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Volumn 121, Issue 5, 2005, Pages 739-748

Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways

Author keywords

[No Author keywords available]

Indexed keywords

BRIDGED COMPOUND; CHAPERONE; HEAT SHOCK COGNATE 70 INTERACTING PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; T COMPLEX PROTEIN 1; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

EID: 20444413061     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.03.024     Document Type: Article
Times cited : (227)

References (58)
  • 2
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • C.A. Ballinger, P. Connell, Y. Wu, Z. Hu, L.J. Thompson, L.Y. Yin, and C. Patterson Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions Mol. Cell. Biol. 19 1999 4535 4545
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 3
    • 4444291856 scopus 로고    scopus 로고
    • Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex
    • P.K. Bansal, R. Abdulle, and K. Kitagawa Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex Mol. Cell. Biol. 24 2004 8069 8079
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8069-8079
    • Bansal, P.K.1    Abdulle, R.2    Kitagawa, K.3
  • 4
    • 0029954823 scopus 로고    scopus 로고
    • Functional interaction of cytosolic Hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo
    • J. Becker, W. Walter, W. Yan, and E.A. Craig Functional interaction of cytosolic Hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo Mol. Cell. Biol. 16 1996 4378 4386
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4378-4386
    • Becker, J.1    Walter, W.2    Yan, W.3    Craig, E.A.4
  • 6
    • 0031868061 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins
    • S.P. Bohen Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins Mol. Cell. Biol. 18 1998 3330 3339
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3330-3339
    • Bohen, S.P.1
  • 8
    • 0033525198 scopus 로고    scopus 로고
    • The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    • J.L. Brodsky, E.D. Werner, M.E. Dubas, J.L. Goeckeler, K.B. Kruse, and A.A. McCracken The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct J. Biol. Chem. 274 1999 3453 3460
    • (1999) J. Biol. Chem. , vol.274 , pp. 3453-3460
    • Brodsky, J.L.1    Werner, E.D.2    Dubas, M.E.3    Goeckeler, J.L.4    Kruse, K.B.5    McCracken, A.A.6
  • 9
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • B. Bukau, and A.L. Horwich 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
  • 10
    • 0041669463 scopus 로고    scopus 로고
    • The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20
    • A. Camasses, A. Bogdanova, A. Shevchenko, and W. Zachariae The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20 Mol. Cell 12 2003 87 100
    • (2003) Mol. Cell , vol.12 , pp. 87-100
    • Camasses, A.1    Bogdanova, A.2    Shevchenko, A.3    Zachariae, W.4
  • 11
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
    • P. Chen, P. Johnson, T. Sommer, S. Jentsch, and M. Hochstrasser Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor Cell 74 1993 357 369
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 13
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • D.M. Cyr, J. Hohfeld, and C. Patterson Protein quality control: U-box-containing E3 ubiquitin ligases join the fold Trends Biochem. Sci. 27 2002 368 375
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 14
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • C.M. Dobson Protein misfolding, evolution and disease Trends Biochem. Sci. 24 1999 329 332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 16
    • 0036810483 scopus 로고    scopus 로고
    • Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question
    • D.A. Dougan, A. Mogk, and B. Bukau Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question Cell. Mol. Life Sci. 59 2002 1607 1616
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1607-1616
    • Dougan, D.A.1    Mogk, A.2    Bukau, B.3
  • 17
    • 0025794119 scopus 로고
    • Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster
    • D.R. Drummond, E.S. Hennessey, and J.C. Sparrow Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster Mol. Gen. Genet. 226 1991 70 80
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 70-80
    • Drummond, D.R.1    Hennessey, E.S.2    Sparrow, J.C.3
  • 18
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • L. Ellgaard, and A. Helenius Quality control in the endoplasmic reticulum Nat. Rev. Mol. Cell Biol. 4 2003 181 191
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 19
    • 0033400674 scopus 로고    scopus 로고
    • Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
    • D.E. Feldman, V. Thulasiraman, R.G. Ferreyra, and J. Frydman Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC Mol. Cell 4 1999 1051 1061
    • (1999) Mol. Cell , vol.4 , pp. 1051-1061
    • Feldman, D.E.1    Thulasiraman, V.2    Ferreyra, R.G.3    Frydman, J.4
  • 20
    • 0345708112 scopus 로고    scopus 로고
    • Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding
    • D.E. Feldman, C. Spiess, D.E. Howard, and J. Frydman Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding Mol. Cell 12 2003 1213 1224
    • (2003) Mol. Cell , vol.12 , pp. 1213-1224
    • Feldman, D.E.1    Spiess, C.2    Howard, D.E.3    Frydman, J.4
  • 22
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • J. Frydman Folding of newly translated proteins in vivo: the role of molecular chaperones Annu. Rev. Biochem. 70 2001 603 647
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 23
    • 0027444947 scopus 로고
    • S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase
