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Volumn 12, Issue 22, 2012, Pages 2460-2469

Protein misfolding in disease and small molecule therapies

Author keywords

Alzheimer's disease; Amyloid; Amyotrophic lateral sclerosis; Folding correctors; Lysosomal diseases; Metabolic diseases; Neurodegenerative diseases; Pharmacological chaperone; Pro teostasis; Protein aggregation; Protein folding; Protein stability

Indexed keywords

1 DEOXYNOJIRIMYCIN; AMYLOID BETA PROTEIN; CHAPERONE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; DOXYCYCLINE; IVACAFTOR; LUMACAFTOR; MIGLUSTAT; PREALBUMIN; TAFAMIDIS; TAUROURSODEOXYCHOLIC ACID; TETRAHYDROBIOPTERIN; THYROXINE;

EID: 84874905513     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026611212220002     Document Type: Review
Times cited : (49)

References (65)
  • 2
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman, I.; Bulleid, N. J., Protein folding and modification in the mammalian endoplasmic reticulum. Annual review of biochemistry 2011, 80, 71-99.
    • (2011) Annual Review of Biochemistry , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 3
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B.; Weissman, J.; Horwich, A., Molecular chaperones and protein quality control. Cell 2006, 125 (3), 443-451.
    • (2006) Cell , vol.125 , Issue.3 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 4
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U.; Hayer-Hartl, M., Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002, 295 (5561), 1852-1858.
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 5
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl, F. U.; Hayer-Hartl, M., Converging concepts of protein folding in vitro and in vivo. Nature structural & molecular biology 2009, 16 (6), 574-581.
    • (2009) Nature Structural & Molecular Biology , vol.16 , Issue.6 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 6
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U.; Bracher, A.; Hayer-Hartl, M., Molecular chaperones in protein folding and proteostasis. Nature 2011, 475 (7356), 324-332.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 7
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M., Protein folding and misfolding. Nature 2003, 426 (6968), 884-890.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 9
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S. E.; Fersht, A. R., Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 1991, 30 (43), 10428-10435.
    • (1991) Biochemistry , vol.30 , Issue.43 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 10
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson, S. E., How do small single-domain proteins fold? Folding & design 1998, 3 (4), R81-91.
    • (1998) Folding & Design , vol.3 , Issue.4
    • Jackson, S.E.1
  • 13
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A.; Chan, H. S., From Levinthal to pathways to funnels. Nature structural biology 1997, 4 (1), 10-19.
    • (1997) Nature Structural Biology , vol.4 , Issue.1 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 18
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F.; Dobson, C. M., Protein misfolding, functional amyloid, and human disease. Annual review of biochemistry 2006, 75, 333-366.
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 20
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F.; Dobson, C. M., Amyloid formation by globular proteins under native conditions. Nature chemical biology 2009, 5 (1), 15-22.
    • (2009) Nature Chemical Biology , vol.5 , Issue.1 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 24
    • 50149112642 scopus 로고    scopus 로고
    • Protein misfolding in conformational disorders: Rescue of folding defects and chemical chaperoning
    • Leandro, P.; Gomes, C. M., Protein misfolding in conformational disorders: rescue of folding defects and chemical chaperoning. Mini Rev Med Chem 2008, 8 (9), 901-911.
    • (2008) Mini Rev Med Chem , vol.8 , Issue.9 , pp. 901-911
    • Leandro, P.1    Gomes, C.M.2
  • 25
    • 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
  • 27
    • 84874832163 scopus 로고    scopus 로고
