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Volumn 83, Issue , 2014, Pages 3-9

Using pharmacological chaperones to restore proteostasis

Author keywords

Chaperone; ERAD; GPCR; Ion channel; Lysosomal storage disease; Pharmacological chaperone; Protein misfolding disease; Proteostasis

Indexed keywords

CHAPERONE;

EID: 84901840776     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2014.04.002     Document Type: Review
Times cited : (42)

References (97)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • W.E. Balch, R.I. Morimoto, A. Dillin, and J.W. Kelly Adapting proteostasis for disease intervention Science 319 2008 916 919 (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 3
    • 84860118506 scopus 로고    scopus 로고
    • The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology
    • C.J. Guerriero, and J.L. Brodsky The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Physiol Rev 92 2012 537 576
    • (2012) Physiol Rev , vol.92 , pp. 537-576
    • Guerriero, C.J.1    Brodsky, J.L.2
  • 4
    • 84875461582 scopus 로고    scopus 로고
    • Diversity in the origins of proteostasis networks - A driver for protein function in evolution
    • E.T. Powers, and W.E. Balch Diversity in the origins of proteostasis networks - a driver for protein function in evolution Nat Rev Mol Cell Biol 14 2013 237 248
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 237-248
    • Powers, E.T.1    Balch, W.E.2
  • 5
    • 84863533791 scopus 로고    scopus 로고
    • The stress of protein misfolding: From single cells to multicellular organisms
    • T. Gidalevitz, V. Prahlad, and R.I. Morimoto The stress of protein misfolding: from single cells to multicellular organisms Cold Spring Harb Perspect Biol 3 2011 a009704
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. 009704
    • Gidalevitz, T.1    Prahlad, V.2    Morimoto, R.I.3
  • 6
    • 84894254592 scopus 로고    scopus 로고
    • Proteostasis and longevity: When does aging really begin?
    • J. Labbadia, and R.I. Morimoto Proteostasis and longevity: when does aging really begin? F1000prime Rep 6 2014 7
    • (2014) F1000prime Rep , vol.6 , pp. 7
    • Labbadia, J.1    Morimoto, R.I.2
  • 8
    • 84863509037 scopus 로고    scopus 로고
    • Emergent properties of proteostasis in managing cystic fibrosis
    • W.E. Balch, D.M. Roth, and D.M. Hutt Emergent properties of proteostasis in managing cystic fibrosis Cold Spring Harb Perspect Biol 3 2011 a004499
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. 004499
    • Balch, W.E.1    Roth, D.M.2    Hutt, D.M.3
  • 9
    • 84856629737 scopus 로고    scopus 로고
    • CFTR: Folding, misfolding and correcting the DeltaF508 conformational defect
    • G.L. Lukacs, and A.S. Verkman CFTR: folding, misfolding and correcting the DeltaF508 conformational defect Trends Mol Med 18 2012 81 91
    • (2012) Trends Mol Med , vol.18 , pp. 81-91
    • Lukacs, G.L.1    Verkman, A.S.2
  • 10
    • 2942633579 scopus 로고    scopus 로고
    • Biology of cardiac arrhythmias: Ion channel protein trafficking
    • DOI 10.1161/01.RES.0000128561.28701.ea
    • B.P. Delisle, B.D. Anson, S. Rajamani, and C.T. January Biology of cardiac arrhythmias - ion channel protein trafficking Circ Res 94 2004 1418 1428 (Pubitemid 38780314)
    • (2004) Circulation Research , vol.94 , Issue.11 , pp. 1418-1428
    • Delisle, B.P.1    Anson, B.D.2    Rajamani, S.3    January, C.T.4
  • 11
    • 84870921351 scopus 로고    scopus 로고
    • Ion channel mutations in neuronal diseases: A genetics perspective
    • O.K. Steinlein Ion channel mutations in neuronal diseases: a genetics perspective Chem Rev 112 2012 6334 6352
    • (2012) Chem Rev , vol.112 , pp. 6334-6352
    • Steinlein, O.K.1
  • 12
    • 16644366865 scopus 로고    scopus 로고
    • Pharmacological chaperone action on G-protein-coupled receptors
    • DOI 10.1016/j.coph.2004.08.001, PII S1471489204001316
    • V. Bernier, D.G. Bichet, and M. Bouvier Pharmacological chaperone action on G-protein-coupled receptors Curr Opin Pharmacol 4 2004 528 533 (Pubitemid 40533016)
    • (2004) Current Opinion in Pharmacology , vol.4 , Issue.5 , pp. 528-533
    • Bernier, V.1    Bichet, D.G.2    Bouvier, M.3
  • 13
    • 34748871331 scopus 로고    scopus 로고
    • G protein-coupled receptor trafficking in health and disease: Lessons learned to prepare for therapeutic mutant rescue in vivo
    • DOI 10.1124/pr.59.3.2
    • P.M. Conn, A. Ulloa-Aguirre, J. Ito, and J.A. Janovick G protein-coupled receptor trafficking in health and disease: lessons learned to prepare for therapeutic mutant rescue in vivo Pharmacol Rev 59 2007 225 250 (Pubitemid 47481435)