    • M. Ghislain, A. Udvardy, and C. Mann S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase Nature 366 1993 358 362
    • (1993) Nature , vol.366 , pp. 358-362
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 24
    • 0034661466 scopus 로고    scopus 로고
    • CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90
    • T. Goasduff, and A.I. Cederbaum CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90 Arch. Biochem. Biophys. 379 2000 321 330
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 321-330
    • Goasduff, T.1    Cederbaum, A.I.2
  • 25
    • 0036678054 scopus 로고    scopus 로고
    • Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity
    • J.L. Goeckeler, A. Stephens, P. Lee, A.J. Caplan, and J.L. Brodsky Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity Mol. Biol. Cell 13 2002 2760 2770
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2760-2770
    • Goeckeler, J.L.1    Stephens, A.2    Lee, P.3    Caplan, A.J.4    Brodsky, J.L.5
  • 26
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • A.L. Goldberg Protein degradation and protection against misfolded or damaged proteins Nature 426 2003 895 899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 27
    • 0035816574 scopus 로고    scopus 로고
    • Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70
    • V. Gusarova, A.J. Caplan, J.L. Brodsky, and E.A. Fisher Apoprotein B degradation is promoted by the molecular chaperones hsp90 and hsp70 J. Biol. Chem. 276 2001 24891 24900
    • (2001) J. Biol. Chem. , vol.276 , pp. 24891-24900
    • Gusarova, V.1    Caplan, A.J.2    Brodsky, J.L.3    Fisher, E.A.4
  • 28
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • R.Y. Hampton ER-associated degradation in protein quality control and cellular regulation Curr. Opin. Cell Biol. 14 2002 476 482
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 29
    • 0036176874 scopus 로고    scopus 로고
    • Diverse effects of mutations in exon II of the von Hippel-Lindau (VHL) tumor suppressor gene on the interaction of pVHL with the cytosolic chaperonin and pVHL-dependent ubiquitin ligase activity
    • W.J. Hansen, M. Ohh, J. Moslehi, K. Kondo, W.G. Kaelin, and W.J. Welch Diverse effects of mutations in exon II of the von Hippel-Lindau (VHL) tumor suppressor gene on the interaction of pVHL with the cytosolic chaperonin and pVHL-dependent ubiquitin ligase activity Mol. Cell. Biol. 22 2002 1947 1960
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1947-1960
    • Hansen, W.J.1    Ohh, M.2    Moslehi, J.3    Kondo, K.4    Kaelin, W.G.5    Welch, W.J.6
  • 30
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • F.U. Hartl, and M. Hayer-Hartl Molecular chaperones in the cytosol: from nascent chain to folded protein Science 295 2002 1852 1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 31
    • 0030728039 scopus 로고    scopus 로고
    • Deadly conformations - protein misfolding in prion disease
    • A.L. Horwich, and J.S. Weissman Deadly conformations - protein misfolding in prion disease Cell 89 1997 499 510
    • (1997) Cell , vol.89 , pp. 499-510
    • Horwich, A.L.1    Weissman, J.S.2
  • 33
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • W.G. Kaelin Jr. Molecular basis of the VHL hereditary cancer syndrome Nat. Rev. Cancer 2 2002 673 682
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 673-682
    • Kaelin Jr., W.G.1
  • 34
    • 0028064780 scopus 로고
    • Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES
    • O. Kandror, L. Busconi, M. Sherman, and A.L. Goldberg Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES J. Biol. Chem. 269 1994 23575 23582
    • (1994) J. Biol. Chem. , vol.269 , pp. 23575-23582
    • Kandror, O.1    Busconi, L.2    Sherman, M.3    Goldberg, A.L.4
  • 35
    • 0034505937 scopus 로고    scopus 로고
    • Protein degradation in mitochondria
    • M. Kaser, and T. Langer Protein degradation in mitochondria Semin. Cell Dev. Biol. 11 2000 181 190
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 181-190
    • Kaser, M.1    Langer, T.2
  • 36
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Z. Kostova, and D.H. Wolf For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection EMBO J. 22 2003 2309 2317
    • (2003) EMBO J. , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 37
    • 0001389495 scopus 로고    scopus 로고
    • Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae
    • D.H. Lee, M.Y. Sherman, and A.L. Goldberg Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae Mol. Cell. Biol. 16 1996 4773 4781
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4773-4781
    • Lee, D.H.1    Sherman, M.Y.2    Goldberg, A.L.3
  • 38
    • 0033578875 scopus 로고    scopus 로고
    • The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone
    • X.D. Liu, K.A. Morano, and D.J. Thiele The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone J. Biol. Chem. 274 1999 26654 26660
    • (1999) J. Biol. Chem. , vol.274 , pp. 26654-26660
    • Liu, X.D.1    Morano, K.A.2    Thiele, D.J.3
  • 39
    • 0035147404 scopus 로고    scopus 로고
    • Molecular chaperones and the art of recognizing a lost cause
    • A.J. McClellan, and J. Frydman Molecular chaperones and the art of recognizing a lost cause Nat. Cell Biol. 3 2001 E51 E53
    • (2001) Nat. Cell Biol. , vol.3
    • McClellan, A.J.1    Frydman, J.2
  • 40
    • 0037404423 scopus 로고    scopus 로고
    • The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex
    • M.W. Melville, A.J. McClellan, A.S. Meyer, A. Darveau, and J. Frydman The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex Mol. Cell. Biol. 23 2003 3141 3151
