Brandner, K.2    Pfanner, N.3
  • 90
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: Modulating protein assembly, disassembly and translocation
    • Walsh, P., Bursac, D., Law, Y.C., Cyr, D. and Lithgow, T. (2004) The J-protein family: modulating protein assembly, disassembly and translocation, EMBO Rep. 5, 567-571.
    • (2004) EMBO Rep. , vol.5 , pp. 567-571
    • Walsh, P.1    Bursac, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 91
    • 0026460892 scopus 로고
    • Mammalian stress response: Cell physiology, structure/function of stress proteins, and implications for medicine and disease
    • Welch, W.J. (1992) Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease, Physiol. Rev. 72, 1063-1081.
    • (1992) Physiol. Rev. , vol.72 , pp. 1063-1081
    • Welch, W.J.1
  • 92
    • 0032587683 scopus 로고    scopus 로고
    • Truncation of βA3/A1-crystallin during aging of the bovine lens; possible implications for lens optical quality
    • Werten, P.J.L., Vos, E. and de Jong, W.W. (1999) Truncation of βA3/A1-crystallin during aging of the bovine lens; possible implications for lens optical quality, Exp. Eye Res. 68, 99-103.
    • (1999) Exp. Eye Res. , vol.68 , pp. 99-103
    • Werten, P.J.L.1    Vos, E.2    De Jong, W.W.3
  • 95
    • 0034805931 scopus 로고    scopus 로고
    • Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease
    • Yoo, C.B., Kim, S.H., Cairns, N., Fountoulakis, M. and Lubec, G. (2001) Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease, Biochem. Biophys. Res. Commun. 280, 249-258.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 249-258
    • Yoo, C.B.1    Kim, S.H.2    Cairns, N.3    Fountoulakis, M.4    Lubec, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.