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Volumn , Issue , 2005, Pages 71-93

GPCR Folding and Maturation: The Effect of Pharmacological Chaperones

Author keywords

Chemical Chaperone; Fabry Disease; Hypogonadotropic Hypogonadism; Nephrogenic Diabetes Insipidus; Pharmacological Chaperone

Indexed keywords


EID: 34447641568     PISSN: 2627535X     EISSN: 26275341     Source Type: Book Series    
DOI: 10.1007/978-1-59259-919-6_3     Document Type: Chapter
Times cited : (3)

References (130)
  • 1
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski K, Kumasaka T, Hori T, et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 2000;289:739–745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3
  • 2
    • 1942487807 scopus 로고    scopus 로고
    • First principles predictions of the structure and function of G-proteincoupled receptors: Validation for bovine rhodopsin
    • Trabanino RJ, Hall SE, Vaidehi N, Floriano WB, Kam VWT, Goddard WA 3rd. First principles predictions of the structure and function of G-proteincoupled receptors: validation for bovine rhodopsin. Biophys J 2004;86:1904–1921.
    • (2004) Biophys J , vol.86 , pp. 1904-1921
    • Trabanino, R.J.1    Hall, S.E.2    Vaidehi, N.3    Floriano, W.B.4    Kam, V.W.T.5    Goddard, W.A.6
  • 3
    • 0028834958 scopus 로고
    • Properties of N-terminal tails in G-protein coupled receptors: A statistical study
    • Wallin E, von Heijne G. Properties of N-terminal tails in G-protein coupled receptors: a statistical study. Protein Eng 1995;8:693–698.
    • (1995) Protein Eng , vol.8 , pp. 693-698
    • Wallin, E.1    von Heijne, G.2
  • 4
    • 0033790343 scopus 로고    scopus 로고
    • Helical membrane protein folding, stability, and evolution
    • Popot JL, Engelman DM. Helical membrane protein folding, stability, and evolution. Annu Rev Biochem 2000;69:881–922.
    • (2000) Annu Rev Biochem , vol.69 , pp. 881-922
    • Popot, J.L.1    Engelman, D.M.2
  • 5
    • 0023889603 scopus 로고
    • Chimeric α2-,β2-adrenergic receptors: Delineation of domains involved in effector coupling and ligand binding specificity
    • Kobilka BK, Kobilka TS, Daniel K, Regan JW, Caron MG, Lefkowitz RJ. Chimeric α2-,β2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity. Science 1988;240:1310–1316.
    • (1988) Science , vol.240 , pp. 1310-1316
    • Kobilka, B.K.1    Kobilka, T.S.2    Daniel, K.3    Regan, J.W.4    Caron, M.G.5    Lefkowitz, R.J.6
  • 6
    • 0028931922 scopus 로고
    • In vivo assembly of rhodopsin from expressed polypeptide fragments
    • Ridge KD, Lee SSJ, Yao LL. In vivo assembly of rhodopsin from expressed polypeptide fragments. Proc Natl Acad Sci USA 1995;92:3204–3208.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3204-3208
    • Ridge, K.D.1    Lee, S.S.J.2    Yao, L.L.3
  • 7
    • 85049320746 scopus 로고    scopus 로고
    • Schöneberg T, Liu J, Wess J. Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor. J Biol Chem 1995;270:18,000–18,006.
    • Schöneberg T, Liu J, Wess J. Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor. J Biol Chem 1995;270:18,000–18,006.
    • (2018) Applied Energy
  • 9
    • 85049320746 scopus 로고    scopus 로고
    • Kurtenbach E, Curtis CA, Pedder EK, Aitken A, Harris ACM, Hulme EC. Muscarinic acetylcholine receptors. Peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation. J Biol Chem 1990;265:13,702–13,708.
    • Kurtenbach E, Curtis CA, Pedder EK, Aitken A, Harris ACM, Hulme EC. Muscarinic acetylcholine receptors. Peptide sequencing identifies residues involved in antagonist binding and disulfide bond formation. J Biol Chem 1990;265:13,702–13,708.
    • (2018) Applied Energy
  • 10
    • 85049320746 scopus 로고    scopus 로고
    • Karnik SS, Khorana HG. Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. J Biol Chem 1990;265:17,520–17,524.
    • Karnik SS, Khorana HG. Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. J Biol Chem 1990;265:17,520–17,524.
    • (2018) Applied Energy
  • 11
    • 0035942215 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants
    • Hwa J, Klein-Seetharaman J, Khorana HG. Structure and function in rhodopsin: mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants. Proc Natl Acad Sci USA 2001;98:4872–4876.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4872-4876
    • Hwa, J.1    Klein-Seetharaman, J.2    Khorana, H.G.3
  • 12
    • 0030069077 scopus 로고    scopus 로고
    • The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: Presence of a disulfide bond
    • Boyd ND, Kage R, Dumas JJ, Krause JE, Leeman SE. The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: presence of a disulfide bond. Proc Natl Acad Sci USA 1996;93:433–437.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 433-437
    • Boyd, N.D.1    Kage, R.2    Dumas, J.J.3    Krause, J.E.4    Leeman, S.E.5
  • 13
    • 0035726693 scopus 로고    scopus 로고
    • G-protein-coupled receptor dimerization: Modulation of receptor function
    • Rios CD, Jordan BA, Gomes I, Devi LA. G-protein-coupled receptor dimerization: modulation of receptor function. Pharmacol Ther 2001;92:71–87.