    • (2007) Pharmacological Reviews , vol.59 , Issue.3 , pp. 225-250
    • Conn, P.M.1    Ulloa-Aguirre, A.2    Ito, J.3    Janovick, J.A.4
  • 15
    • 84896695581 scopus 로고    scopus 로고
    • Chemical kinetics for drug discovery to combat protein aggregation diseases
    • P. Arosio, M. Vendruscolo, C.M. Dobson, and T.P. Knowles Chemical kinetics for drug discovery to combat protein aggregation diseases Trends Pharmacol Sci 35 2014 127 135
    • (2014) Trends Pharmacol Sci , vol.35 , pp. 127-135
    • Arosio, P.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.4
  • 17
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: Progress and prognosis
    • S.L. Lindquist, and J.W. Kelly Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis Cold Spring Harb Perspect Biol 3 2011 a004507
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , pp. 004507
    • Lindquist, S.L.1    Kelly, J.W.2
  • 18
    • 50249175120 scopus 로고    scopus 로고
    • Chemical and biological approaches synergize to ameliorate protein-folding diseases
    • T.W. Mu, D.S.T. Ong, Y.J. Wang, W.E. Balch, J.R. Yates, and L. Segatori et al. Chemical and biological approaches synergize to ameliorate protein-folding diseases Cell 134 2008 769 781
    • (2008) Cell , vol.134 , pp. 769-781
    • Mu, T.W.1    Ong, D.S.T.2    Wang, Y.J.3    Balch, W.E.4    Yates, J.R.5    Segatori, L.6
  • 19
    • 84890858016 scopus 로고    scopus 로고
    • SAHA enhances proteostasis of epilepsy-associated alpha1(A322D) beta2gamma2 GABAA receptors
    • X.-J. Di, D.-Y. Han, Y.-J. Wang, M.R. Chance, and T.-W. Mu SAHA enhances proteostasis of epilepsy-associated alpha1(A322D)beta2gamma2 GABAA receptors Chem Biol 20 2013 1456 1468
    • (2013) Chem Biol , vol.20 , pp. 1456-1468
    • Di, X.-J.1    Han, D.-Y.2    Wang, Y.-J.3    Chance, M.R.4    Mu, T.-W.5
  • 21
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • M. Schroder, and R.J. Kaufman The mammalian unfolded protein response Annu Rev Biochem 74 2005 739 789 (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 22
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • P. Walter, and D. Ron The unfolded protein response: from stress pathway to homeostatic regulation Science 334 2011 1081 1086
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 23
    • 40149095757 scopus 로고    scopus 로고
    • Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis
    • T.W. Mu, D.M. Fowler, and J.W. Kelly Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis PLoS Biol 6 2008 e26
    • (2008) PLoS Biol , vol.6 , pp. 26
    • Mu, T.W.1    Fowler, D.M.2    Kelly, J.W.3
  • 25
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • J.L. Brodsky Cleaning up: ER-associated degradation to the rescue Cell 151 2012 1163 1167
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 26
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • DOI 10.1126/science.290.5497.1717
    • D.J. Klionsky, and S.D. Emr Cell biology - autophagy as a regulated pathway of cellular degradation Science 290 2000 1717 1721 (Pubitemid 32004796)
    • (2000) Science , vol.290 , Issue.5497 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 27
    • 84875434910 scopus 로고    scopus 로고
    • FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts
    • D.S. Ong, Y.J. Wang, Y.L. Tan, J.R. Yates 3rd, T.W. Mu, and J.W. Kelly FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts Chem Biol 20 2013 403 415
    • (2013) Chem Biol , vol.20 , pp. 403-415
    • Ong, D.S.1    Wang, Y.J.2    Tan, Y.L.3    Yates III, J.R.4    Mu, T.W.5    Kelly, J.W.6
  • 29
    • 84890033475 scopus 로고    scopus 로고
    • Identification of GABAC receptor protein homeostasis network components from three tandem mass spectrometry proteomics approaches
    • Y.J. Wang, D.Y. Han, T. Tabib, J.R. Yates, and T.W. Mu Identification of GABAC receptor protein homeostasis network components from three tandem mass spectrometry proteomics approaches J Proteome Res 27 2013 5570 5586
    • (2013) J Proteome Res , vol.27 , pp. 5570-5586
    • Wang, Y.J.1    Han, D.Y.2    Tabib, T.3    Yates, J.R.4    Mu, T.W.5
  • 31
    • 84866623060 scopus 로고    scopus 로고
    • Flagging and docking: Dual roles for N-glycans in protein quality control and cellular proteostasis
    • D.N. Hebert, and M. Molinari Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis Trends Biochem Sci 37 2012 404 410
    • (2012) Trends Biochem Sci , vol.37 , pp. 404-410
