메뉴 건너뛰기




Volumn 12, Issue 22, 2012, Pages 2504-2522

On the design of broad based screening assays to identify potential pharmacological chaperones of protein misfolding diseases

Author keywords

Groel chaperonin; Missense mutations; Pharmacological chaperones; Protein misfolding; Surface plasmon resonance

Indexed keywords

2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); ALPHA 1 ANTITRYPSIN; ALPHA GALACTOSIDASE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; AQUAPORIN 2; BETA 2 MICROGLOBULIN; BETA GLUCOSIDASE; CHAPERONE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; HUNTINGTIN; MYOCILIN; PHENYLALANINE 4 MONOOXYGENASE; POLYCYSTIN 2; PREALBUMIN; PROTEIN P53; SUPEROXIDE DISMUTASE; TAFAMIDIS; TAU PROTEIN;

EID: 84874885337     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026611212220006     Document Type: Review
Times cited : (14)

References (111)
  • 1
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A.; Chan, H. S. From Levinthal to pathways to funnels. Nat. Struct. Biol., 1997, 4 (1), 10-19.
    • (1997) Nat. Struct. Biol , vol.4 , Issue.1 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 2
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H.; Sligar, S. G.; Wolynes, P. G. The energy landscapes and motions of proteins. Science, 1991, 254 (5038), 1598-1603.
    • (1991) Science , vol.254 , Issue.5038 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 4
    • 78650217130 scopus 로고    scopus 로고
    • Cellular proteomes have broad distributions of protein stability
    • Ghosh, K.; Dill, K. Cellular proteomes have broad distributions of protein stability. Biophys. J., 2010, 99 (12), 3996-4002.
    • (2010) Biophys. J , vol.99 , Issue.12 , pp. 3996-4002
    • Ghosh, K.1    Dill, K.2
  • 6
    • 50249175120 scopus 로고    scopus 로고
    • Chemical and biological approaches synergize to ameliorate protein-folding diseases
    • Mu, T. W.; Ong, D. S.; Wang, Y. J.; Balch, W. E.; Yates, J. R., 3rd; Segatori, L.; Kelly, J. W. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell, 2008, 134 (5), 769-781.
    • (2008) Cell , vol.134 , Issue.5 , pp. 769-781
    • Mu, T.W.1    Ong, D.S.2    Wang, Y.J.3    Balch, W.E.4    Yates, J.R.5    Segatori, L.6    Kelly, J.W.7
  • 7
    • 70350347721 scopus 로고    scopus 로고
    • What are pharmacological chaperones and why are they interesting?
    • Ringe, D.; Petsko, G. A. What are pharmacological chaperones and why are they interesting? J Biol, 2009, 8 (9), 80.
    • (2009) J Biol , vol.8 , Issue.9 , pp. 80
    • Ringe, D.1    Petsko, G.A.2
  • 8
    • 78751550063 scopus 로고    scopus 로고
    • Chemical and pharmacological chaperones: Appli cation for recombinant protein production and protein folding diseases
    • Rajan, R. S.; Tsumoto, K.; Tokunaga, M.; Tokunaga, H.; Kita, Y.; Arakawa, T. Chemical and pharmacological chaperones: appli cation for recombinant protein production and protein folding diseases. Curr. Med. Chem., 2011, 18 (1), 1-15.
    • (2011) Curr. Med. Chem , vol.18 , Issue.1 , pp. 1-15
    • Rajan, R.S.1    Tsumoto, K.2    Tokunaga, M.3    Tokunaga, H.4    Kita, Y.5    Arakawa, T.6
  • 9
    • 79551482638 scopus 로고    scopus 로고
    • A polymorphic position in electron transfer flavoprotein modulates kinetic stability as evidenced by thermal stress
    • Henriques, B. J.; Fisher, M. T.; Bross, P.; Gomes, C. M. A polymorphic position in electron transfer flavoprotein modulates kinetic stability as evidenced by thermal stress. FEBS Lett., 2011, 585 (3), 505-510.
    • (2011) FEBS Lett , vol.585 , Issue.3 , pp. 505-510
    • Henriques, B.J.1    Fisher, M.T.2    Bross, P.3    Gomes, C.M.4
  • 12
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik, K. S.; Joachim, C. L.; Selkoe, D. J. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A., 1986, 83 (11), 4044-4048.
    • (1986) Proc. Natl. Acad. Sci. U. S. A , vol.83 , Issue.11 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 15
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng, S. H.; Gregory, R. J.; Marshall, J.; Paul, S.; Souza, D. W.; White, G. A.; O'Riordan, C. R.; Smith, A. E. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell, 1990, 63 (4), 827-834.
    • (1990) Cell , vol.63 , Issue.4 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5    White, G.A.6    O'Riordan, C.R.7    Smith, A.E.8
  • 16
    • 26444609722 scopus 로고    scopus 로고
    • ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity
    • Ron, I.; Horowitz, M. ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum. Mol. Genet., 2005, 14 (16), 2387-2398.