    • Protein homeostasis as a therapeutic target for diseases of protein conformation
    • this issue
    • Calamini, B.; Morimoto, R. I., Protein homeostasis as a therapeutic target for diseases of protein conformation. Current Topics Medicinal Chemistry 2012, (this issue).
    • (2012) Current Topics Medicinal Chemistry
    • Calamini, B.1    Morimoto, R.I.2
  • 29
    • 84861421529 scopus 로고    scopus 로고
    • The transthyretin amyloidoses: From delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug
    • Johnson, S. M.; Connelly, S.; Fearns, C.; Powers, E. T.; Kelly, J. W., The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug. Journal of molecular biology 2012, 421 (2-3), 185-203.
    • (2012) Journal of Molecular Biology , vol.421 , Issue.2-3 , pp. 185-203
    • Johnson, S.M.1    Connelly, S.2    Fearns, C.3    Powers, E.T.4    Kelly, J.W.5
  • 30
    • 84864931018 scopus 로고    scopus 로고
    • Clearance of extracellular misfolded proteins in systemic amyloidosis: Experience with transthyretin
    • Almeida, M. R.; Saraiva, M. J., Clearance of extracellular misfolded proteins in systemic amyloidosis: experience with transthyretin. FEBS letters 2012, 586 (18), 2891-2896.
    • (2012) FEBS Letters , vol.586 , Issue.18 , pp. 2891-2896
    • Almeida, M.R.1    Saraiva, M.J.2
  • 33
    • 79960910835 scopus 로고    scopus 로고
    • Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation
    • Ferreira, N.; Saraiva, M. J.; Almeida, M. R., Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation. FEBS letters 2011, 585 (15), 2424-2430.
    • (2011) FEBS Letters , vol.585 , Issue.15 , pp. 2424-2430
    • Ferreira, N.1    Saraiva, M.J.2    Almeida, M.R.3
  • 35
    • 84855650426 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidosis: In vivo evidence from FAP mice models
    • Ferreira, N.; Saraiva, M. J.; Almeida, M. R., Epigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidosis: in vivo evidence from FAP mice models. PloS one 2012, 7 (1), e29933.
    • (2012) PloS One , vol.7 , Issue.1
    • Ferreira, N.1    Saraiva, M.J.2    Almeida, M.R.3
  • 38
    • 84866295520 scopus 로고    scopus 로고
    • Cystic fibrosis: Insight into CFTR pathophysiology and pharmacotherapy
    • Lubamba, B.; Dhooghe, B.; Noel, S.; Leal, T., Cystic fibrosis: Insight into CFTR pathophysiology and pharmacotherapy. Clinical biochemistry 2012, 45 (15), 1132-1144.
    • (2012) Clinical Biochemistry , vol.45 , Issue.15 , pp. 1132-1144
    • Lubamba, B.1    Dhooghe, B.2    Noel, S.3    Leal, T.4
  • 39
    • 84863509037 scopus 로고    scopus 로고
    • Emergent properties of proteostasis in managing cystic fibrosis
    • Balch, W. E.; Roth, D. M.; Hutt, D. M., Emergent properties of proteostasis in managing cystic fibrosis. Cold Spring Harb Perspect Biol 2011, 3 (2).
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , Issue.2
    • Balch, W.E.1    Roth, D.M.2    Hutt, D.M.3
  • 43
    • 84874922100 scopus 로고    scopus 로고
    • CFTR potentiator vx-770 (ivacaftor) opens the defective channel gate of mutant cftr in a phosphorylation-dependent but atp-independent manner
    • Eckford, P. D.; Li, C.; Ramjeesingh, M.; Bear, C. E., CFTR potentiator vx-770 (ivacaftor) opens the defective channel gate of mutant cftr in a phosphorylation-dependent but atp-independent manner. The Journal of biological chemistry 2012.
    • (2012) The Journal of Biological Chemistry
    • Eckford, P.D.1    Li, C.2    Ramjeesingh, M.3    Bear, C.E.4
  • 46
    • 77449098166 scopus 로고    scopus 로고
    • Treating lysosomal storage diseases with pharma cological chaperones: From concept to clinics
    • Parenti, G., Treating lysosomal storage diseases with pharma cological chaperones: from concept to clinics. EMBO molecular medicine 2009, 1 (5), 268-279.
    • (2009) EMBO Molecular Medicine , vol.1 , Issue.5 , pp. 268-279
    • Parenti, G.1
  • 47
    • 0033018496 scopus 로고    scopus 로고
    • Accelerated transport and maturation of lysosomal alpha-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor
    • Fan, J. Q.; Ishii, S.; Asano, N.; Suzuki, Y., Accelerated transport and maturation of lysosomal alpha-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nature medicine 1999, 5 (1), 112-115.