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3141-3151
    • Melville, M.W.1    McClellan, A.J.2    Meyer, A.S.3    Darveau, A.4    Frydman, J.5
  • 41
    • 0036848793 scopus 로고    scopus 로고
    • Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins
    • K. Mitsui, H. Nakayama, T. Akagi, M. Nekooki, K. Ohtawa, K. Takio, T. Hashikawa, and N. Nukina Purification of polyglutamine aggregates and identification of elongation factor-1alpha and heat shock protein 84 as aggregate-interacting proteins J. Neurosci. 22 2002 9267 9277
    • (2002) J. Neurosci. , vol.22 , pp. 9267-9277
    • Mitsui, K.1    Nakayama, H.2    Akagi, T.3    Nekooki, M.4    Ohtawa, K.5    Takio, K.6    Hashikawa, T.7    Nukina, N.8
  • 42
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase
    • D.F. Nathan, and S. Lindquist Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase Mol. Cell. Biol. 15 1995 3917 3925
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 43
    • 0024469206 scopus 로고
    • Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae
    • C.M. Nicolet, and E.A. Craig Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae Mol. Cell. Biol. 9 1989 3638 3646
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3638-3646
    • Nicolet, C.M.1    Craig, E.A.2
  • 44
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • S.I. Nishikawa, S.W. Fewell, Y. Kato, J.L. Brodsky, and T. Endo Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation J. Cell Biol. 153 2001 1061 1070
    • (2001) J. Cell Biol. , vol.153 , pp. 1061-1070
    • Nishikawa, S.I.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 45
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • D. Picard Heat-shock protein 90, a chaperone for folding and regulation Cell. Mol. Life Sci. 59 2002 1640 1648
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 46
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • C. Scheufler, A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F.U. Hartl, and I. Moarefi Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Cell 101 2000 199 210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 47
    • 0034682465 scopus 로고    scopus 로고
    • Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products
    • A.R. Schoenfeld, E.J. Davidowitz, and R.D. Burk Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products Proc. Natl. Acad. Sci. USA 97 2000 8507 8512
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8507-8512
    • Schoenfeld, A.R.1    Davidowitz, E.J.2    Burk, R.D.3
  • 48
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • W. Seufert, and S. Jentsch Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins EMBO J. 9 1990 543 550
    • (1990) EMBO J. , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 49
    • 0141592584 scopus 로고    scopus 로고
    • Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD
    • C. Taxis, R. Hitt, S.H. Park, P.M. Deak, Z. Kostova, and D.H. Wolf Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD J. Biol. Chem. 278 2003 35903 35913
    • (2003) J. Biol. Chem. , vol.278 , pp. 35903-35913
    • Taxis, C.1    Hitt, R.2    Park, S.H.3    Deak, P.M.4    Kostova, Z.5    Wolf, D.H.6
  • 50
    • 0033521588 scopus 로고    scopus 로고
    • In vivo newly translated polypeptides are sequestered in a protected folding environment
    • V. Thulasiraman, C.F. Yang, and J. Frydman In vivo newly translated polypeptides are sequestered in a protected folding environment EMBO J. 18 1999 85 95
    • (1999) EMBO J. , vol.18 , pp. 85-95
    • Thulasiraman, V.1    Yang, C.F.2    Frydman, J.3
  • 51
  • 52
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • R. Verma, S. Chen, R. Feldman, D. Schieltz, J. Yates, J. Dohmen, and R.J. Deshaies Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes Mol. Biol. Cell 11 2000 3425 3439
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 53
    • 0028587244 scopus 로고
    • A yeast TCP-1-like protein is required for actin function in vivo
    • D.B. Vinh, and D.G. Drubin A yeast TCP-1-like protein is required for actin function in vivo Proc. Natl. Acad. Sci. USA 91 1994 9116 9120
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9116-9120
    • Vinh, D.B.1    Drubin, D.G.2
  • 54
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: modulating protein assembly, disassembly and translocation
    • P. Walsh, D. Bursac, Y.C. Law, D. Cyr, and T. Lithgow The J-protein family: modulating protein assembly, disassembly and translocation EMBO Rep. 5 2004 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
  • 55
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: folding, refolding, and degrading proteins
    • S. Wickner, M.R. Maurizi, and S. Gottesman Posttranslational quality control: folding, refolding, and degrading proteins Science 286 1999 1888 1893
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 57
    • 0037099735 scopus 로고    scopus 로고
    • Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing
    • T. Yamano, S. Murata, N. Shimbara, N. Tanaka, T. Chiba, K. Tanaka, K. Yui, and H. Udono Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing J. Exp. Med. 196 2002 185 196
    • (2002) J. Exp. Med. , vol.196 , pp. 185-196
    • Yamano, T.1    Murata, S.2    Shimbara, N.3    Tanaka, N.4    Chiba, T.5    Tanaka, K.6    Yui, K.7    Udono, H.8
  • 58
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: a specialized but essential protein-folding tool
    • J.C. Young, I. Moarefi, and F.U. Hartl Hsp90: a specialized but essential protein-folding tool J. Cell Biol. 154 2001 267 273
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3


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