    • (2005) Hum. Mol. Genet , vol.14 , Issue.16 , pp. 2387-2398
    • Ron, I.1    Horowitz, M.2
  • 17
    • 0028269904 scopus 로고
    • Molecular basis of Fabry disease: Mutations and polymorphisms in the human alpha-galactosidase A gene
    • Eng, C. M.; Desnick, R. J. Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum. Mutat., 1994, 3 (2), 103-111.
    • (1994) Hum. Mutat , vol.3 , Issue.2 , pp. 103-111
    • Eng, C.M.1    Desnick, R.J.2
  • 19
    • 0022639484 scopus 로고
    • Serum levels of beta 2-microglobulin as a new form of amyloid protein in patients undergoing long-term hemodialysis
    • Gejyo, F.; Homma, N.; Suzuki, Y.; Arakawa, M. Serum levels of beta 2-microglobulin as a new form of amyloid protein in patients undergoing long-term hemodialysis. N. Engl. J. Med., 1986, 314 (9), 585-586.
    • (1986) N. Engl. J. Med , vol.314 , Issue.9 , pp. 585-586
    • Gejyo, F.1    Homma, N.2    Suzuki, Y.3    Arakawa, M.4
  • 20
    • 0021266985 scopus 로고
    • Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin)
    • Saraiva, M. J.; Birken, S.; Costa, P. P.; Goodman, D. S. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J. Clin. Invest., 1984, 74 (1), 104-119.
    • (1984) J. Clin. Invest , vol.74 , Issue.1 , pp. 104-119
    • Saraiva, M.J.1    Birken, S.2    Costa, P.P.3    Goodman, D.S.4
  • 21
    • 0034110962 scopus 로고    scopus 로고
    • Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype
    • Waters, P. J.; Parniak, M. A.; Akerman, B. R.; Scriver, C. R. Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype. Mol. Genet. Metab., 2000, 69 (2), 101-110.
    • (2000) Mol. Genet. Metab , vol.69 , Issue.2 , pp. 101-110
    • Waters, P.J.1    Parniak, M.A.2    Akerman, B.R.3    Scriver, C.R.4
  • 22
    • 84863275816 scopus 로고    scopus 로고
    • Frequent heterogeneous missense mutations of GGAP2 in prostate cancer: Implications for tumor biology, clonality and mutation analysis
    • Cai, Y.; Wang, J.; Ren, C.; Ittmann, M. Frequent heterogeneous missense mutations of GGAP2 in prostate cancer: implications for tumor biology, clonality and mutation analysis. PLoS One, 2012, 7 (2), e32708.
    • (2012) PLoS One , vol.7 , Issue.2
    • Cai, Y.1    Wang, J.2    Ren, C.3    Ittmann, M.4
  • 23
    • 79955907500 scopus 로고    scopus 로고
    • The structural impact of cancer-associated missense mutations in oncogenes and tumor suppressors
    • Stehr, H.; Jang, S. H.; Duarte, J. M.; Wierling, C.; Lehrach, H.; Lappe, M.; Lange, B. M. The structural impact of cancer-associated missense mutations in oncogenes and tumor suppressors. Mol Cancer, 2011, 10, 54.
    • (2011) Mol Cancer , vol.10 , pp. 54
    • Stehr, H.1    Jang, S.H.2    Duarte, J.M.3    Wierling, C.4    Lehrach, H.5    Lappe, M.6    Lange, B.M.7
  • 25
    • 80052028694 scopus 로고    scopus 로고
    • Messing up disorder: How do missense mutations in the tumor suppressor protein APC lead to cancer?
    • Minde, D. P.; Anvarian, Z.; Rudiger, S. G.; Maurice, M. M. Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer? Mol Cancer, 2011, 10, 101.
    • (2011) Mol Cancer , vol.10 , pp. 101
    • Minde, D.P.1    Anvarian, Z.2    Rudiger, S.G.3    Maurice, M.M.4
  • 26
    • 0031656903 scopus 로고    scopus 로고
    • Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase
    • Koutnikova, H.; Campuzano, V.; Koenig, M. Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase. Hum. Mol. Genet., 1998, 7 (9), 1485-1489.
    • (1998) Hum. Mol. Genet , vol.7 , Issue.9 , pp. 1485-1489
    • Koutnikova, H.1    Campuzano, V.2    Koenig, M.3
  • 28
    • 33645861655 scopus 로고    scopus 로고
    • Gene therapy for lysosomal storage diseases
    • Sands, M. S.; Davidson, B. L. Gene therapy for lysosomal storage diseases. Mol Ther, 2006, 13 (5), 839-849.
    • (2006) Mol Ther , vol.13 , Issue.5 , pp. 839-849
    • Sands, M.S.1    Davidson, B.L.2
  • 29
    • 0029557063 scopus 로고
    • Liver-directed gene therapy: Molecular tools and current preclinical and clinical studies
    • Alt, M.; Caselmann, W. H. Liver-directed gene therapy: molecular tools and current preclinical and clinical studies. J. Hepatol., 1995, 23 (6), 746-758.
    • (1995) J. Hepatol , vol.23 , Issue.6 , pp. 746-758
    • Alt, M.1    Caselmann, W.H.2
  • 30
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W. E.; Morimoto, R. I.; Dillin, A.; Kelly, J. W. Adapting proteostasis for disease intervention. Science, 2008, 319 (5865), 916-919.