    • Hebert, D.N.1    Molinari, M.2
  • 32
    • 79961171901 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: The central enzyme of N-linked protein glycosylation
    • E. Mohorko, R. Glockshuber, and M. Aebi Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation J Inherit Metab Dis 34 2011 869 878
    • (2011) J Inherit Metab Dis , vol.34 , pp. 869-878
    • Mohorko, E.1    Glockshuber, R.2    Aebi, M.3
  • 33
    • 84880586512 scopus 로고    scopus 로고
    • N-linked protein glycosylation in the ER
    • M. Aebi N-linked protein glycosylation in the ER Trends Cell Biol 1833 2013 2430 2437
    • (2013) Trends Cell Biol , vol.1833 , pp. 2430-2437
    • Aebi, M.1
  • 34
    • 84897130414 scopus 로고    scopus 로고
    • Glycoprotein folding and quality-control mechanisms in protein-folding diseases
    • S.P. Ferris, V.K. Kodali, and R.J. Kaufman Glycoprotein folding and quality-control mechanisms in protein-folding diseases Dis Model Mech 7 2014 331 341
    • (2014) Dis Model Mech , vol.7 , pp. 331-341
    • Ferris, S.P.1    Kodali, V.K.2    Kaufman, R.J.3
  • 35
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • G.Z. Lederkremer Glycoprotein folding, quality control and ER-associated degradation Curr Opin Struct Biol 19 2009 515 523
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 37
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • DOI 10.1016/S0092-8674(00)80928-9
    • B. Bukau, and A.L. Horwich The Hsp70 and Hsp60 chaperone machines Cell 92 1998 351 366 (Pubitemid 28093013)
    • (1998) Cell , vol.92 , Issue.3 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 38
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • DOI 10.1038/381571a0
    • F.U. Hartl Molecular chaperones in cellular protein folding Nature 381 1996 571 580 (Pubitemid 26177472)
    • (1996) Nature , vol.381 , Issue.6583 , pp. 571-580
    • Hartl, F.U.1
  • 40
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • B. Bukau, J. Weissman, and A. Horwich Molecular chaperones and protein quality control Cell 125 2006 443 451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 41
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • F.U. Hartl, A. Bracher, and M. Hayer-Hartl Molecular chaperones in protein folding and proteostasis Nature 475 2011 324 332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 42
    • 78650141466 scopus 로고    scopus 로고
    • Emergent properties of proteostasis-COPII coupled systems in human health and disease
    • K.E. Routledge, V. Gupta, and W.E. Balch Emergent properties of proteostasis-COPII coupled systems in human health and disease Mol Membr Biol 27 2010 385 397
    • (2010) Mol Membr Biol , vol.27 , pp. 385-397
    • Routledge, K.E.1    Gupta, V.2    Balch, W.E.3
  • 44
    • 80054729346 scopus 로고    scopus 로고
    • COPII and COPI traffic at the ER-Golgi interface
    • T. Szul, and E. Sztul COPII and COPI traffic at the ER-Golgi interface Physiology 26 2011 348 364
    • (2011) Physiology , vol.26 , pp. 348-364
    • Szul, T.1    Sztul, E.2
  • 45
  • 46
    • 84894284572 scopus 로고    scopus 로고
    • Pharmacological chaperones correct misfolded GPCRs and rescue function: Protein trafficking as a therapeutic target
    • G. Maya-Nunez, A. Ulloa-Aguirre, J.A. Janovick, and P.M. Conn Pharmacological chaperones correct misfolded GPCRs and rescue function: protein trafficking as a therapeutic target Subcell Biochem 63 2012 263 289
    • (2012) Subcell Biochem , vol.63 , pp. 263-289
    • Maya-Nunez, G.1    Ulloa-Aguirre, A.2    Janovick, J.A.3    Conn, P.M.4
  • 47
    • 84861420190 scopus 로고    scopus 로고
    • Pharmacological chaperoning of nicotinic acetylcholine receptors reduces the endoplasmic reticulum stress response
    • R. Srinivasan, C.I. Richards, C. Xiao, D. Rhee, R. Pantoja, and D.A. Dougherty et al. Pharmacological chaperoning of nicotinic acetylcholine receptors reduces the endoplasmic reticulum stress response Mol Pharmacol 81 2012 759 769
    • (2012) Mol Pharmacol , vol.81 , pp. 759-769
    • Srinivasan, R.1    Richards, C.I.2    Xiao, C.3    Rhee, D.4    Pantoja, R.5    Dougherty, D.A.6
  • 48
    • 33646578825 scopus 로고    scopus 로고
    • Rescue of folding defects in ABC transporters using pharmacological chaperones
    • DOI 10.1007/s10863-005-9499-3
    • T.W. Loo, M.C. Bartlett, and D.M. Clarke Rescue of folding defects in ABC transporters using pharmacological chaperones J Bioenerg Biomembr 37 2005 501 507 (Pubitemid 43725183)