    • (2001) Pharmacol Ther , vol.92 , pp. 71-87
    • Rios, C.D.1    Jordan, B.A.2    Gomes, I.3    Devi, L.A.4
  • 14
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: An emerging concept for G protein-coupled receptor ontogeny and function
    • Angers S, Salahpour A, Bouvier M. Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu Rev Pharmacol Toxicol 2002;42:409–435.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 15
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • George SR, O’Dowd BF, Lee SP. G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat Rev Drug Discov 2002;1:808–820.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 808-820
    • George, S.R.1    O’Dowd, B.F.2    Lee, S.P.3
  • 17
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr Rev 2000;21:90–113.
    • (2000) Endocr Rev , vol.21 , pp. 90-113
    • Gether, U.1
  • 20
    • 0035056623 scopus 로고    scopus 로고
    • 2a-adrenergic receptor conformational stability and cell-surface turnover
    • 2a-adrenergic receptor conformational stability and cell-surface turnover. Mol Pharmacol 2001;59:929–938.
    • (2001) Mol Pharmacol , vol.59 , pp. 929-938
    • Wilson, M.H.1    Highfield, H.A.2    Limbird, L.E.3
  • 21
    • 0026058548 scopus 로고
    • Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa
    • Sung CH, Schneider BG, Agarwal N, Papermaster DS, Nathans J. Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Proc Natl Acad Sci USA 1991;88:8840–8844.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8840-8844
    • Sung, C.H.1    Schneider, B.G.2    Agarwal, N.3    Papermaster, D.S.4    Nathans, J.5
  • 22
    • 85049320746 scopus 로고    scopus 로고
    • Bai M, Quinn S, Trivedi S, et al. Expression and characterization of inactivating and activating mutations in the human Ca
    • 2+ o-sensing receptor. J Biol Chem 1996;271:19,537–19,545.
    • (2018) Applied Energy
  • 23
    • 85049320746 scopus 로고    scopus 로고
    • Tanaka H, Moroi K, Iwai J, et al. Novel mutations of the endothelin B receptor gene in patients with Hirschsprung’s disease and their characterization. J Biol Chem 1998;273:11,378–11,383.
    • Tanaka H, Moroi K, Iwai J, et al. Novel mutations of the endothelin B receptor gene in patients with Hirschsprung’s disease and their characterization. J Biol Chem 1998;273:11,378–11,383.
    • (2018) Applied Energy
  • 24
    • 0034642294 scopus 로고    scopus 로고
    • Defective intracellular transport and processing of OA1 is a major cause of ocular albinism type 1
    • d’Addio M, Pizzigoni A, Bassi MT, et al. Defective intracellular transport and processing of OA1 is a major cause of ocular albinism type 1. Hum Mol Genet 2000;9:3011–3018.
    • (2000) Hum Mol Genet , vol.9 , pp. 3011-3018
    • D’Addio, M.1    Pizzigoni, A.2    Bassi, M.T.3
  • 25
    • 0033711033 scopus 로고    scopus 로고
    • Mutations of gonadotropins and gonadotropin receptors: Elucidating the physiology and pathophysiology of pituitarygonadal function
    • Themmen APN, Huhtaniemi IT. Mutations of gonadotropins and gonadotropin receptors: elucidating the physiology and pathophysiology of pituitarygonadal function. Endocr Rev 2000;21:551–583.
    • (2000) Endocr Rev , vol.21 , pp. 551-583
    • Themmen, A.P.N.1    Huhtaniemi, I.T.2
  • 27
    • 0035663195 scopus 로고    scopus 로고
    • Thyrotropin receptor mutations as a tool to understand thyrotropin receptor action
    • Wonerow P, Neumann S, Gudermann T, Paschke R. Thyrotropin receptor mutations as a tool to understand thyrotropin receptor action. J Mol Med 2001;79:707–721.
    • (2001) J Mol Med , vol.79 , pp. 707-721
    • Wonerow, P.1    Neumann, S.2    Gudermann, T.3    Paschke, R.4
  • 28
    • 0036774528 scopus 로고    scopus 로고
    • Receptor-misrouting: An unexpectedly prevalent and rescuable etiology in GnRHR-mediated hypogonadotropic hypogonadism
    • Leaños-Miranda A, Janovick JA, Conn PM. Receptor-misrouting: an unexpectedly prevalent and rescuable etiology in GnRHR-mediated hypogonadotropic hypogonadism. J Clin Endocrinol Metab 2002;87:4825–4828.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 4825-4828
    • Leaños-Miranda, A.1    Janovick, J.A.2    Conn, P.M.3
  • 29
    • 0037439274 scopus 로고    scopus 로고
    • Intracellular retention is a common characteristic of childhood obesity-associated MC4R mutations
    • Lubrano-Berthelier C, Durand E, Dubern B, et al. Intracellular retention is a common characteristic of childhood obesity-associated MC4R mutations. Hum Mol Genet 2003;12:145–153.
    • (2003) Hum Mol Genet , vol.12 , pp. 145-153
    • Lubrano-Berthelier, C.1    Durand, E.2    Dubern, B.3
  • 30
    • 1542358991 scopus 로고    scopus 로고
    • Inherited diseases involving G proteins and G protein-coupled receptors
    • Spiegel AM, Weinstein LS. Inherited diseases involving G proteins and G protein-coupled receptors. Annu Rev Med 2004;55:27–39.
    • (2004) Annu Rev Med , vol.55 , pp. 27-39
    • Spiegel, A.M.1    Weinstein, L.S.2
  • 31
    • 0034330457 scopus 로고    scopus 로고
    • Traffic jam: A compendium of human diseases that affect intracellular transport processes
    • Aridor M, Hannan LA. Traffic jam: a compendium of human diseases that affect intracellular transport processes. Traffic 2000;1:836–851.