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 31
    • 78650811435 scopus 로고    scopus 로고
    • Structural biology: Proteins in dynamic equilibrium
    • Bernado, P.; Blackledge, M. Structural biology: Proteins in dynamic equilibrium. Nature, 2010, 468 (7327), 1046-1048.
    • (2010) Nature , vol.468 , Issue.7327 , pp. 1046-1048
    • Bernado, P.1    Blackledge, M.2
  • 34
    • 0037062951 scopus 로고    scopus 로고
    • RNA interference
    • Hannon, G. J. RNA interference. Nature, 2002, 418 (6894), 244-251.
    • (2002) Nature , vol.418 , Issue.6894 , pp. 244-251
    • Hannon, G.J.1
  • 35
    • 80052137678 scopus 로고    scopus 로고
    • Combination therapy utilizing shRNA knockdown and an optimized resistant transgene for rescue of diseases caused by misfolded proteins
    • Li, C.; Xiao, P.; Gray, S. J.; Weinberg, M. S.; Samulski, R. J. Combination therapy utilizing shRNA knockdown and an optimized resistant transgene for rescue of diseases caused by misfolded proteins. Proc. Natl. Acad. Sci. U. S. A., 2011, 108 (34), 14258-14263.
    • (2011) Proc. Natl. Acad. Sci. U. S. A , vol.108 , Issue.34 , pp. 14258-14263
    • Li, C.1    Xiao, P.2    Gray, S.J.3    Weinberg, M.S.4    Samulski, R.J.5
  • 36
    • 0026658476 scopus 로고
    • Altered protein folding may be the molecular basis of most cases of cystic fibrosis
    • Thomas, P. J.; Ko, Y. H.; Pedersen, P. L. Altered protein folding may be the molecular basis of most cases of cystic fibrosis. FEBS Lett., 1992, 312 (1), 7-9.
    • (1992) FEBS Lett , vol.312 , Issue.1 , pp. 7-9
    • Thomas, P.J.1    Ko, Y.H.2    Pedersen, P.L.3
  • 37
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • Pind, S.; Riordan, J. R.; Williams, D. B. Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem., 1994, 269 (17), 12784-12788.
    • (1994) J. Biol. Chem , vol.269 , Issue.17 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    Williams, D.B.3
  • 38
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Yang, Y.; Janich, S.; Cohn, J. A.; Wilson, J. M. The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc. Natl. Acad. Sci. U. S. A., 1993, 90 (20), 9480-9484.
    • (1993) Proc. Natl. Acad. Sci. U. S. A , vol.90 , Issue.20 , pp. 9480-9484
    • Yang, Y.1    Janich, S.2    Cohn, J.A.3    Wilson, J.M.4
  • 39
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham, G. C.; Lu, Z.; King, S.; Sorscher, E.; Tousson, A.; Cyr, D. M. The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J., 1999, 18 (6), 1492-1505.
    • (1999) EMBO J , vol.18 , Issue.6 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 40
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward, C. L.; Kopito, R. R. Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J. Biol. Chem., 1994, 269 (41), 25710-25718.
    • (1994) J. Biol. Chem , vol.269 , Issue.41 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 41
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning, G. M.; Anderson, M. P.; Amara, J. F.; Marshall, J.; Smith, A. E.; Welsh, M. J. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature, 1992, 358 (6389), 761-764.
    • (1992) Nature , vol.358 , Issue.6389 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 42
    • 84055211699 scopus 로고    scopus 로고
    • Compromised mutant EFEMP1 secretion associated with macular dystrophy remedied by proteostasis network alteration
    • Hulleman J.D., Kaushal S., Balch W.E., Kelly J.W., Compromised mutant EFEMP1 secretion associated with macular dystrophy remedied by proteostasis network alteration. Mol Biol Cell.2011 22(24),4765-4775.
    • (2011) Mol Biol Cell , vol.22 , Issue.24 , pp. 4765-4775
    • Hulleman, J.D.1    Kaushal, S.2    Balch, W.E.3    Kelly, J.W.4
  • 43
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein
    • Brown, C. R.; Hong-Brown, L. Q.; Biwersi, J.; Verkman, A. S.; Welch, W. J. Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones, 1996, 1 (2), 117-125.
    • (1996) Cell Stress Chaperones , vol.1 , Issue.2 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 44
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey, P. H.; Clark, M. E.; Hand, S. C.; Bowlus, R. D.; Somero, G. N. Living with water stress: evolution of osmolyte systems. Science, 1982, 217 (4566), 1214-1222.
    • (1982) Science , vol.217 , Issue.4566 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 45
    • 46449109015 scopus 로고    scopus 로고
    • Structure and energetics of the hydrogen-bonded backbone in protein folding
    • Bolen, D. W.; Rose, G. D. Structure and energetics of the hydrogen-bonded backbone in protein folding. Annu. Rev. Biochem., 2008, 77, 339-362.
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 339-362
    • Bolen, D.W.1    Rose, G.D.2
  • 46
    • 68349098938 scopus 로고    scopus 로고
    • Correction of the disease phenotype of myocilin-causing glaucoma by a natural osmolyte
    • Jia, L. Y.; Gong, B.; Pang, C. P.; Huang, Y.; Lam, D. S.; Wang, N.; Yam, G. H. Correction of the disease phenotype of myocilin-causing glaucoma by a natural osmolyte. Invest. Ophthalmol. Vis. Sci., 2009, 50 (8), 3743-3749.