    • (2005) Journal of Bioenergetics and Biomembranes , vol.37 , Issue.6 , pp. 501-507
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 49
    • 84861421529 scopus 로고    scopus 로고
    • The transthyretin amyloidoses: From delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug
    • S.M. Johnson, S. Connelly, C. Fearns, E.T. Powers, and J.W. Kelly The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug J Mol Biol 421 2012 185 203
    • (2012) J Mol Biol , vol.421 , pp. 185-203
    • Johnson, S.M.1    Connelly, S.2    Fearns, C.3    Powers, E.T.4    Kelly, J.W.5
  • 50
    • 84893369317 scopus 로고    scopus 로고
    • Neuronopathic lysosomal storage diseases: Clinical and pathologic findings
    • C.E. Prada, and G.A. Grabowski Neuronopathic lysosomal storage diseases: clinical and pathologic findings Dev Disabil Res Rev 17 2013 226 246
    • (2013) Dev Disabil Res Rev , vol.17 , pp. 226-246
    • Prada, C.E.1    Grabowski, G.A.2
  • 51
    • 84892755879 scopus 로고    scopus 로고
    • Lysosomal storage disorders: Old diseases, present and future challenges
    • A.D. Klein, and A.H. Futerman Lysosomal storage disorders: old diseases, present and future challenges Pediatr Endocrinol Rev 11 Suppl. 1 2013 59 63
    • (2013) Pediatr Endocrinol Rev , vol.11 , Issue.SUPPL. 1 , pp. 59-63
    • Klein, A.D.1    Futerman, A.H.2
  • 52
    • 84866278220 scopus 로고    scopus 로고
    • Gaucher disease paradigm: From ERAD to comorbidity
    • I. Bendikov-Bar, and M. Horowitz Gaucher disease paradigm: from ERAD to comorbidity Hum Mutat 33 2012 1398 1407
    • (2012) Hum Mutat , vol.33 , pp. 1398-1407
    • Bendikov-Bar, I.1    Horowitz, M.2
  • 53
    • 84876084462 scopus 로고    scopus 로고
    • A phase 2 study of migalastat hydrochloride in females with Fabry disease: Selection of population, safety and pharmacodynamic effects
    • R. Giugliani, S. Waldek, D.P. Germain, K. Nicholls, D.G. Bichet, and J.K. Simosky et al. A phase 2 study of migalastat hydrochloride in females with Fabry disease: selection of population, safety and pharmacodynamic effects Mol Genet Metab 109 2013 86 92
    • (2013) Mol Genet Metab , vol.109 , pp. 86-92
    • Giugliani, R.1    Waldek, S.2    Germain, D.P.3    Nicholls, K.4    Bichet, D.G.5    Simosky, J.K.6
  • 54
    • 84856411368 scopus 로고    scopus 로고
    • Pharmacological chaperone therapy for Fabry disease
    • S. Ishii Pharmacological chaperone therapy for Fabry disease Proc Jpn Acad Ser B Phys Biol Sci 88 2012 18 30
    • (2012) Proc Jpn Acad ser B Phys Biol Sci , vol.88 , pp. 18-30
    • Ishii, S.1
  • 55
    • 84875312816 scopus 로고    scopus 로고
    • Gaucher disease: A comprehensive review
    • B.E. Rosenbloom, and N.J. Weinreb Gaucher disease: a comprehensive review Crit Rev Oncog 18 2013 163 175
    • (2013) Crit Rev Oncog , vol.18 , pp. 163-175
    • Rosenbloom, B.E.1    Weinreb, N.J.2
  • 56
    • 0033018496 scopus 로고    scopus 로고
    • Accelerated transport and maturation of lysosomal α-galactosidase A in fabry lymphoblasts by an enzyme inhibitor
    • DOI 10.1038/4801
    • J.Q. Fan, S. Ishii, N. Asano, and Y. Suzuki Accelerated transport and maturation of lysosomal alpha-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor Nat Med 5 1999 112 115 (Pubitemid 29051008)
    • (1999) Nature Medicine , vol.5 , Issue.1 , pp. 112-115
    • Fan, J.-Q.1    Ishii, S.2    Asano, N.3    Suzuki, Y.4
  • 57
    • 0043235841 scopus 로고    scopus 로고
    • A contradictory treatment for lysosomal storage disorders: Inhibitors enhance mutant enzyme activity
    • J.Q. Fan A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity Trends Pharmacol Sci 24 2003 355 360
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 355-360
    • Fan, J.Q.1
  • 58
    • 34748914170 scopus 로고    scopus 로고
    • Pharmacologic chaperoning as a strategy to treat Gaucher disease
    • DOI 10.1111/j.1742-4658.2007.06042.x
    • Z. Yu, A.R. Sawkar, and J.W. Kelly Pharmacologic chaperoning as a strategy to treat Gaucher disease FEBS J 274 2007 4944 4950 (Pubitemid 47481193)
    • (2007) FEBS Journal , vol.274 , Issue.19 , pp. 4944-4950
    • Yu, Z.1    Sawkar, A.R.2    Kelly, J.W.3
  • 59
    • 79957628617 scopus 로고    scopus 로고
    • Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders
    • K.J. Valenzano, R. Khanna, A.C. Powe, R. Boyd, G. Lee, and J.J. Flanagan et al. Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders Assay Drug Dev Technol 9 2011 213 235
    • (2011) Assay Drug Dev Technol , vol.9 , pp. 213-235
    • Valenzano, K.J.1    Khanna, R.2    Powe, A.C.3    Boyd, R.4    Lee, G.5    Flanagan, J.J.6