    • (2000) Traffic , vol.1 , pp. 836-851
    • Aridor, M.1    Hannan, L.A.2
  • 32
    • 0036843129 scopus 로고    scopus 로고
    • Traffic jams II: An update of diseases of intracellular transport
    • Aridor M, Hannan LA. Traffic jams II: an update of diseases of intracellular transport. Traffic 2002;3:781–790.
    • (2002) Traffic , vol.3 , pp. 781-790
    • Aridor, M.1    Hannan, L.A.2
  • 33
    • 85049320746 scopus 로고    scopus 로고
    • Petäjä-Repo UE, Hogue M, Laperrière A, Walker P, Bouvier M. Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor. J Biol Chem 2000;275:13,727–13,736.
    • Petäjä-Repo UE, Hogue M, Laperrière A, Walker P, Bouvier M. Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor. J Biol Chem 2000;275:13,727–13,736.
    • (2018) Applied Energy
  • 34
    • 0035830863 scopus 로고    scopus 로고
    • Newly synthesized human δ opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome
    • Petäjä-Repo UE, Hogue M, Laperrière A, Bhalla S, Walker P, Bouvier M. Newly synthesized human δ opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome. J Biol Chem 2001;276:4416–4423.
    • (2001) J Biol Chem , vol.276 , pp. 4416-4423
    • Petäjä-Repo, U.E.1    Hogue, M.2    Laperrière, A.3    Bhalla, S.4    Walker, P.5    Bouvier, M.6
  • 35
    • 0027093726 scopus 로고
    • Identification and characterization of a luteinizing hormone/chorionic gonadotropin (LH/CG) receptor precursor in a human kidney cell line stably transfected with the rat luteal LH/CG receptor complementary DNA
    • Hipkin RW, Sánchez-Yagüe J, Ascoli M. Identification and characterization of a luteinizing hormone/chorionic gonadotropin (LH/CG) receptor precursor in a human kidney cell line stably transfected with the rat luteal LH/CG receptor complementary DNA. Mol Endocrinol 1992;6:2210–2218.
    • (1992) Mol Endocrinol , vol.6 , pp. 2210-2218
    • Hipkin, R.W.1    Sánchez-Yagüe, J.2    Ascoli, M.3
  • 36
    • 0030059066 scopus 로고    scopus 로고
    • Anti-human FSH receptor monoclonal antibodies: Immunochemical and immunocytochemical characterization of the receptor
    • Vannier B, Loosfelt H, Meduri G, Pichon C, Milgrom E. Anti-human FSH receptor monoclonal antibodies: immunochemical and immunocytochemical characterization of the receptor. Biochemistry 1996;35:1358–1366.
    • (1996) Biochemistry , vol.35 , pp. 1358-1366
    • Vannier, B.1    Loosfelt, H.2    Meduri, G.3    Pichon, C.4    Milgrom, E.5
  • 37
    • 0030614476 scopus 로고    scopus 로고
    • Basolateral localization and transcytosis of gonadotropin and thyrotropin receptors expressed in Madin-Darby canine kidney cells
    • Beau I, Misrahi M, Gross B, et al. Basolateral localization and transcytosis of gonadotropin and thyrotropin receptors expressed in Madin-Darby canine kidney cells. J Biol Chem 1997;272:5241–5248.
    • (1997) J Biol Chem , vol.272 , pp. 5241-5248
    • Beau, I.1    Misrahi, M.2    Gross, B.3
  • 39
    • 0345826101 scopus 로고    scopus 로고
    • Identification and structural characterization of the neuronal luteinizing hormone receptor associated with sensory systems
    • Apaja PM, Harju KT, Aatsinki JT, Petäjä-Repo UE, Rajaniemi HJ. Identification and structural characterization of the neuronal luteinizing hormone receptor associated with sensory systems. J Biol Chem 2004;279:1899–1906.
    • (2004) J Biol Chem , vol.279 , pp. 1899-1906
    • Apaja, P.M.1    Harju, K.T.2    Aatsinki, J.T.3    Petäjä-Repo, U.E.4    Rajaniemi, H.J.5
  • 40
    • 85049320746 scopus 로고    scopus 로고
    • Fishburn CS, Elazar Z, Fuchs S. Differential glycosylation and intracellular trafficking for the long and short isoforms of the D
    • 2 dopamine receptor. J Biol Chem 1995;270:29,819–29,824.
    • (2018) Applied Energy
  • 41
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and degradation of CFTR
    • Kopito RR. Biosynthesis and degradation of CFTR. Physiol Rev 1999;79:S167–S173.
    • (1999) Physiol Rev , vol.79 , pp. S167-S173
    • Kopito, R.R.1
  • 42
    • 0025279114 scopus 로고
    • 2-adrenergic receptor subtype, the gene for which is located on chromosome 2
    • 2-adrenergic receptor subtype, the gene for which is located on chromosome 2. Proc Natl Acad Sci USA 1990;87:5094–5098.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5094-5098
    • Lomasney, J.W.1    Lorenz, W.2    Allen, L.F.3
  • 43
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi AJ. Protein glucosylation and its role in protein folding. Annu Rev Biochem 2000;69:69–93.
    • (2000) Annu Rev Biochem , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 44
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A, Aebi M. Intracellular functions of N-linked glycans. Science 2001;291:2364–2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 45
    • 0032777709 scopus 로고    scopus 로고
    • O-Glycosylation of the V2 vasopressin receptor
    • Sadeghi H, Birnbaumer M. O-Glycosylation of the V2 vasopressin receptor. Glycobiology 1999;9:731–737.