    • (2009) Invest. Ophthalmol. Vis. Sci , vol.50 , Issue.8 , pp. 3743-3749
    • Jia, L.Y.1    Gong, B.2    Pang, C.P.3    Huang, Y.4    Lam, D.S.5    Wang, N.6    Yam, G.H.7
  • 47
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency
    • Burrows, J. A.; Willis, L. K.; Perlmutter, D. H. Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency. Proc. Natl. Acad. Sci. U. S. A., 2000, 97 (4), 1796-1801.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , Issue.4 , pp. 1796-1801
    • Burrows, J.A.1    Willis, L.K.2    Perlmutter, D.H.3
  • 48
    • 0033521139 scopus 로고    scopus 로고
    • Misfolding of mutant aquaporin-2 water channels in nephrogenic diabetes insipidus
    • Tamarappoo, B. K.; Yang, B.; Verkman, A. S. Misfolding of mutant aquaporin-2 water channels in nephrogenic diabetes insipidus. J. Biol. Chem., 1999, 274 (49), 34825-34831.
    • (1999) J. Biol. Chem , vol.274 , Issue.49 , pp. 34825-34831
    • Tamarappoo, B.K.1    Yang, B.2    Verkman, A.S.3
  • 49
    • 0035955689 scopus 로고    scopus 로고
    • Natural osmolyte trimethylamine N-oxide corrects assembly defects of mutant branched-chain alpha-ketoacid decarboxylase in maple syrup urine disease
    • Song, J. L.; Chuang, D. T. Natural osmolyte trimethylamine N-oxide corrects assembly defects of mutant branched-chain alpha-ketoacid decarboxylase in maple syrup urine disease. J. Biol. Chem., 2001, 276 (43), 40241-40246.
    • (2001) J. Biol. Chem , vol.276 , Issue.43 , pp. 40241-40246
    • Song, J.L.1    Chuang, D.T.2
  • 51
    • 0033002710 scopus 로고    scopus 로고
    • Restoration of mutant TP53 to normal TP53 function by glycerol as a chemical chaperone
    • Ohnishi, T.; Ohnishi, K.; Wang, X.; Takahashi, A.; Okaichi, K. Restoration of mutant TP53 to normal TP53 function by glycerol as a chemical chaperone. Radiat. Res., 1999, 151 (4), 498-500.
    • (1999) Radiat. Res , vol.151 , Issue.4 , pp. 498-500
    • Ohnishi, T.1    Ohnishi, K.2    Wang, X.3    Takahashi, A.4    Okaichi, K.5
  • 52
    • 0034978522 scopus 로고    scopus 로고
    • Glycerol increases the yield and activity of human phenylalanine hydroxylase mutant enzymes produced in a prokaryotic expression system
    • Leandro, P.; Lechner, M. C.; Tavares de Almeida, I.; Konecki, D. Glycerol increases the yield and activity of human phenylalanine hydroxylase mutant enzymes produced in a prokaryotic expression system. Mol. Genet. Metab., 2001, 73 (2), 173-178.
    • (2001) Mol. Genet. Metab , vol.73 , Issue.2 , pp. 173-178
    • Leandro, P.1    Lechner, M.C.2    Tavares de Almeida, I.3    Konecki, D.4
  • 53
    • 0028968593 scopus 로고
    • Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing
    • Deen, P. M.; Croes, H.; van Aubel, R. A.; Ginsel, L. A.; van Os, C. H. Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing. J. Clin. Invest., 1995, 95 (5), 2291-2296.
    • (1995) J. Clin. Invest , vol.95 , Issue.5 , pp. 2291-2296
    • Deen, P.M.1    Croes, H.2    van Aubel, R.A.3    Ginsel, L.A.4    van Os, C.H.5
  • 54
    • 0036537523 scopus 로고    scopus 로고
    • Heteroligomerization of an Aquaporin-2 mutant with wild-type Aquaporin-2 and their misrouting to late endosomes/ lysosomes explains dominant nephrogenic diabetes insipidus
    • Marr, N.; Bichet, D. G.; Lonergan, M.; Arthus, M. F.; Jeck, N.; Seyberth, H. W.; Rosenthal, W.; van Os, C. H.; Oksche, A.; Deen, P. M. Heteroligomerization of an Aquaporin-2 mutant with wild-type Aquaporin-2 and their misrouting to late endosomes/ lysosomes explains dominant nephrogenic diabetes insipidus. Hum. Mol. Genet., 2002, 11 (7), 779-789.
    • (2002) Hum. Mol. Genet , vol.11 , Issue.7 , pp. 779-789
    • Marr, N.1    Bichet, D.G.2    Lonergan, M.3    Arthus, M.F.4    Jeck, N.5    Seyberth, H.W.6    Rosenthal, W.7    van Os, C.H.8    Oksche, A.9    Deen, P.M.10
  • 55
    • 0033037909 scopus 로고    scopus 로고
    • Differentiated human NT2-N neurons possess a high intracellular content of myo-inositol
    • Novak, J. E.; Turner, R. S.; Agranoff, B. W.; Fisher, S. K. Differentiated human NT2-N neurons possess a high intracellular content of myo-inositol. J. Neurochem., 1999, 72 (4), 1431-1440.