  • 60
    • 77953127358 scopus 로고    scopus 로고
    • 2,5-Dideoxy-2,5-imino-d-altritol as a new class of pharmacological chaperone for Fabry disease
    • A. Kato, Y. Yamashita, S. Nakagawa, Y. Koike, I. Adachi, and J. Hollinshead et al. 2,5-Dideoxy-2,5-imino-d-altritol as a new class of pharmacological chaperone for Fabry disease Bioorg Med Chem 18 2010 3790 3794
    • (2010) Bioorg Med Chem , vol.18 , pp. 3790-3794
    • Kato, A.1    Yamashita, Y.2    Nakagawa, S.3    Koike, Y.4    Adachi, I.5    Hollinshead, J.6
  • 61
    • 84891868024 scopus 로고    scopus 로고
    • A thermodynamic assay to test pharmacological chaperones for Fabry disease
    • G. Andreotti, V. Citro, A. Correra, and M.V. Cubellis A thermodynamic assay to test pharmacological chaperones for Fabry disease Biochim Biophys Acta 1840 2014 1214 1224
    • (2014) Biochim Biophys Acta , vol.1840 , pp. 1214-1224
    • Andreotti, G.1    Citro, V.2    Correra, A.3    Cubellis, M.V.4
  • 62
    • 84555202420 scopus 로고    scopus 로고
    • The molecular basis of pharmacological chaperoning in human alpha-galactosidase
    • A.I. Guce, N.E. Clark, J.J. Rogich, and S.C. Garman The molecular basis of pharmacological chaperoning in human alpha-galactosidase Chem Biol 18 2011 1521 1526
    • (2011) Chem Biol , vol.18 , pp. 1521-1526
    • Guce, A.I.1    Clark, N.E.2    Rogich, J.J.3    Garman, S.C.4
  • 64
    • 33845240108 scopus 로고    scopus 로고
    • Chemical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants
    • A.R. Sawkar, M. Schmitz, K.P. Zimmer, D. Reczek, T. Edmunds, and W.E. Balch et al. Chemical chaperones and permissive temperatures alter localization of Gaucher disease associated glucocerebrosidase variants ACS Chem Biol 1 2006 235 251
    • (2006) ACS Chem Biol , vol.1 , pp. 235-251
    • Sawkar, A.R.1    Schmitz, M.2    Zimmer, K.P.3    Reczek, D.4    Edmunds, T.5    Balch, W.E.6
  • 65
    • 77954749600 scopus 로고    scopus 로고
    • Click chemistry approach to new N-substituted aminocyclitols as potential pharmacological chaperones for Gaucher disease
    • L. Diaz, J. Bujons, J. Casas, A. Llebaria, and A. Delgado Click chemistry approach to new N-substituted aminocyclitols as potential pharmacological chaperones for Gaucher disease J Med Chem 53 2010 5248 5255
    • (2010) J Med Chem , vol.53 , pp. 5248-5255
    • Diaz, L.1    Bujons, J.2    Casas, J.3    Llebaria, A.4    Delgado, A.5
  • 66
    • 84876158235 scopus 로고    scopus 로고
    • Glucocerebrosidase inhibitors for the treatment of Gaucher disease
    • A. Trapero, and A. Llebaria Glucocerebrosidase inhibitors for the treatment of Gaucher disease Future Med Chem 5 2013 573 590
    • (2013) Future Med Chem , vol.5 , pp. 573-590
    • Trapero, A.1    Llebaria, A.2
  • 67
    • 33846265304 scopus 로고    scopus 로고
    • Isofagomine- and 2,5-anhydro-2,5-imino-D-glucitol-based glucocerebrosidase pharmacological chaperones for gaucher disease intervention
    • DOI 10.1021/jm060677i
    • Z. Yu, A.R. Sawkar, L.J. Whalen, C.-H. Wong, and J.W. Kelly Isofagomine- and 2,5-anhydro-2,5-imino-d-glucitol-based glucocerebrosidase pharmacological chaperones for Gaucher disease intervention J Med Chem 50 2007 94 100 (Pubitemid 46105502)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.1 , pp. 94-100
    • Yu, Z.1    Sawkar, A.R.2    Whalen, L.J.3    Wong, C.-H.4    Kelly, J.W.5
  • 69
    • 0033615646 scopus 로고    scopus 로고
    • Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects
    • Z. Zhou, Q. Gong, and C.T. January Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects J Biol Chem 274 1999 31123 31126
    • (1999) J Biol Chem , vol.274 , pp. 31123-31126
    • Zhou, Z.1    Gong, Q.2    January, C.T.3
  • 70
    • 84873397801 scopus 로고    scopus 로고
    • Novel pharmacological strategies to treat cystic fibrosis
    • J.W. Hanrahan, H.M. Sampson, and D.Y. Thomas Novel pharmacological strategies to treat cystic fibrosis Trends Pharmacol Sci 34 2013 119 125
    • (2013) Trends Pharmacol Sci , vol.34 , pp. 119-125
    • Hanrahan, J.W.1    Sampson, H.M.2    Thomas, D.Y.3
  • 71
    • 77955509085 scopus 로고    scopus 로고
    • GABA acts as a ligand chaperone in the early secretory pathway to promote cell surface expression of GABAA receptors
    • R.S. Eshaq, L.D. Stahl, R. Stone 2nd, S.S. Smith, L.C. Robinson, and N.J. Leidenheimer GABA acts as a ligand chaperone in the early secretory pathway to promote cell surface expression of GABAA receptors Brain Res 1346 2010 1 13