    • (1999) Glycobiology , vol.9 , pp. 731-737
    • Sadeghi, H.1    Birnbaumer, M.2
  • 46
    • 0035805223 scopus 로고    scopus 로고
    • O-Glycosylation of G-protein-coupled receptor, octopus rhodopsin. Direct analysis by FAB mass spectrometry
    • Nakagawa M, Miyamoto T, Kusakabe R, et al. O-Glycosylation of G-protein-coupled receptor, octopus rhodopsin. Direct analysis by FAB mass spectrometry. FEBS Lett 2001;496:19–24.
    • (2001) FEBS Lett , vol.496 , pp. 19-24
    • Nakagawa, M.1    Miyamoto, T.2    Kusakabe, R.3
  • 47
    • 0038757730 scopus 로고    scopus 로고
    • Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function
    • Qanbar R, Bouvier M. Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function. Pharmacol Ther 2003;97:1–33.
    • (2003) Pharmacol Ther , vol.97 , pp. 1-33
    • Qanbar, R.1    Bouvier, M.2
  • 48
    • 85049320746 scopus 로고    scopus 로고
    • Rands E, Candelore MR, Cheung AH, Hill WS, Strader CD, Dixon RA. Mutational analysis of β-adrenergic receptor glycosylation. J Biol Chem 1990;265:10,759–10,764.
    • Rands E, Candelore MR, Cheung AH, Hill WS, Strader CD, Dixon RA. Mutational analysis of β-adrenergic receptor glycosylation. J Biol Chem 1990;265:10,759–10,764.
    • (2018) Applied Energy
  • 49
    • 0028354244 scopus 로고
    • Structure and function in rhodopsin: The role of asparagine-linked glycosylation
    • Kaushal S, Ridge KD, Khorana HG. Structure and function in rhodopsin: the role of asparagine-linked glycosylation. Proc Natl Acad Sci USA 1994;91:4024–4028.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4024-4028
    • Kaushal, S.1    Ridge, K.D.2    Khorana, H.G.3
  • 50
    • 0030051035 scopus 로고    scopus 로고
    • Mutagenesis of N glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane
    • Couvineau A, Fabre C, Gaudin P, Maoret JJ, Laburthe M. Mutagenesis of N glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane. Biochemistry 1996;35:1745–1752.
    • (1996) Biochemistry , vol.35 , pp. 1745-1752
    • Couvineau, A.1    Fabre, C.2    Gaudin, P.3    Maoret, J.J.4    Laburthe, M.5
  • 53
    • 0028872763 scopus 로고
    • The lutropin/choriogonadotropin receptor is palmitoylated at intracellular cysteine residues
    • Zhu H, Wang H, Ascoli M. The lutropin/choriogonadotropin receptor is palmitoylated at intracellular cysteine residues. Mol Endocrinol 1995;9:141–150.
    • (1995) Mol Endocrinol , vol.9 , pp. 141-150
    • Zhu, H.1    Wang, H.2    Ascoli, M.3
  • 54
    • 0031732763 scopus 로고    scopus 로고
    • Palmitoylation of human thyrotropin receptor: Slower intracellular trafficking of the palmitoylation-defective mutant
    • Tanaka K, Nagayama Y, Nishihara E, Namba H, Yamashita S, Niwa M. Palmitoylation of human thyrotropin receptor: slower intracellular trafficking of the palmitoylation-defective mutant. Endocrinology 1998;139:803–806.
    • (1998) Endocrinology , vol.139 , pp. 803-806
    • Tanaka, K.1    Nagayama, Y.2    Nishihara, E.3    Namba, H.4    Yamashita, S.5    Niwa, M.6
  • 55
    • 85049320746 scopus 로고    scopus 로고
    • Blanpain C, Wittamer V, Vanderwinden JM, et al. Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways. J Biol Chem 2001;276:23,795–23,804.
    • Blanpain C, Wittamer V, Vanderwinden JM, et al. Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways. J Biol Chem 2001;276:23,795–23,804.
    • (2018) Applied Energy
  • 56
    • 85049320746 scopus 로고    scopus 로고
    • Percherancier Y, Planchenault T, Valenzuela-Fernandez A, Virelizier JL, Arenzana-Seisdedos F, Bachelerie F. Palmitoylation-dependent control of degradation, life span, and membrane expression of the CCR5 receptor. J Biol Chem 2001;276:31,936–31,944.
    • Percherancier Y, Planchenault T, Valenzuela-Fernandez A, Virelizier JL, Arenzana-Seisdedos F, Bachelerie F. Palmitoylation-dependent control of degradation, life span, and membrane expression of the CCR5 receptor. J Biol Chem 2001;276:31,936–31,944.
    • (2018) Applied Energy
  • 57
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A. Setting the standards: quality control in the secretory pathway. Science 1999;286:1882–1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 58
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L, Helenius A. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 2003;4:181–191.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 59
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta ES, Parodi AJ. Quality control and protein folding in the secretory pathway. Annu Rev Cell Dev Biol 2003;19:649–676.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 60
    • 0031734361 scopus 로고    scopus 로고
    • Association of gonadotropin receptor precursors with the protein folding chaperone calnexin
    • Rozell TG, Davis DP, Chai Y, Segaloff DL. Association of gonadotropin receptor precursors with the protein folding chaperone calnexin. Endocrinology 1998;139:1588–1593.