    • (1999) J. Neurochem , vol.72 , Issue.4 , pp. 1431-1440
    • Novak, J.E.1    Turner, R.S.2    Agranoff, B.W.3    Fisher, S.K.4
  • 56
    • 77749319656 scopus 로고    scopus 로고
    • A cellular perspective on conformational disease: The role of genetic background and proteostasis networks
    • Gidalevitz, T.; Kikis, E. A.; Morimoto, R. I. A cellular perspective on conformational disease: the role of genetic background and proteostasis networks. Curr. Opin. Struct. Biol., 2010, 20 (1), 23-32.
    • (2010) Curr. Opin. Struct. Biol , vol.20 , Issue.1 , pp. 23-32
    • Gidalevitz, T.1    Kikis, E.A.2    Morimoto, R.I.3
  • 57
    • 67650410543 scopus 로고    scopus 로고
    • Biological and chemical approaches to diseases of proteostasis deficiency
    • Powers, E. T.; Morimoto, R. I.; Dillin, A.; Kelly, J. W.; Balch, W. E. Biological and chemical approaches to diseases of proteostasis deficiency. Annu. Rev. Biochem., 2009, 78, 959-991.
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 959-991
    • Powers, E.T.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4    Balch, W.E.5
  • 58
    • 84866488172 scopus 로고    scopus 로고
    • The heat shock response: Systems biology of proteotoxic stress in aging and disease
    • Morimoto, R. I. The heat shock response: systems biology of proteotoxic stress in aging and disease. Cold Spring Harb. Symp. Quant. Biol., 2011, 76, 91-99.
    • (2011) Cold Spring Harb. Symp. Quant. Biol , vol.76 , pp. 91-99
    • Morimoto, R.I.1
  • 60
    • 0344059035 scopus 로고    scopus 로고
    • Structure-activity relations of successful pharma cologic chaperones for rescue of naturally occurring and manu factured mutants of the gonadotropin-releasing hormone receptor
    • Janovick, J. A.; Goulet, M.; Bush, E.; Greer, J.; Wettlaufer, D. G.; Conn, P. M. Structure-activity relations of successful pharma cologic chaperones for rescue of naturally occurring and manu factured mutants of the gonadotropin-releasing hormone receptor. J. Pharmacol. Exp. Ther., 2003, 305 (2), 608-614.
    • (2003) J. Pharmacol. Exp. Ther , vol.305 , Issue.2 , pp. 608-614
    • Janovick, J.A.1    Goulet, M.2    Bush, E.3    Greer, J.4    Wettlaufer, D.G.5    Conn, P.M.6
  • 61
    • 33746058237 scopus 로고    scopus 로고
    • Streamlining lead discovery by aligning in silico and high-throughput screening
    • Davies, J. W.; Glick, M.; Jenkins, J. L. Streamlining lead discovery by aligning in silico and high-throughput screening. Curr. Opin. Chem. Biol., 2006, 10 (4), 343-351.
    • (2006) Curr. Opin. Chem. Biol , vol.10 , Issue.4 , pp. 343-351
    • Davies, J.W.1    Glick, M.2    Jenkins, J.L.3
  • 62
    • 77950562400 scopus 로고    scopus 로고
    • Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyo trophic lateral sclerosis using computational methods
    • Nowak, R. J.; Cuny, G. D.; Choi, S.; Lansbury, P. T.; Ray, S. S. Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyo trophic lateral sclerosis using computational methods. J. Med. Chem., 2010, 53 (7), 2709-2718.
    • (2010) J. Med. Chem , vol.53 , Issue.7 , pp. 2709-2718
    • Nowak, R.J.1    Cuny, G.D.2    Choi, S.3    Lansbury, P.T.4    Ray, S.S.5
  • 64
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen, F. E.; Kelly, J. W. Therapeutic approaches to protein-misfolding diseases. Nature, 2003, 426 (6968), 905-909.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 65
    • 66649137718 scopus 로고    scopus 로고
    • Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability
    • Lieberman, R. L.; D'Aquino J.A.; Ringe, D.; Petsko, G. A. Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability. Biochemistry (Mosc).2009, 48 (22), 4816-4827.
    • (2009) Biochemistry (Mosc) , vol.48 , Issue.22 , pp. 4816-4827
    • Lieberman, R.L.1    D'aquino, J.A.2    Ringe, D.3    Petsko, G.A.4
  • 67
    • 14844361966 scopus 로고    scopus 로고
    • Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation
    • Ray, S. S.; Nowak, R. J.; Brown, R. H., Jr.; Lansbury, P. T., Jr. Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. Proc. Natl. Acad. Sci. U. S. A., 2005, 102 (10), 3639-3644.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , Issue.10 , pp. 3639-3644
    • Ray, S.S.1    Nowak, R.J.2    Brown Jr., R.H.3    Lansbury Jr., P.T.4
  • 68
    • 24644464284 scopus 로고    scopus 로고
    • Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening
    • Pedemonte, N.; Lukacs, G. L.; Du, K.; Caci, E.; Zegarra-Moran, O.; Galietta, L. J.; Verkman, A. S. Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening. J. Clin. Invest., 2005, 115 (9), 2564-2571.