    • (2010) Brain Res , vol.1346 , pp. 1-13
    • Eshaq, R.S.1    Stahl, L.D.2    Stone II, R.3    Smith, S.S.4    Robinson, L.C.5    Leidenheimer, N.J.6
  • 72
    • 27844472836 scopus 로고    scopus 로고
    • Nicotine acts as a pharmacological chaperone to up-regulate human α4β2 acetylcholine receptors
    • DOI 10.1124/mol.105.012419
    • A. Kuryatov, J. Luo, J. Cooper, and J. Lindstrom Nicotine acts as a pharmacological chaperone to up-regulate human alpha 4 beta 2 acetylcholine receptors Mol Pharmacol 68 2005 1839 1851 (Pubitemid 41654365)
    • (2005) Molecular Pharmacology , vol.68 , Issue.6 , pp. 1839-1851
    • Kuryatov, A.1    Luo, J.2    Cooper, J.3    Lindstrom, J.4
  • 73
    • 65549132734 scopus 로고    scopus 로고
    • Nicotine is a selective pharmacological chaperone of acetylcholine receptor number and stoichiometry. Implications for drug discovery
    • H.A. Lester, C. Xiao, R. Srinivasan, C.D. Son, J. Miwa, and R. Pantoja et al. Nicotine is a selective pharmacological chaperone of acetylcholine receptor number and stoichiometry. Implications for drug discovery AAPS J 11 2009 167 177
    • (2009) AAPS J , vol.11 , pp. 167-177
    • Lester, H.A.1    Xiao, C.2    Srinivasan, R.3    Son, C.D.4    Miwa, J.5    Pantoja, R.6
  • 75
    • 0037085464 scopus 로고    scopus 로고
    • The binding site for channel blockers that rescue misprocessed human long QT syndrome type 2 ether-A-gogo-related gene (HERG) mutations
    • DOI 10.1074/jbc.M107345200
    • E. Ficker, C.A. Obejero-Paz, S. Zhao, and A.M. Brown The binding site for channel blockers that rescue misprocessed human long QT syndrome type 2 ether-a-gogo-related gene (HERG) mutations J Biol Chem 277 2002 4989 4998 (Pubitemid 34968538)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 4989-4998
    • Ficker, E.1    Obejero-Paz, C.A.2    Zhao, S.3    Brown, A.M.4
  • 76
    • 33745282127 scopus 로고    scopus 로고
    • Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones
    • Y. Wang, M.C. Bartlett, T.W. Loo, and D.M. Clarke Specific rescue of cystic fibrosis transmembrane conductance regulator processing mutants using pharmacological chaperones Mol Pharmacol 70 2006 297 302
    • (2006) Mol Pharmacol , vol.70 , pp. 297-302
    • Wang, Y.1    Bartlett, M.C.2    Loo, T.W.3    Clarke, D.M.4
  • 77
    • 36348989763 scopus 로고    scopus 로고
    • Correctors promote maturation of Cystic Fibrosis Transmembrane conductance Regulator (CFTR)-processing mutants by binding to the protein
    • DOI 10.1074/jbc.C700175200
    • Y. Wang, T.W. Loo, M.C. Bartlett, and D.M. Clarke Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein J Biol Chem 282 2007 33247 33251 (Pubitemid 350159496)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33247-33251
    • Wang, Y.1    Loo, T.W.2    Bartlett, M.C.3    Clarke, D.M.4
  • 78
    • 79951829938 scopus 로고    scopus 로고
    • Identification of a NBD1-binding pharmacological chaperone that corrects the trafficking defect of F508del-CFTR
    • H.M. Sampson, R. Robert, J. Liao, E. Matthes, G.W. Carlile, and J.W. Hanrahan et al. Identification of a NBD1-binding pharmacological chaperone that corrects the trafficking defect of F508del-CFTR Chem Biol 18 2011 231 242
    • (2011) Chem Biol , vol.18 , pp. 231-242
    • Sampson, H.M.1    Robert, R.2    Liao, J.3    Matthes, E.4    Carlile, G.W.5    Hanrahan, J.W.6
  • 79
    • 0035827680 scopus 로고    scopus 로고
    • Novel CFTR chloride channel activators identified by screening of combinatorial libraries based on flavone and benzoquinolizinium lead compounds
    • L.J. Galietta, M.F. Springsteel, M. Eda, E.J. Niedzinski, K. By, and M.J. Haddadin et al. Novel CFTR chloride channel activators identified by screening of combinatorial libraries based on flavone and benzoquinolizinium lead compounds J Biol Chem 276 2001 19723 19728
    • (2001) J Biol Chem , vol.276 , pp. 19723-19728
    • Galietta, L.J.1    Springsteel, M.F.2    Eda, M.3    Niedzinski, E.J.4    By, K.5    Haddadin, M.J.6
  • 80
    • 84881437750 scopus 로고    scopus 로고
    • Gating of pentameric ligand-gated ion channels: Structural insights and ambiguities
    • C.J. Dacosta, and J.E. Baenziger Gating of pentameric ligand-gated ion channels: structural insights and ambiguities Structure 21 2013 1271 1283
    • (2013) Structure , vol.21 , pp. 1271-1283
    • Dacosta, C.J.1    Baenziger, J.E.2
  • 82
    • 0038277048 scopus 로고    scopus 로고
    • Different binding orientations for the same agonist at homologous receptors: A lock and key or a simple wedge?