    • (1998) Endocrinology , vol.139 , pp. 1588-1593
    • Rozell, T.G.1    Davis, D.P.2    Chai, Y.3    Segaloff, D.L.4
  • 61
    • 0035849533 scopus 로고    scopus 로고
    • Association of calnexin with wild type and mutant AVPR2 that causes nephrogenic diabetes insipidus
    • Morello JP, Salahpour A, Petäjä-Repo UE, et al. Association of calnexin with wild type and mutant AVPR2 that causes nephrogenic diabetes insipidus. Biochemistry 2001;40:6766–6775.
    • (2001) Biochemistry , vol.40 , pp. 6766-6775
    • Morello, J.P.1    Salahpour, A.2    Petäjä-Repo, U.E.3
  • 62
    • 0036413254 scopus 로고    scopus 로고
    • Association of the thyrotropin receptor with calnexin, calreticulin and BiP. Effects on the maturation of the receptor
    • Siffroi-Fernandez S, Giraud A, Lanet J, Franc JL. Association of the thyrotropin receptor with calnexin, calreticulin and BiP. Effects on the maturation of the receptor. Eur J Biochem 2002;269:4930–4937.
    • (2002) Eur J Biochem , vol.269 , pp. 4930-4937
    • Siffroi-Fernandez, S.1    Giraud, A.2    Lanet, J.3    Franc, J.L.4
  • 63
    • 0038147442 scopus 로고    scopus 로고
    • Endoplasmic reticulum retention, degradation, and aggregation of olfactory G-protein coupled receptors
    • Lu M, Echeverri F, Moyer BD. Endoplasmic reticulum retention, degradation, and aggregation of olfactory G-protein coupled receptors. Traffic 2003;4:416–433.
    • (2003) Traffic , vol.4 , pp. 416-433
    • Lu, M.1    Echeverri, F.2    Moyer, B.D.3
  • 64
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/ Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham GC, Lu Z, King S, Sorscher E, Tousson A, Cyr DM. The Hdj-2/ Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J 1999;18:1492–1505.
    • (1999) EMBO J , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 65
    • 85049320746 scopus 로고    scopus 로고
    • Chapple JP, Cheetham ME. The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. J Biol Chem 2003;278:19,087–19,094.
    • Chapple JP, Cheetham ME. The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation. J Biol Chem 2003;278:19,087–19,094.
    • (2018) Applied Energy
  • 67
    • 0035011489 scopus 로고    scopus 로고
    • Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein
    • Bermak JC, Li M, Bullock C, Zhou QY. Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein. Nat Cell Biol 2001;3:492–498.
    • (2001) Nat Cell Biol , vol.3 , pp. 492-498
    • Bermak, J.C.1    Li, M.2    Bullock, C.3    Zhou, Q.Y.4
  • 68
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley NJ, Baker EK, Stamnes MA, Zuker CS. The cyclophilin homolog ninaA is required in the secretory pathway. Cell 1991;67:255–263.
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1    Baker, E.K.2    Stamnes, M.A.3    Zuker, C.S.4
  • 69
    • 0029859847 scopus 로고    scopus 로고
    • Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin
    • Ferreira PA, Nakayama TA, Pak WL, Travis GH. Cyclophilin-related protein RanBP2 acts as chaperone for red/green opsin. Nature 1996;383:637–640.
    • (1996) Nature , vol.383 , pp. 637-640
    • Ferreira, P.A.1    Nakayama, T.A.2    Pak, W.L.3    Travis, G.H.4
  • 70
    • 0032076851 scopus 로고    scopus 로고
    • Odorant receptor localization to olfactory cilia is mediated by ODR-4, a novel membrane-associated protein
    • Dwyer ND, Troemel ER, Sengupta P, Bargmann CI. Odorant receptor localization to olfactory cilia is mediated by ODR-4, a novel membrane-associated protein. Cell 1998;93:455–466.
    • (1998) Cell , vol.93 , pp. 455-466
    • Dwyer, N.D.1    Troemel, E.R.2    Sengupta, P.3    Bargmann, C.I.4
  • 71
    • 0037423953 scopus 로고    scopus 로고
    • Functional expression of murine V2R pheromone receptors involves selective association with the M10 and M1 families of MHC class Ib molecules
    • Loconto J, Papes F, Chang E, et al. Functional expression of murine V2R pheromone receptors involves selective association with the M10 and M1 families of MHC class Ib molecules. Cell 2003;112:607–618.
    • (2003) Cell , vol.112 , pp. 607-618
    • Loconto, J.1    Papes, F.2    Chang, E.3
  • 72
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
    • McLatchie LM, Fraser NJ, Main MJ, et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 1998;393:333–339.
    • (1998) Nature , vol.393 , pp. 333-339
    • McLatchie, L.M.1    Fraser, N.J.2    Main, M.J.3
  • 73
    • 0033013790 scopus 로고    scopus 로고
    • The amino terminus of receptor activity modifying proteins is a critical determinant of glycosylation state and ligand binding of calcitonin receptor-like receptor
    • Fraser NJ, Wise A, Brown J, McLatchie LM, Main MJ, Foord SM. The amino terminus of receptor activity modifying proteins is a critical determinant of glycosylation state and ligand binding of calcitonin receptor-like receptor. Mol Pharmacol 1999;55:1054–1059.
    • (1999) Mol Pharmacol , vol.55 , pp. 1054-1059
    • Fraser, N.J.1    Wise, A.2    Brown, J.3    McLatchie, L.M.4    Main, M.J.5    Foord, S.M.6
  • 77
  • 79
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito RR. ER quality control: the cytoplasmic connection. Cell 1997;88:427–430.