    • (2005) J. Clin. Invest , vol.115 , Issue.9 , pp. 2564-2571
    • Pedemonte, N.1    Lukacs, G.L.2    Du, K.3    Caci, E.4    Zegarra-Moran, O.5    Galietta, L.J.6    Verkman, A.S.7
  • 70
    • 34547557698 scopus 로고    scopus 로고
    • Correctors of protein trafficking defects identified by a novel high-throughput screening assay
    • Carlile, G. W.; Robert, R.; Zhang, D.; Teske, K. A.; Luo, Y.; Hanrahan, J. W.; Thomas, D. Y. Correctors of protein trafficking defects identified by a novel high-throughput screening assay. Chembiochem, 2007, 8 (9), 1012-1020.
    • (2007) Chembiochem , vol.8 , Issue.9 , pp. 1012-1020
    • Carlile, G.W.1    Robert, R.2    Zhang, D.3    Teske, K.A.4    Luo, Y.5    Hanrahan, J.W.6    Thomas, D.Y.7
  • 71
    • 59949099584 scopus 로고    scopus 로고
    • Discovery of amyloid-beta aggregation inhibitors using an engineered assay for intracellu-lar protein folding and solubility
    • Lee L.L., Ha H., Chang Y.T., DeLisa M.P., Discovery of amyloid-beta aggregation inhibitors using an engineered assay for intracellu-lar protein folding and solubility. Protein Sci. 2009 18(2), 277-286.
    • (2009) Protein Sci , vol.18 , Issue.2 , pp. 277-286
    • Lee, L.L.1    Ha, H.2    Chang, Y.T.3    Delisa, M.P.4
  • 72
    • 33748588165 scopus 로고    scopus 로고
    • Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
    • Ignatova, Z.; Gierasch, L. M. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc. Natl. Acad. Sci. U. S. A., 2006, 103 (36), 13357-13361.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , Issue.36 , pp. 13357-13361
    • Ignatova, Z.1    Gierasch, L.M.2
  • 74
    • 33749850046 scopus 로고    scopus 로고
    • Universal screening methods and applications of ThermoFluor
    • Cummings, M. D.; Farnum, M. A.; Nelen, M. I. Universal screening methods and applications of ThermoFluor. J Biomol Screen, 2006, 11 (7), 854-863.
    • (2006) J Biomol Screen , vol.11 , Issue.7 , pp. 854-863
    • Cummings, M.D.1    Farnum, M.A.2    Nelen, M.I.3
  • 75
    • 67849129183 scopus 로고    scopus 로고
    • High-throughput thermal scanning: A general, rapid dye-binding thermal shift screen for protein engineering
    • Lavinder, J. J.; Hari, S. B.; Sullivan, B. J.; Magliery, T. J. High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering. J. Am. Chem. Soc., 2009, 131 (11), 3794-3795.
    • (2009) J. Am. Chem. Soc , vol.131 , Issue.11 , pp. 3794-3795
    • Lavinder, J.J.1    Hari, S.B.2    Sullivan, B.J.3    Magliery, T.J.4
  • 76
    • 79960750159 scopus 로고    scopus 로고
    • Therapeutic rescue of misfolded mutants: Validation of primary high throughput screens for identification of pharmacoperone drugs
    • Janovick, J. A.; Park, B. S.; Conn, P. M. Therapeutic rescue of misfolded mutants: validation of primary high throughput screens for identification of pharmacoperone drugs. PLoS ONE, 2011, 6 (7), e22784.
    • (2011) PLoS ONE , vol.6 , Issue.7
    • Janovick, J.A.1    Park, B.S.2    Conn, P.M.3
  • 77
    • 0033936317 scopus 로고    scopus 로고
    • Multistep mechanism of substrate binding determines chaperone activity of Hsp70
    • Mayer, M. P.; Schroder, H.; Rudiger, S.; Paal, K.; Laufen, T.; Bukau, B. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol., 2000, 7 (7), 586-593.
    • (2000) Nat. Struct. Biol , vol.7 , Issue.7 , pp. 586-593
    • Mayer, M.P.1    Schroder, H.2    Rudiger, S.3    Paal, K.4    Laufen, T.5    Bukau, B.6
  • 78
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga, H. H.; Craig, E. A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol., 2010, 11 (8), 579-592.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , Issue.8 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 79
    • 79955984427 scopus 로고    scopus 로고
    • Conformational dynamics of the molecular chaperone Hsp90
    • Krukenberg, K. A.; Street, T. O.; Lavery, L. A.; Agard, D. A. Conformational dynamics of the molecular chaperone Hsp90. Q. Rev. Biophys., 2011, 44 (2), 229-255.
    • (2011) Q. Rev. Biophys , vol.44 , Issue.2 , pp. 229-255
    • Krukenberg, K.A.1    Street, T.O.2    Lavery, L.A.3    Agard, D.A.4
  • 80
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler, A.; Lurz, R.; Lueder, G.; Priller, J.; Lehrach, H.; Hayer-Hartl, M. K.; Hartl, F. U.; Wanker, E. E. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet., 2001, 10 (12), 1307-1315.
