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Volumn 7, Issue 1, 2014, Pages 9-14

Mechanisms of protein-folding diseases at a glance

Author keywords

Disease; Misfolding; Protein; Yeast

Indexed keywords

AMYLOID; CHAPERONE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; MUTANT PROTEIN; PREALBUMIN; PROTEIN P53;

EID: 84892408458     PISSN: 17548403     EISSN: 17548411     Source Type: Journal    
DOI: 10.1242/dmm.013474     Document Type: Article
Times cited : (234)

References (72)
  • 2
    • 0034112079 scopus 로고    scopus 로고
    • Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck)
    • Bijlmakers, M. J. and Marsh, M. (2000). Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck). Mol. Biol. Cell 11, 1585-1595.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1585-1595
    • Bijlmakers, M.J.1    Marsh, M.2
  • 3
    • 79955754372 scopus 로고    scopus 로고
    • Structure-dependent impairment of intracellular apolipoprotein E4 trafficking and its detrimental effects are rescued by small-molecule structure correctors
    • Brodbeck, J., McGuire, J., Liu, Z. P., Meyer-Franke, A., Balestra, M. E., Jeong, D. E., Pleiss, M., McComas, C., Hess, F., Witter, D. et al. (2011). Structure-dependent impairment of intracellular apolipoprotein E4 trafficking and its detrimental effects are rescued by small-molecule structure correctors. J. Biol. Chem. 286, 17217-17226.
    • (2011) J. Biol. Chem , vol.286 , pp. 17217-17226
    • Brodbeck, J.1    McGuire, J.2    Liu, Z.P.3    Meyer-Franke, A.4    Balestra, M.E.5    Jeong, D.E.6    Pleiss, M.7    McComas, C.8    Hess, F.9    Witter, D.10
  • 4
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B. and Lansbury, P. T. (2003). Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267-298.
    • (2003) Annu. Rev. Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 6
    • 79960296401 scopus 로고    scopus 로고
    • Chemical chaperones protect epidermolysis bullosa simplex keratinocytes from heat stress-induced keratin aggregation: Involvement of heat shock proteins and MAP kinases
    • Chamcheu, J. C., Navsaria, H., Pihl-Lundin, I., Liovic, M., Vahlquist, A. and Törmä, H. (2011b). Chemical chaperones protect epidermolysis bullosa simplex keratinocytes from heat stress-induced keratin aggregation: involvement of heat shock proteins and MAP kinases. J. Invest. Dermatol. 131, 1684-1691.
    • (2011) J. Invest. Dermatol , vol.131 , pp. 1684-1691
    • Chamcheu, J.C.1    Navsaria, H.2    Pihl-Lundin, I.3    Liovic, M.4    Vahlquist, A.5    Törmä, H.6
  • 7
    • 84863104815 scopus 로고    scopus 로고
    • Progress towards genetic and pharmacological therapies for keratin genodermatoses: Current perspective and future promise
    • Chamcheu, J. C., Wood, G. S., Siddiqui, I. A., Syed, D. N., Adhami, V. M., Teng, J. M. and Mukhtar, H. (2012). Progress towards genetic and pharmacological therapies for keratin genodermatoses: current perspective and future promise. Exp. Dermatol. 21, 481-489.
    • (2012) Exp. Dermatol , vol.21 , pp. 481-489
    • Chamcheu, J.C.1    Wood, G.S.2    Siddiqui, I.A.3    Syed, D.N.4    Adhami, V.M.5    Teng, J.M.6    Mukhtar, H.7
  • 9
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. and Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 10
    • 82755181717 scopus 로고    scopus 로고
    • The cellular pathology of lysosomal diseases
    • Cox, T. M. and Cachón-González, M. B. (2012). The cellular pathology of lysosomal diseases. J. Pathol. 226, 241-254.
    • (2012) J. Pathol , vol.226 , pp. 241-254
    • Cox, T.M.1    Cachón-González, M.B.2
  • 11
    • 84869761071 scopus 로고    scopus 로고
    • The protein-folding problem, 50 years on
    • Dill, K. A. and MacCallum, J. L. (2012). The protein-folding problem, 50 years on. Science 338, 1042-1046.