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 80
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathways
    • Bonifacino JS, Weissman AM. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu Rev Cell Dev Biol 1998;14:19–57.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 81
    • 0037287977 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein degradation
    • Jarosch E, Lenk U, Sommer T. Endoplasmic reticulum-associated protein degradation. Int Rev Cytol 2003;223:39–81.
    • (2003) Int Rev Cytol , vol.223 , pp. 39-81
    • Jarosch, E.1    Lenk, U.2    Sommer, T.3
  • 82
    • 0032536903 scopus 로고    scopus 로고
    • Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
    • Yang M, Omura S, Bonifacino JS, Weissman AM. Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J Exp Med 1998;187:835–846.
    • (1998) J Exp Med , vol.187 , pp. 835-846
    • Yang, M.1    Omura, S.2    Bonifacino, J.S.3    Weissman, A.M.4
  • 83
    • 0033605219 scopus 로고    scopus 로고
    • Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
    • Liu Y, Choudhury P, Cabral CM, Sifers RN. Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. J Biol Chem 1999;274:5861–5867.
    • (1999) J Biol Chem , vol.274 , pp. 5861-5867
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 84
    • 0034981027 scopus 로고    scopus 로고
    • A novel ER a-mannosidase-like protein accelerates ER-associated degradation
    • Hosokawa N, Wada I, Hasegawa K, et al. A novel ER a-mannosidase-like protein accelerates ER-associated degradation. EMBO Rep 2001;2:415–422.
    • (2001) EMBO Rep , vol.2 , pp. 415-422
    • Hosokawa, N.1    Wada, I.2    Hasegawa, K.3
  • 85
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari M, Calanca V, Galli C, Lucca P, Paganetti P. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 2003;299:1397–1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 86
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y, Hosokawa N, Wada I, Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 2003;299:1394–1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 87
    • 85049320746 scopus 로고    scopus 로고
    • Illing ME, Rajan RS, Bence NF, Kopito RR. A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J Biol Chem 2002;277:34,150–34,160.
    • Illing ME, Rajan RS, Bence NF, Kopito RR. A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J Biol Chem 2002;277:34,150–34,160.
    • (2018) Applied Energy
  • 88
    • 0037099080 scopus 로고    scopus 로고
    • The cellular fate of mutant rhodopsin: Quality control, degradation and aggresome formation
    • Saliba RS, Munro PMG, Luthert PJ, Cheetham ME. The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J Cell Sci 2002;115:2907–2918.
    • (2002) J Cell Sci , vol.115 , pp. 2907-2918
    • Saliba, R.S.1    Munro, P.M.G.2    Luthert, P.J.3    Cheetham, M.E.4
  • 90
    • 0042835772 scopus 로고    scopus 로고
    • Thyrotropin-releasing hormone receptor processing: Role of ubiquitination and proteasomal degradation
    • Cook LB, Zhu CC, Hinkle PM. Thyrotropin-releasing hormone receptor processing: role of ubiquitination and proteasomal degradation. Mol Endocrinol 2003;17:1777–1791.
    • (2003) Mol Endocrinol , vol.17 , pp. 1777-1791
    • Cook, L.B.1    Zhu, C.C.2    Hinkle, P.M.3
  • 91
  • 92
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol–water mixtures
    • Gekko K, Timasheff SN. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol–water mixtures. Biochemistry 1981;20:4667–4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 93
    • 0026534357 scopus 로고
    • Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol
    • Sawano H, Koumoto Y, Ohta K, Sasaki Y, Segawa S, Tachibana H. Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol. FEBS Lett 1992;303:11–14.
    • (1992) FEBS Lett , vol.303 , pp. 11-14
    • Sawano, H.1    Koumoto, Y.2    Ohta, K.3    Sasaki, Y.4    Segawa, S.5    Tachibana, H.6
  • 94
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the ΔF508 cystic fibrosis transmembrane conductance regulator protein
    • Brown CR, Hong-Brown LQ, Biwersi J, Verkman AS, Welch WJ. Chemical chaperones correct the mutant phenotype of the ΔF508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones 1996;1:117–125.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 95
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • Sato S, Ward CL, Krouse ME, Wine JJ, Kopito RR. Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J Biol Chem 1996;271:635–638.
    • (1996) J Biol Chem , vol.271 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5
  • 96
    • 0032524048 scopus 로고    scopus 로고
    • Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones
    • Tamarappoo BK, Verkman AS. Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones. J Clin Invest 1998; 101:2257–2267.
    • (1998) J Clin Invest , vol.101 , pp. 2257-2267
    • Tamarappoo, B.K.1    Verkman, A.S.2
  • 97
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant a1-antitrypsin (α1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in α1-AT deficiency
    • Burrows JAJ, Willis LK, Perlmutter DH. Chemical chaperones mediate increased secretion of mutant a1-antitrypsin (α1-AT) Z: a potential pharmacological strategy for prevention of liver injury and emphysema in α1-AT deficiency. Proc Natl Acad Sci USA 2000;97:1796–1801.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1796-1801
    • Burrows, J.A.J.1    Willis, L.K.2    Perlmutter, D.H.3
  • 98
    • 85047683541 scopus 로고    scopus 로고
    • Chemical chaperones: A pharmacological strategy for disorders of protein folding and trafficking
    • Perlmutter DH. Chemical chaperones: a pharmacological strategy for disorders of protein folding and trafficking. Pediatr Res 2002;52:832–836.
    • (2002) Pediatr Res , vol.52 , pp. 832-836
    • Perlmutter, D.H.1
  • 99
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen DW, Baskakov IV. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J Mol Biol 2001;310:955–963.