    • (2001) Hum. Mol. Genet , vol.10 , Issue.12 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Lehrach, H.5    Hayer-Hartl, M.K.6    Hartl, F.U.7    Wanker, E.E.8
  • 81
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck, P. K.; Chan, H. Y.; Trojanowski, J. Q.; Lee, V. M.; Bonini, N. M. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science, 2002, 295 (5556), 865-868.
    • (2002) Science , vol.295 , Issue.5556 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 84
    • 27144456262 scopus 로고    scopus 로고
    • The amino-terminal domain of ClpB supports binding to strongly aggregated proteins
    • Barnett, M. E.; Nagy, M.; Kedzierska, S.; Zolkiewski, M. The amino-terminal domain of ClpB supports binding to strongly aggregated proteins. J. Biol. Chem., 2005, 280 (41), 34940-34945.
    • (2005) J. Biol. Chem , vol.280 , Issue.41 , pp. 34940-34945
    • Barnett, M.E.1    Nagy, M.2    Kedzierska, S.3    Zolkiewski, M.4
  • 86
    • 10044275315 scopus 로고    scopus 로고
    • Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
    • Schlieker, C.; Tews, I.; Bukau, B.; Mogk, A. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. FEBS Lett., 2004, 578 (3), 351-356.
    • (2004) FEBS Lett , vol.578 , Issue.3 , pp. 351-356
    • Schlieker, C.1    Tews, I.2    Bukau, B.3    Mogk, A.4
  • 87
    • 3142657524 scopus 로고    scopus 로고
    • Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104
    • Lum, R.; Tkach, J. M.; Vierling, E.; Glover, J. R. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J. Biol. Chem., 2004, 279 (28), 29139-29146.
    • (2004) J. Biol. Chem , vol.279 , Issue.28 , pp. 29139-29146
    • Lum, R.1    Tkach, J.M.2    Vierling, E.3    Glover, J.R.4
  • 89
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff, Y. O.; Lindquist, S. L.; Ono, B.; Inge-Vechtomov, S. G.; Liebman, S. W. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science, 1995, 268 (5212), 880-884.
    • (1995) Science , vol.268 , Issue.5212 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 90
    • 33846941900 scopus 로고    scopus 로고
    • Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity
    • Doyle, S. M.; Shorter, J.; Zolkiewski, M.; Hoskins, J. R.; Lindquist, S.; Wickner, S. Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat. Struct. Mol. Biol., 2007, 14 (2), 114-122.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , Issue.2 , pp. 114-122
    • Doyle, S.M.1    Shorter, J.2    Zolkiewski, M.3    Hoskins, J.R.4    Lindquist, S.5    Wickner, S.6
  • 91
    • 78049498592 scopus 로고    scopus 로고
    • ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage
    • Estorninho, M.; Smith, H.; Thole, J.; Harders-Westerveen, J.; Kierzek, A.; Butler, R. E.; Neyrolles, O.; Stewart, G. R. ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage. Microbiology, 2010, 156 (Pt 11), 3445-3455.
    • (2010) Microbiology , vol.156 , Issue.Pt 11 , pp. 3445-3455
    • Estorninho, M.1    Smith, H.2    Thole, J.3    Harders-Westerveen, J.4    Kierzek, A.5    Butler, R.E.6    Neyrolles, O.7    Stewart, G.R.8
  • 93
    • 0032852245 scopus 로고    scopus 로고
    • A novel role for 100 kD heat shock proteins in the parasite Leishmania donovani
    • Krobitsch, S.; Clos, J. A novel role for 100 kD heat shock proteins in the parasite Leishmania donovani. Cell Stress Chaperones, 1999, 4 (3), 191-198.
    • (1999) Cell Stress Chaperones , vol.4 , Issue.3 , pp. 191-198
    • Krobitsch, S.1    Clos, J.2
  • 94
    • 0034634334 scopus 로고    scopus 로고
    • Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli
    • Kim, K. I.; Cheong, G. W.; Park, S. C.; Ha, J. S.; Woo, K. M.; Choi, S. J.; Chung, C. H. Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli. J. Mol. Biol., 2000, 303 (5), 655-666.
    • (2000) J. Mol. Biol , vol.303 , Issue.5 , pp. 655-666
    • Kim, K.I.1    Cheong, G.W.2    Park, S.C.3    Ha, J.S.4    Woo, K.M.5    Choi, S.J.6    Chung, C.H.7
  • 95
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    • Parsell, D. A.; Kowal, A. S.; Lindquist, S. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J. Biol. Chem., 1994, 269 (6), 4480-4487.
    • (1994) J. Biol. Chem , vol.269 , Issue.6 , pp. 4480-4487
    • Parsell, D.A.1    Kowal, A.S.2    Lindquist, S.3
  • 96
    • 0035793721 scopus 로고    scopus 로고
    • The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites
    • Schlee, S.; Groemping, Y.; Herde, P.; Seidel, R.; Reinstein, J. The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites. J. Mol. Biol., 2001, 306 (4), 889-899.