    • (2012) Science , vol.338 , pp. 1042-1046
    • Dill, K.A.1    Maccallum, J.L.2
  • 12
    • 0029766916 scopus 로고    scopus 로고
    • Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins
    • Dong, L. M. and Weisgraber, K. H. (1996). Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins. J. Biol. Chem. 271, 19053-19057.
    • (1996) J. Biol. Chem , vol.271 , pp. 19053-19057
    • Dong, L.M.1    Weisgraber, K.H.2
  • 13
    • 0028092997 scopus 로고
    • Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms
    • Dong, L. M., Wilson, C., Wardell, M. R., Simmons, T., Mahley, R. W., Weisgraber, K. H. and Agard, D. A. (1994). Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms. J. Biol. Chem. 269, 22358-22365.
    • (1994) J. Biol. Chem , vol.269 , pp. 22358-22365
    • Dong, L.M.1    Wilson, C.2    Wardell, M.R.3    Simmons, T.4    Mahley, R.W.5    Weisgraber, K.H.6    Agard, D.A.7
  • 15
    • 33746099650 scopus 로고    scopus 로고
    • Protein aggregation in crowded environments
    • Ellis, R. J. and Minton, A. P. (2006). Protein aggregation in crowded environments. Biol. Chem. 387, 485-497.
    • (2006) Biol. Chem , vol.387 , pp. 485-497
    • Ellis, R.J.1    Minton, A.P.2
  • 16
    • 0030823158 scopus 로고    scopus 로고
    • Effects of age, sex, and ethnicity on the association between apolipoprotein e genotype and Alzheimer disease. A meta-analysis
    • APOE and Alzheimer Disease Meta Analysis Consortium
    • Farrer, L. A., Cupples, L. A., Haines, J. L., Hyman, B., Kukull, W. A., Mayeux, R., Myers, R. H., Pericak-Vance, M. A., Risch, N., van Duijn, C. M.; APOE and Alzheimer Disease Meta Analysis Consortium (1997). Effects of age, sex, and ethnicity on the association between apolipoprotein E genotype and Alzheimer disease. A meta-analysis. JAMA 278, 1349-1356.
    • (1997) JAMA , vol.278 , pp. 1349-1356
    • Farrer, L.A.1    Cupples, L.A.2    Haines, J.L.3    Hyman, B.4    Kukull, W.A.5    Mayeux, R.6    Myers, R.H.7    Pericak-Vance, M.A.8    Risch, N.9    Van Duijn, C.M.10
  • 17
    • 84862636275 scopus 로고    scopus 로고
    • Mutant p53: One name, many proteins
    • Freed-Pastor, W. A. and Prives, C. (2012). Mutant p53: one name, many proteins. Genes Dev. 26, 1268-1286.
    • (2012) Genes Dev , vol.26 , pp. 1268-1286
    • Freed-Pastor, W.A.1    Prives, C.2
  • 18
    • 0027522365 scopus 로고
    • The p53 protein is an unusually shaped tetramer that binds directly to DNA
    • Friedman, P. N., Chen, X., Bargonetti, J. and Prives, C. (1993). The p53 protein is an unusually shaped tetramer that binds directly to DNA. Proc. Natl. Acad. Sci. USA 90, 3319-3323.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3319-3323
    • Friedman, P.N.1    Chen, X.2    Bargonetti, J.3    Prives, C.4
  • 19
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • Futerman, A. H. and van Meer, G. (2004). The cell biology of lysosomal storage disorders. Nat. Rev. Mol. Cell Biol. 5, 554-565.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 554-565
    • Futerman, A.H.1    Van Meer, G.2
  • 20
    • 84871650725 scopus 로고    scopus 로고
    • Small molecules that target protein misfolding
    • Gavrin, L. K., Denny, R. A. and Saiah, E. (2012). Small molecules that target protein misfolding. J. Med. Chem. 55, 10823-10843.
    • (2012) J. Med. Chem , vol.55 , pp. 10823-10843
    • Gavrin, L.K.1    Denny, R.A.2    Saiah, E.3
  • 21
    • 0036430085 scopus 로고    scopus 로고
    • Membrane transport in sickle cell disease
    • Gibson, J. S. and Ellory, J. C. (2002). Membrane transport in sickle cell disease. Blood Cells Mol. Dis. 28, 303-314.