    • DOI 10.1021/ja0348086
    • T.W. Mu, H.A. Lester, and D.A. Dougherty Different binding orientations for the same agonist at homologous receptors: a lock and key or a simple wedge? J Am Chem Soc 125 2003 6850 6851 (Pubitemid 36682767)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.23 , pp. 6850-6851
    • Mu, T.-W.1    Lester, H.A.2    Dougherty, D.A.3
  • 84
    • 78650873492 scopus 로고    scopus 로고
    • Nicotine up-regulates alpha4beta2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning
    • R. Srinivasan, R. Pantoja, F.J. Moss, E.D. Mackey, C.D. Son, and J. Miwa et al. Nicotine up-regulates alpha4beta2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning J Gen Physiol 137 2011 59 79
    • (2011) J Gen Physiol , vol.137 , pp. 59-79
    • Srinivasan, R.1    Pantoja, R.2    Moss, F.J.3    Mackey, E.D.4    Son, C.D.5    Miwa, J.6
  • 85
    • 68749105852 scopus 로고    scopus 로고
    • Enhancement of the surface expression of G protein-coupled receptors
    • J.H. Dunham, and R.A. Hall Enhancement of the surface expression of G protein-coupled receptors Trends Biotechnol 27 2009 541 545
    • (2009) Trends Biotechnol , vol.27 , pp. 541-545
    • Dunham, J.H.1    Hall, R.A.2
  • 87
    • 33645416161 scopus 로고    scopus 로고
    • Pharmacologic chaperones as a potential treatment for X-linked nephrogenic diabetes insipidus
    • V. Bernier, J.P. Morello, A. Zarruk, N. Debrand, A. Salahpour, and M. Lonergan et al. Pharmacologic chaperones as a potential treatment for X-linked nephrogenic diabetes insipidus J Am Soc Nephrol 17 2006 232 243
    • (2006) J Am Soc Nephrol , vol.17 , pp. 232-243
    • Bernier, V.1    Morello, J.P.2    Zarruk, A.3    Debrand, N.4    Salahpour, A.5    Lonergan, M.6
  • 88
    • 77956119735 scopus 로고    scopus 로고
    • Potential of nonpeptide (ant)agonists to rescue vasopressin V2 receptor mutants for the treatment of X-linked nephrogenic diabetes insipidus
    • E.L. Los, P.M. Deen, and J.H. Robben Potential of nonpeptide (ant)agonists to rescue vasopressin V2 receptor mutants for the treatment of X-linked nephrogenic diabetes insipidus J Neuroendocrinol 22 2010 393 399
    • (2010) J Neuroendocrinol , vol.22 , pp. 393-399
    • Los, E.L.1    Deen, P.M.2    Robben, J.H.3
  • 89
    • 33846237329 scopus 로고    scopus 로고
    • Functional rescue of vasopressin V2 receptor mutants in MDCK cells by pharmacochaperones: Relevance to therapy of nephrogenic diabetes insipidus
    • J.H. Robben, M. Sze, N.V. Knoers, and P.M. Deen Functional rescue of vasopressin V2 receptor mutants in MDCK cells by pharmacochaperones: relevance to therapy of nephrogenic diabetes insipidus Am J Physiol Renal Physiol 292 2007 F253 F260
    • (2007) Am J Physiol Renal Physiol , vol.292
    • Robben, J.H.1    Sze, M.2    Knoers, N.V.3    Deen, P.M.4
  • 90
    • 0036322898 scopus 로고    scopus 로고
    • Rescue of hypogonadotropic hypogonadism-causing and manufactured GnRH receptor mutants by a specific protein-folding template: Misrouted proteins as a novel disease etiology and therapeutic target
    • DOI 10.1210/jc.87.7.3255
    • J.A. Janovick, G. Maya-Nunez, and P.M. Conn Rescue of hypogonadotropic hypogonadism-causing and manufactured GnRH receptor mutants by a specific protein-folding template: misrouted proteins as a novel disease etiology and therapeutic target J Clin Endocrinol Metab 87 2002 3255 3262 (Pubitemid 34816374)
    • (2002) Journal of Clinical Endocrinology and Metabolism , vol.87 , Issue.7 , pp. 3255-3262
    • Janovick, J.A.1    Maya-Nunez, G.2    Conn, P.M.3
  • 91