    • (2001) J. Mol. Biol , vol.306 , Issue.4 , pp. 889-899
    • Schlee, S.1    Groemping, Y.2    Herde, P.3    Seidel, R.4    Reinstein, J.5
  • 97
    • 0037155139 scopus 로고    scopus 로고
    • Roles of the two ATP binding sites of ClpB from Thermus thermophilus
    • Watanabe, Y. H.; Motohashi, K.; Yoshida, M. Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J. Biol. Chem., 2002, 277 (8), 5804-5809.
    • (2002) J. Biol. Chem , vol.277 , Issue.8 , pp. 5804-5809
    • Watanabe, Y.H.1    Motohashi, K.2    Yoshida, M.3
  • 98
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
    • Zolkiewski, M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem., 1999, 274 (40), 28083-28086.
    • (1999) J. Biol. Chem , vol.274 , Issue.40 , pp. 28083-28086
    • Zolkiewski, M.1
  • 99
    • 0024439338 scopus 로고
    • Demonstration by genetic suppression of interaction of GroE products with many proteins
    • Van Dyk, T. K.; Gatenby, A. A.; LaRossa, R. A. Demonstration by genetic suppression of interaction of GroE products with many proteins. Nature, 1989, 342 (6248), 451-453.
    • (1989) Nature , vol.342 , Issue.6248 , pp. 451-453
    • van Dyk, T.K.1    Gatenby, A.A.2    Larossa, R.A.3
  • 100
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki, N.; Tawfik, D. S. Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature, 2009, 459 (7247), 668-673.
    • (2009) Nature , vol.459 , Issue.7247 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 102
    • 0025940841 scopus 로고
    • Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
    • Viitanen, P. V.; Donaldson, G. K.; Lorimer, G. H.; Lubben, T. H.; Gatenby, A. A. Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry (Mosc).1991, 30 (40), 9716-9723.
    • (1991) Biochemistry (Mosc) , vol.30 , Issue.40 , pp. 9716-9723
    • Viitanen, P.V.1    Donaldson, G.K.2    Lorimer, G.H.3    Lubben, T.H.4    Gatenby, A.A.5
  • 103
    • 0032582806 scopus 로고    scopus 로고
    • Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein
    • Smith, K. E.; Voziyan, P. A.; Fisher, M. T. Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein. J. Biol. Chem., 1998, 273 (44), 28677-28681.
    • (1998) J. Biol. Chem , vol.273 , Issue.44 , pp. 28677-28681
    • Smith, K.E.1    Voziyan, P.A.2    Fisher, M.T.3
  • 106
    • 0033822333 scopus 로고    scopus 로고
    • Refolding a glutamine synthetase truncation mutant in vitro: Identifying superior condi tions using a combination of chaperonins and osmolytes
    • Voziyan, P. A.; Jadhav, L.; Fisher, M. T. Refolding a glutamine synthetase truncation mutant in vitro: identifying superior condi tions using a combination of chaperonins and osmolytes. J. Pharm. Sci., 2000, 89 (8), 1036-1045.
    • (2000) J. Pharm. Sci , vol.89 , Issue.8 , pp. 1036-1045
    • Voziyan, P.A.1    Jadhav, L.2    Fisher, M.T.3
  • 107
    • 0029875225 scopus 로고    scopus 로고
    • Nucleotide binding-promoted confor mational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL
    • Lin, Z.; Eisenstein, E. Nucleotide binding-promoted confor mational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL. Proc. Natl. Acad. Sci. U. S. A., 1996, 93 (5), 1977-1981.
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , Issue.5 , pp. 1977-1981
    • Lin, Z.1    Eisenstein, E.2
  • 108
    • 0029090130 scopus 로고
    • Kinetic analysis of interactions between GroEL and reduced alpha-lactalbumin. Effect of GroES and nucleotides
    • Murai, N.; Taguchi, H.; Yoshida, M. Kinetic analysis of interactions between GroEL and reduced alpha-lactalbumin. Effect of GroES and nucleotides. J. Biol. Chem., 1995, 270 (34), 19957-19963.
    • (1995) J. Biol. Chem , vol.270 , Issue.34 , pp. 19957-19963
    • Murai, N.1    Taguchi, H.2    Yoshida, M.3
  • 109
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton, W. A.; Horwich, A. L. GroEL-mediated protein folding. Protein Sci., 1997, 6 (4), 743-760.
    • (1997) Protein Sci , vol.6 , Issue.4 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 110
    • 0026446343 scopus 로고
    • Prevention of protein denaturation under heat stress by the chaperonin Hsp60
    • Martin, J.; Horwich, A. L.; Hartl, F. U. Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science, 1992, 258 (5084), 995-998.
    • (1992) Science , vol.258 , Issue.5084 , pp. 995-998
    • Martin, J.1    Horwich, A.L.2    Hartl, F.U.3
  • 111
    • 0034490988 scopus 로고    scopus 로고
    • Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: Off-pathway aggregation propensity does not determine the co-chaperonin requirement
    • Voziyan, P. A. Fisher, M. T. Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the co-chaperonin requirement. Protein Sci., 2000, 9 (12), 2405-2412.
    • (2000) Protein Sci , vol.9 , Issue.12 , pp. 2405-2412
    • Voziyan, P.A.1    Fisher, M.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.