    • (2002) Blood Cells Mol. Dis , vol.28 , pp. 303-314
    • Gibson, J.S.1    Ellory, J.C.2
  • 22
    • 4644293577 scopus 로고    scopus 로고
    • Conformation-dependent antibodies target diseases of protein misfolding
    • Glabe, C. G. (2004). Conformation-dependent antibodies target diseases of protein misfolding. Trends Biochem. Sci. 29, 542-547.
    • (2004) Trends Biochem. Sci , vol.29 , pp. 542-547
    • Glabe, C.G.1
  • 23
    • 53049096591 scopus 로고    scopus 로고
    • Phenotype, diagnosis, and treatment of Gaucher's disease
    • Grabowski, G. A. (2008). Phenotype, diagnosis, and treatment of Gaucher's disease. Lancet 372, 1263-1271.
    • (2008) Lancet , vol.372 , pp. 1263-1271
    • Grabowski, G.A.1
  • 24
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A. and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 25
    • 28244499949 scopus 로고    scopus 로고
    • Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and - 12, NFkappaB, and BAP31 but not the unfolded protein response
    • Hidvegi, T., Schmidt, B. Z., Hale, P. and Perlmutter, D. H. (2005). Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and - 12, NFkappaB, and BAP31 but not the unfolded protein response. J. Biol. Chem. 280, 39002-39015.
    • (2005) J. Biol. Chem , vol.280 , pp. 39002-39015
    • Hidvegi, T.1    Schmidt, B.Z.2    Hale, P.3    Perlmutter, D.H.4
  • 27
    • 70449313520 scopus 로고
    • A terminal peptide sequence of human haemoglobin?
    • Hunt, J. A. and Ingram, V. M. (1959). A terminal peptide sequence of human haemoglobin? Nature 184 Suppl. 9, 640-641.
    • (1959) Nature , vol.184 , Issue.SUPPL. 9 , pp. 640-641
    • Hunt, J.A.1    Ingram, V.M.2
  • 28
    • 84872346089 scopus 로고    scopus 로고
    • Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy
    • Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q. and Lee, V. M. (2013). Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy. J. Neurosci. 33, 1024-1037.
    • (2013) J. Neurosci , vol.33 , pp. 1024-1037
    • Iba, M.1    Guo, J.L.2    McBride, J.D.3    Zhang, B.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 29
    • 1842337282 scopus 로고
    • Gene mutations in human haemoglobin: The chemical difference between normal and sickle cell haemoglobin
    • Ingram, V. M. (1957). Gene mutations in human haemoglobin: the chemical difference between normal and sickle cell haemoglobin. Nature 180, 326-328.
    • (1957) Nature , vol.180 , pp. 326-328
    • Ingram V., .M.1
  • 30
    • 78149452881 scopus 로고    scopus 로고
    • Protein homeostasis and the phenotypic manifestation of genetic diversity: Principles and mechanisms
    • Jarosz, D. F., Taipale, M. and Lindquist, S. (2010). Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annu. Rev. Genet. 44, 189-216.
    • (2010) Annu. Rev. Genet , vol.44 , pp. 189-216
    • Jarosz, D.F.1    Taipale, M.2    Lindquist, S.3
  • 31
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W. and Glabe, C. G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 32
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat, M. H., Jones, S. N. and Vousden, K. H. (1997). Regulation of p53 stability by Mdm2. Nature 387, 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 33
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T. and Lansbury, P. T., Jr (2002). Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418, 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 34
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: Progress and prognosis
    • Lindquist, S. L. and Kelly, J. W. (2011). Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb. Perspect. Biol. 3, a004507.
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Lindquist, S.L.1    Kelly, J.W.2
  • 36
    • 0026755363 scopus 로고
    • The mechanism of Z alpha 1-antitrypsin accumulation in the liver
    • Lomas, D. A., Evans, D. L., Finch, J. T. and Carrell, R. W. (1992). The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 357, 605-607.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 37
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O'Brien, P., Trojanowski, J. Q. and Lee, V. M. (2012). Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338, 949-953.
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 38
    • 0028173205 scopus 로고
    • Amyloidassociated proteins alpha 1-antichymotrypsin and apolipoprotein e promote assembly of Alzheimer beta-protein into filaments
    • Ma, J. Y., Yee, A., Brewer, H. B., Jr, Das, S. and Potter, H. (1994). Amyloidassociated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments. Nature 372, 92-94.