    • (1999) Nature Medicine , vol.5 , Issue.1 , pp. 112-115
    • Fan, J.Q.1    Ishii, S.2    Asano, N.3    Suzuki, Y.4
  • 52
    • 84864006285 scopus 로고    scopus 로고
    • The pharmacological chaperone AT2220 increases recom binant human acid alpha-glucosidase uptake and glycogen reduction in a mouse model of Pompe disease
    • Khanna, R.; Flanagan, J. J.; Feng, J.; Soska, R.; Frascella, M.; Pellegrino, L. J.; Lun, Y.; Guillen, D.; Lockhart, D. J.; Valenzano, K. J., The pharmacological chaperone AT2220 increases recom binant human acid alpha-glucosidase uptake and glycogen reduction in a mouse model of Pompe disease. PloS one 2012, 7 (7), e40776.
    • (2012) PloS One , vol.7 , Issue.7
    • Khanna, R.1    Flanagan, J.J.2    Feng, J.3    Soska, R.4    Frascella, M.5    Pellegrino, L.J.6    Lun, Y.7    Guillen, D.8    Lockhart, D.J.9    Valenzano, K.J.10
  • 54
    • 8844256618 scopus 로고    scopus 로고
    • Tetrahydrobiopterin protects phenylalanine hydroxylase activity in vivo: Implications for tetrahydrobiopterin-responsive hyperphenylalaninemia
    • Thony, B.; Ding, Z.; Martinez, A., Tetrahydrobiopterin protects phenylalanine hydroxylase activity in vivo: implications for tetrahydrobiopterin-responsive hyperphenylalaninemia. FEBS letters 2004, 577 (3), 507-511.
    • (2004) FEBS Letters , vol.577 , Issue.3 , pp. 507-511
    • Thony, B.1    Ding, Z.2    Martinez, A.3
  • 55
    • 79958701858 scopus 로고    scopus 로고
    • The interplay between genotype, metabolic state and cofactor treatment governs phenylalanine hydroxylase function and drug response
    • Staudigl, M.; Gersting, S. W.; Danecka, M. K.; Messing, D. D.; Woidy, M.; Pinkas, D.; Kemter, K. F.; Blau, N.; Muntau, A. C., The interplay between genotype, metabolic state and cofactor treatment governs phenylalanine hydroxylase function and drug response. Human molecular genetics 2011, 20 (13), 2628-2641.
    • (2011) Human Molecular Genetics , vol.20 , Issue.13 , pp. 2628-2641
    • Staudigl, M.1    Gersting, S.W.2    Danecka, M.K.3    Messing, D.D.4    Woidy, M.5    Pinkas, D.6    Kemter, K.F.7    Blau, N.8    Muntau, A.C.9
  • 60
    • 78650709553 scopus 로고    scopus 로고
    • Emerging roles for riboflavin in functional rescue of mitochondrial beta-oxidation flavoenzymes
    • Henriques, B. J.; Olsen, R. K.; Bross, P.; Gomes, C. M., Emerging roles for riboflavin in functional rescue of mitochondrial beta-oxidation flavoenzymes. Current medicinal chemistry 2010, 17 (32), 3842-3854.
    • (2010) Current Medicinal Chemistry , vol.17 , Issue.32 , pp. 3842-3854
    • Henriques, B.J.1    Olsen, R.K.2    Bross, P.3    Gomes, C.M.4
  • 62
    • 84864527932 scopus 로고    scopus 로고
    • Molecular mechanisms of riboflavin responsiveness in patients with ETF-QO variations and multiple acyl-CoA dehydrogenation deficiency
    • Cornelius, N.; Frerman, F. E.; Corydon, T. J.; Palmfeldt, J.; Bross, P.; Gregersen, N.; Olsen, R. K., Molecular mechanisms of riboflavin responsiveness in patients with ETF-QO variations and multiple acyl-CoA dehydrogenation deficiency. Human molecular genetics 2012, 21 (15), 3435-3448.
    • (2012) Human Molecular Genetics , vol.21 , Issue.15 , pp. 3435-3448
    • Cornelius, N.1    Frerman, F.E.2    Corydon, T.J.3    Palmfeldt, J.4    Bross, P.5    Gregersen, N.6    Olsen, R.K.7
  • 64
    • 63249105550 scopus 로고    scopus 로고
    • Role of flavinylation in a mild variant of multiple acyl-CoA dehydrogenation deficiency: A molecular rationale for the effects of riboflavin supplementation
    • Henriques, B. J.; Rodrigues, J. V.; Olsen, R. K.; Bross, P.; Gomes, C. M., Role of flavinylation in a mild variant of multiple acyl-CoA dehydrogenation deficiency: a molecular rationale for the effects of riboflavin supplementation. The Journal of biological chemistry 2009, 284 (7), 4222-42229.
    • (2009) The Journal of Biological Chemistry , vol.284 , Issue.7 , pp. 4222-42229
    • Henriques, B.J.1    Rodrigues, J.V.2    Olsen, R.K.3    Bross, P.4    Gomes, C.M.5
  • 65
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.