    • (2001) J Mol Biol , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 100
    • 0031021804 scopus 로고    scopus 로고
    • Correction of defective protein kinesis of human P glycoprotein mutants by substrates and modulators
    • Loo TW, Clarke DM. Correction of defective protein kinesis of human P glycoprotein mutants by substrates and modulators. J Biol Chem 1997;272:709–712.
    • (1997) J Biol Chem , vol.272 , pp. 709-712
    • Loo, T.W.1    Clarke, D.M.2
  • 101
    • 0033018496 scopus 로고    scopus 로고
    • Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor
    • Fan JQ, Ishii S, Asano N, Suzuki Y. Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat Med 1999;5:112–115.
    • (1999) Nat Med , vol.5 , pp. 112-115
    • Fan, J.Q.1    Ishii, S.2    Asano, N.3    Suzuki, Y.4
  • 102
    • 0033936361 scopus 로고    scopus 로고
    • In vitro inhibition and intracellular enhancement of lysosomal α-galactosidase A activity in Fabry lymphoblasts by 1deoxygalactonojirimycin and its derivatives
    • Asano N, Ishii S, Kizu H, et al. In vitro inhibition and intracellular enhancement of lysosomal α-galactosidase A activity in Fabry lymphoblasts by 1deoxygalactonojirimycin and its derivatives. Eur J Biochem 2000;267:4179–4186.
    • (2000) Eur J Biochem , vol.267 , pp. 4179-4186
    • Asano, N.1    Ishii, S.2    Kizu, H.3
  • 103
    • 85049320746 scopus 로고    scopus 로고
    • Matsuda J, Suzuki O, Oshima A, et al. Chemical chaperone therapy for brain pathology in G
    • M1-gangliosidosis. Proc Natl Acad Sci USA 2003;100:15,912– 15,917.
    • (2018) Applied Energy
  • 104
    • 85049320746 scopus 로고    scopus 로고
    • Sawkar AR, Cheng WC, Beutler E, Wong CH, Balch WE, Kelly JW. Chemical chaperones increase the cellular activity of N370S β-glucosidase: a therapeutic strategy for Gaucher disease. Proc Natl Acad Sci USA 2002;99:15,428–15,433.
    • Sawkar AR, Cheng WC, Beutler E, Wong CH, Balch WE, Kelly JW. Chemical chaperones increase the cellular activity of N370S β-glucosidase: a therapeutic strategy for Gaucher disease. Proc Natl Acad Sci USA 2002;99:15,428–15,433.
    • (2018) Applied Energy
  • 105
    • 85049320746 scopus 로고    scopus 로고
    • Zhou Z, Gong Q, January CT. Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects. J Biol Chem 1999;274:31,123–31,126.
    • Zhou Z, Gong Q, January CT. Correction of defective protein trafficking of a mutant HERG potassium channel in human long QT syndrome. Pharmacological and temperature effects. J Biol Chem 1999;274:31,123–31,126.
    • (2018) Applied Energy
  • 106
    • 0037085464 scopus 로고    scopus 로고
    • The binding site for channel blockers that rescue misprocessed human long QT syndrome type 2 ether-agogo-related gene (HERG) mutations
    • Ficker E, Obejero-Paz CA, Zhao S, Brown AM. The binding site for channel blockers that rescue misprocessed human long QT syndrome type 2 ether-agogo-related gene (HERG) mutations. J Biol Chem 2002;277:4989–4998.
    • (2002) J Biol Chem , vol.277 , pp. 4989-4998
    • Ficker, E.1    Obejero-Paz, C.A.2    Zhao, S.3    Brown, A.M.4
  • 107
    • 85049320746 scopus 로고    scopus 로고
    • Paulussen A, Raes A, Matthijs G, Snyders DJ, Cohen N, Aerssens J. A novel mutation (T65P) in the PAS domain of the human potassium channel HERG results in the long QT syndrome by trafficking deficiency. J Biol Chem 2002;277:48,610–48,616.
    • Paulussen A, Raes A, Matthijs G, Snyders DJ, Cohen N, Aerssens J. A novel mutation (T65P) in the PAS domain of the human potassium channel HERG results in the long QT syndrome by trafficking deficiency. J Biol Chem 2002;277:48,610–48,616.
    • (2018) Applied Energy
  • 108
    • 0037129911 scopus 로고    scopus 로고
    • + channel long-QT2 mutations: Human ether-a-go-go-related gene rescue without block
    • + channel long-QT2 mutations: human ether-a-go-go-related gene rescue without block. Circulation 2002;105:2830–2835.
    • (2002) Circulation , vol.105 , pp. 2830-2835
    • Rajamani, S.1    Anderson, C.L.2    Anson, B.D.3    January, C.T.4
  • 109
    • 85049320746 scopus 로고    scopus 로고
    • Yan F, Lin CW, Weisiger E, Cartier EA, Taschenberger G, Shyng SL. Sulfonylureas correct trafficking defects of ATP-sensitive potassium channels caused by mutations in the sulfonylurea receptor. J Biol Chem 2004;279:11,096–11,105.
    • Yan F, Lin CW, Weisiger E, Cartier EA, Taschenberger G, Shyng SL. Sulfonylureas correct trafficking defects of ATP-sensitive potassium channels caused by mutations in the sulfonylurea receptor. J Biol Chem 2004;279:11,096–11,105.
    • (2018) Applied Energy
  • 110
    • 85049320746 scopus 로고    scopus 로고
    • Halaban R, Cheng E, Svedine S, Aron R, Hebert DN. Proper folding and endoplasmic reticulum to Golgi transport of tyrosinase are induced by its substrates, DOPA and tyrosine. J Biol Chem 2001;276:11,933–11,938.