    • (1994) Nature , vol.372 , pp. 92-94
    • Ma, J.Y.1    Yee, A.2    Brewer Jr., H.B.3    Das, S.4    Potter, H.5
  • 39
    • 0029786498 scopus 로고    scopus 로고
    • Long-term treatment of girls with ornithine transcarbamylase deficiency
    • Maestri, N. E., Brusilow, S. W., Clissold, D. B. and Bassett, S. S. (1996). Long-term treatment of girls with ornithine transcarbamylase deficiency. N. Engl. J. Med. 335, 855-860.
    • (1996) N. Engl. J. Med , vol.335 , pp. 855-860
    • Maestri, N.E.1    Brusilow, S.W.2    Clissold, D.B.3    Bassett, S.S.4
  • 41
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M. and Cyr, D. M. (2001). The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 3, 100-105.
    • (2001) Nat. Cell Biol , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 42
    • 0025731379 scopus 로고
    • Cotranslation of activated mutant p53 with wild type drives the wild-type p53 protein into the mutant conformation
    • Milner, J. and Medcalf, E. A. (1991). Cotranslation of activated mutant p53 with wild type drives the wild-type p53 protein into the mutant conformation. Cell 65, 765-774.
    • (1991) Cell , vol.65 , pp. 765-774
    • Milner, J.1    Medcalf, E.A.2
  • 43
    • 0026060757 scopus 로고
    • Tumor suppressor p53: Analysis of wild-type and mutant p53 complexes
    • Milner, J., Medcalf, E. A. and Cook, A. C. (1991). Tumor suppressor p53: analysis of wild-type and mutant p53 complexes. Mol. Cell. Biol. 11, 12-19.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 12-19
    • Milner, J.1    Medcalf, E.A.2    Cook, A.C.3
  • 44
    • 84861319134 scopus 로고    scopus 로고
    • A review of augmentation therapy for alpha-1 antitrypsin deficiency
    • Mohanka, M., Khemasuwan, D. and Stoller, J. K. (2012). A review of augmentation therapy for alpha-1 antitrypsin deficiency. Expert Opin. Biol. Ther. 12, 685-700.
    • (2012) Expert Opin. Biol. Ther , vol.12 , pp. 685-700
    • Mohanka, M.1    Khemasuwan, D.2    Stoller, J.K.3
  • 45
    • 84862868531 scopus 로고    scopus 로고
    • Spreading of neurodegenerative pathology via neuron-toneuron transmission of beta-amyloid
    • Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J. and Hallbeck, M. (2012). Spreading of neurodegenerative pathology via neuron-toneuron transmission of beta-amyloid. J. Neurosci. 32, 8767-8777.
    • (2012) J. Neurosci , vol.32 , pp. 8767-8777
    • Nath, S.1    Agholme, L.2    Kurudenkandy, F.R.3    Granseth, B.4    Marcusson, J.5    Hallbeck, M.6
  • 46
    • 0028232662 scopus 로고
    • Differential effects of apolipoproteins E3 and E4 on neuronal growth in vitro
    • Nathan, B. P., Bellosta, S., Sanan, D. A., Weisgraber, K. H., Mahley, R. W. and Pitas, R. E. (1994). Differential effects of apolipoproteins E3 and E4 on neuronal growth in vitro. Science 264, 850-852.
    • (1994) Science , vol.264 , pp. 850-852
    • Nathan, B.P.1    Bellosta, S.2    Sanan, D.A.3    Weisgraber, K.H.4    Mahley, R.W.5    Pitas, R.E.6
  • 47
    • 56449094841 scopus 로고    scopus 로고
    • Autophagy and the ubiquitinproteasome system: Collaborators in neuroprotection
    • Nedelsky, N. B., Todd, P. K. and Taylor, J. P. (2008). Autophagy and the ubiquitinproteasome system: collaborators in neuroprotection. Biochim. Biophys. Acta 1782, 691-699.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 691-699
    • Nedelsky, N.B.1    Todd, P.K.2    Taylor, J.P.3
  • 48
    • 84855987854 scopus 로고    scopus 로고
    • Structure-based design of conformation- and sequence-specific antibodies against amyloid β
    • Perchiacca, J. M., Ladiwala, A. R., Bhattacharya, M. and Tessier, P. M. (2012). Structure-based design of conformation- and sequence-specific antibodies against amyloid β. Proc. Natl. Acad. Sci. USA 109, 84-89.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 84-89
    • Perchiacca, J.M.1    Ladiwala, A.R.2    Bhattacharya, M.3    Tessier, P.M.4
  • 49
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • Qu, B. H., Strickland, E. H. and Thomas, P. J. (1997). Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding. J. Biol. Chem. 272, 15739-15744.