    • 84891357083 scopus 로고    scopus 로고
    • Restoration of testis function in hypogonadotropic hypogonadal mice harboring a misfolded GnRHR mutant by pharmacoperone drug therapy
    • J.A. Janovick, M.D. Stewart, D. Jacob, L.D. Martin, J.M. Deng, and C.A. Stewart et al. Restoration of testis function in hypogonadotropic hypogonadal mice harboring a misfolded GnRHR mutant by pharmacoperone drug therapy Proc Natl Acad Sci USA 110 2013 21030 21035
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 21030-21035
    • Janovick, J.A.1    Stewart, M.D.2    Jacob, D.3    Martin, L.D.4    Deng, J.M.5    Stewart, C.A.6
  • 92
    • 80052682475 scopus 로고    scopus 로고
    • Pharmacological chaperones for misfolded gonadotropin-releasing hormone receptors
    • P.M. Conn, and A. Ulloa-Aguirre Pharmacological chaperones for misfolded gonadotropin-releasing hormone receptors Adv Pharmacol 62 2011 109 141
    • (2011) Adv Pharmacol , vol.62 , pp. 109-141
    • Conn, P.M.1    Ulloa-Aguirre, A.2
  • 93
    • 84855831674 scopus 로고    scopus 로고
    • Defective trafficking of rhodopsin and its role in retinal degenerations
    • T.J. Hollingsworth, and A.K. Gross Defective trafficking of rhodopsin and its role in retinal degenerations Int Rev Cell Mol Biol 293 2012 1 44
    • (2012) Int Rev Cell Mol Biol , vol.293 , pp. 1-44
    • Hollingsworth, T.J.1    Gross, A.K.2
  • 94
    • 0038529723 scopus 로고    scopus 로고
    • Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa
    • DOI 10.1074/jbc.M300087200
    • S.M. Noorwez, V. Kuksa, Y. Imanishi, L. Zhu, S. Filipek, and K. Palczewski et al. Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa J Biol Chem 278 2003 14442 14450 (Pubitemid 36799997)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14442-14450
    • Noorwez, S.M.1    Kuksa, V.2    Imanishi, Y.3    Zhu, L.4    Filipek, S.5    Palczewski, K.6    Kaushal, S.7
  • 95
    • 1942469395 scopus 로고    scopus 로고
    • Retinoids Assist the Cellular Folding of the Autosomal Dominant Retinitis Pigmentosa Opsin Mutant P23H
    • DOI 10.1074/jbc.M312101200
    • S.M. Noorwez, R. Malhotra, J.H. McDowell, K.A. Smith, M.P. Krebs, and S. Kaushal Retinoids assist the cellular folding of the autosomal dominant retinitis pigmentosa opsin mutant P23H J Biol Chem 279 2004 16278 16284 (Pubitemid 38509322)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16278-16284
    • Noorwez, S.M.1    Malhotra, R.2    McDowell, J.H.3    Smith, K.A.4    Krebs, M.P.5    Kaushal, S.6
  • 96
    • 73649098238 scopus 로고    scopus 로고
    • Molecular mechanisms of rhodopsin retinitis pigmentosa and the efficacy of pharmacological rescue
    • M.P. Krebs, D.C. Holden, P. Joshi, C.L. Clark 3rd, A.H. Lee, and S. Kaushal Molecular mechanisms of rhodopsin retinitis pigmentosa and the efficacy of pharmacological rescue J Mol Biol 395 2010 1063 1078
    • (2010) J Mol Biol , vol.395 , pp. 1063-1078
    • Krebs, M.P.1    Holden, D.C.2    Joshi, P.3    Clark III, C.L.4    Lee, A.H.5    Kaushal, S.6
  • 97
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation
    • DOI 10.1093/emboj/21.7.1628
    • U.E. Petaja-Repo, M. Hogue, S. Bhalla, A. Laperriere, J.P. Morello, and M. Bouvier Ligands act as pharmacological chaperones and increase the efficiency of delta opioid receptor maturation EMBO J 21 2002 1628 1637 (Pubitemid 34614619)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1628-1637
    • Petaja-Repo, U.E.1    Hogue, M.2    Bhalla, S.3    Laperriere, A.4    Morello, J.-P.5    Bouvier, M.6


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