    • (1997) J. Biol. Chem , vol.272 , pp. 15739-15744
    • Qu, B.H.1    Strickland, E.H.2    Thomas, P.J.3
  • 51
    • 26444609722 scopus 로고    scopus 로고
    • ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity
    • Ron, I. and Horowitz, M. (2005). ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum. Mol. Genet. 14, 2387-2398.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 2387-2398
    • Ron, I.1    Horowitz, M.2
  • 53
    • 9444225484 scopus 로고    scopus 로고
    • Mechanical stress induces profound remodelling of keratin filaments and cell junctions in epidermolysis bullosa simplex keratinocytes
    • Russell, D., Andrews, P. D., James, J. and Lane, E. B. (2004). Mechanical stress induces profound remodelling of keratin filaments and cell junctions in epidermolysis bullosa simplex keratinocytes. J. Cell Sci. 117, 5233-5243.
    • (2004) J. Cell Sci , vol.117 , pp. 5233-5243
    • Russell, D.1    Andrews, P.D.2    James, J.3    Lane, E.B.4
  • 54
    • 0037180511 scopus 로고    scopus 로고
    • Chemical chaperones increase the cellular activity of N370S betaglucosidase: A therapeutic strategy for Gaucher disease
    • Sawkar, A. R., Cheng, W. C., Beutler, E., Wong, C. H., Balch, W. E. and Kelly, J. W. (2002). Chemical chaperones increase the cellular activity of N370S betaglucosidase: a therapeutic strategy for Gaucher disease. Proc. Natl. Acad. Sci. USA 99, 15428-15433.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15428-15433
    • Sawkar, A.R.1    Cheng, W.C.2    Beutler, E.3    Wong, C.H.4    Balch, W.E.5    Kelly, J.W.6
  • 55
    • 27744459735 scopus 로고    scopus 로고
    • Gaucher disease-associated glucocerebrosidases show mutation-dependent chemical chaperoning profiles
    • Sawkar, A. R., Adamski-Werner, S. L., Cheng, W. C., Wong, C. H., Beutler, E., Zimmer, K. P. and Kelly, J. W. (2005). Gaucher disease-associated glucocerebrosidases show mutation-dependent chemical chaperoning profiles. Chem. Biol. 12, 1235-1244.
    • (2005) Chem. Biol , vol.12 , pp. 1235-1244
    • Sawkar, A.R.1    Adamski-Werner, S.L.2    Cheng, W.C.3    Wong, C.H.4    Beutler, E.5    Zimmer, K.P.6    Kelly, J.W.7
  • 56
    • 33745293617 scopus 로고    scopus 로고
    • Therapeutic strategies to ameliorate lysosomal storage disorders - A focus on Gaucher disease
    • Sawkar, A. R., D'Haeze, W. and Kelly, J. W. (2006). Therapeutic strategies to ameliorate lysosomal storage disorders-a focus on Gaucher disease. Cell. Mol. Life Sci. 63, 1179-1192.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 1179-1192
    • Sawkar, A.R.1    D'Haeze, W.2    Kelly, J.W.3
  • 57
    • 33751082387 scopus 로고    scopus 로고
    • Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis
    • Sekijima, Y., Dendle, M. A. and Kelly, J. W. (2006). Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis. Amyloid 13, 236-249.
    • (2006) Amyloid , vol.13 , pp. 236-249
    • Sekijima, Y.1    Dendle, M.A.2    Kelly, J.W.3
  • 59
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith, M. H., Ploegh, H. L. and Weissman, J. S. (2011). Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 334, 1086-1090.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 60
    • 71349083669 scopus 로고    scopus 로고
    • Conformational diseases: Looking into the eyes
    • Surguchev, A. and Surguchov, A. (2010). Conformational diseases: looking into the eyes. Brain Res. Bull. 81, 12-24.
    • (2010) Brain Res. Bull , vol.81 , pp. 12-24
    • Surguchev, A.1    Surguchov, A.2
  • 61
    • 84880307149 scopus 로고    scopus 로고
    • Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells
    • Taipale, M., Krykbaeva, I., Whitesell, L., Santagata, S., Zhang, J., Liu, Q., Gray, N. S. and Lindquist, S. (2013). Chaperones as thermodynamic sensors of drug-target interactions reveal kinase inhibitor specificities in living cells. Nat. Biotechnol. 31, 630-637.
    • (2013) Nat. Biotechnol , vol.31 , pp. 630-637
    • Taipale, M.1    Krykbaeva, I.2    Whitesell, L.3    Santagata, S.4    Zhang, J.5    Liu, Q.6    Gray, N.S.7    Lindquist, S.8
  • 63
    • 66749115386 scopus 로고    scopus 로고
    • Amyloid deposits: Protection against toxic protein species?
    • Treusch, S., Cyr, D. M. and Lindquist, S. (2009). Amyloid deposits: protection against toxic protein species? Cell Cycle 8, 1668-1674.
    • (2009) Cell Cycle , vol.8 , pp. 1668-1674
    • Treusch, S.1    Cyr, D.M.2    Lindquist, S.3
  • 64
    • 84861881296 scopus 로고    scopus 로고
    • The ubiquitin system, an immense realm
    • Varshavsky, A. (2012). The ubiquitin system, an immense realm. Annu. Rev. Biochem. 81, 167-176.
    • (2012) Annu. Rev. Biochem , vol.81 , pp. 167-176
    • Varshavsky, A.1
  • 67
    • 1542283819 scopus 로고    scopus 로고
    • Epidermolysis bullosa simplex-type mutations alter the dynamics of the keratin cytoskeleton and reveal a contribution of actin to the transport of keratin subunits
    • Werner, N. S., Windoffer, R., Strnad, P., Grund, C., Leube, R. E. and Magin, T. M. (2004). Epidermolysis bullosa simplex-type mutations alter the dynamics of the keratin cytoskeleton and reveal a contribution of actin to the transport of keratin subunits. Mol. Biol. Cell 15, 990-1002.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 990-1002
    • Werner, N.S.1    Windoffer, R.2    Strnad, P.3    Grund, C.4    Leube, R.E.5    Magin, T.M.6
  • 68
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E. and Neckers, L. M. (1994). Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 91, 8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 69
    • 84867796642 scopus 로고    scopus 로고
    • Inhibiting HSP90 to treat cancer: A strategy in evolution
    • Whitesell, L., Santagata, S. and Lin, N. U. (2012). Inhibiting HSP90 to treat cancer: a strategy in evolution. Curr. Mol. Med. 12, 1108-1124.
    • (2012) Curr. Mol. Med , vol.12 , pp. 1108-1124
    • Whitesell, L.1    Santagata, S.2    Lin, N.U.3
  • 70
    • 80053564708 scopus 로고    scopus 로고
    • Amyloid in neurodegenerative diseases: Friend or foe?
    • Wolfe, K. J. and Cyr, D. M. (2011). Amyloid in neurodegenerative diseases: friend or foe? Semin. Cell Dev. Biol. 22, 476-481.
    • (2011) Semin. Cell Dev. Biol , vol.22 , pp. 476-481
    • Wolfe, K.J.1    Cyr, D.M.2
  • 71
    • 0027291238 scopus 로고
    • Heat-shock protein hsp90 governs the activity of pp60v-src kinase
    • Xu, Y. and Lindquist, S. (1993). Heat-shock protein hsp90 governs the activity of pp60v-src kinase. Proc. Natl. Acad. Sci. USA 90, 7074-7078.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 72
    • 0033524442 scopus 로고    scopus 로고
    • Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90
    • Xu, Y., Singer, M. A. and Lindquist, S. (1999). Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proc. Natl. Acad. Sci. USA 96, 109-114.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 109-114
    • Xu, Y.1    Singer, M.A.2    Lindquist, S.3


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