    • Halaban R, Cheng E, Svedine S, Aron R, Hebert DN. Proper folding and endoplasmic reticulum to Golgi transport of tyrosinase are induced by its substrates, DOPA and tyrosine. J Biol Chem 2001;276:11,933–11,938.
    • (2018) Applied Energy
  • 111
    • 85049320746 scopus 로고    scopus 로고
    • Wiens GD, O’Hare T, Rittenberg MB. Recovering antibody secretion using a hapten ligand as a chemical chaperone. J Biol Chem 2001;276:40,933–40,939.
    • Wiens GD, O’Hare T, Rittenberg MB. Recovering antibody secretion using a hapten ligand as a chemical chaperone. J Biol Chem 2001;276:40,933–40,939.
    • (2018) Applied Energy
  • 112
    • 0037154149 scopus 로고    scopus 로고
    • A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants
    • Friedler A, Hansson LO, Veprintsev DB, et al. A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants. Proc Natl Acad Sci USA 2002;99:937–942.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 937-942
    • Friedler, A.1    Hansson, L.O.2    Veprintsev, D.B.3
  • 113
    • 85049320746 scopus 로고    scopus 로고
    • Issaeva N, Friedler A, Bozko P, Wiman KG, Fersht AR, Selivanova G. Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide. Proc Natl Acad Sci USA 2003;100:13,303–13,307.
    • Issaeva N, Friedler A, Bozko P, Wiman KG, Fersht AR, Selivanova G. Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide. Proc Natl Acad Sci USA 2003;100:13,303–13,307.
    • (2018) Applied Energy
  • 114
    • 0034118221 scopus 로고    scopus 로고
    • Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants
    • Morello JP, Salahpour A, Laperrière A, et al. Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J Clin Invest 2000;105:887–895.
    • (2000) J Clin Invest , vol.105 , pp. 887-895
    • Morello, J.P.1    Salahpour, A.2    Laperrière, A.3
  • 115
    • 85049320746 scopus 로고    scopus 로고
    • Tan CM, Nickols HH, Limbird LE. Appropriate polarization following pharmacological rescue of V2 vasopressin receptors encoded by X-linked nephrogenic diabetes insipidus alleles involves a conformation of the receptor that also attains mature glycosylation. J Biol Chem 2003;278:35,678–35,686.
    • Tan CM, Nickols HH, Limbird LE. Appropriate polarization following pharmacological rescue of V2 vasopressin receptors encoded by X-linked nephrogenic diabetes insipidus alleles involves a conformation of the receptor that also attains mature glycosylation. J Biol Chem 2003;278:35,678–35,686.
    • (2018) Applied Energy
  • 116
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation
    • Petäjä-Repo UE, Hogue M, Bhalla S, Laperrière A, Morello JP, Bouvier M. Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation. EMBO J 2002;21:1628–1637.
    • (2002) EMBO J , vol.21 , pp. 1628-1637
    • Petäjä-Repo, U.E.1    Hogue, M.2    Bhalla, S.3    Laperrière, A.4    Morello, J.P.5    Bouvier, M.6
  • 117
    • 0037561587 scopus 로고    scopus 로고
    • Rescuing the traffic-deficient mutants of rat μ-opioid receptors with hydrophobic ligands
    • Chaipatikul V, Erickson-Herbrandson LJ, Loh HH, Law PY. Rescuing the traffic-deficient mutants of rat μ-opioid receptors with hydrophobic ligands. Mol Pharmacol 2003;64:32–41.
    • (2003) Mol Pharmacol , vol.64 , pp. 32-41
    • Chaipatikul, V.1    Erickson-Herbrandson, L.J.2    Loh, H.H.3    Law, P.Y.4
  • 118
    • 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
    • Janovick JA, Maya-Nunez G, Conn PM. 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 2002;87:3255–3262.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 3255-3262
    • Janovick, J.A.1    Maya-Nunez, G.2    Conn, P.M.3
  • 119
    • 0344059035 scopus 로고    scopus 로고
    • Structure–activity relations of successful pharmacologic chaperones for rescue of naturally occurring and manufactured mutants of the gonadotropin-releasing hormone receptor
    • Janovick JA, Goulet M, Bush E, Greer J, Wettlaufer DG, Conn PM. Structure–activity relations of successful pharmacologic chaperones for rescue of naturally occurring and manufactured mutants of the gonadotropin-releasing hormone receptor. J Pharmacol Exp Ther 2003;305:608–614.
    • (2003) J Pharmacol Exp Ther , vol.305 , pp. 608-614
    • Janovick, J.A.1    Goulet, M.2    Bush, E.3    Greer, J.4    Wettlaufer, D.G.5    Conn, P.M.6
  • 120
    • 85049320746 scopus 로고    scopus 로고
    • Li T, Sandberg MA, Pawlyk BS, et al. Effect of vitamin A supplementation on rhodopsin mutants threonine-17 → methionine and proline-347 → serine in transgenic mice and in cell cultures. Proc Natl Acad Sci USA 1998;95:11,933–11,938.
    • Li T, Sandberg MA, Pawlyk BS, et al. Effect of vitamin A supplementation on rhodopsin mutants threonine-17 → methionine and proline-347 → serine in transgenic mice and in cell cultures. Proc Natl Acad Sci USA 1998;95:11,933–11,938.
    • (2018) Applied Energy
  • 121
    • 85049320746 scopus 로고    scopus 로고
    • Noorwez SM, Kuksa V, Imanishi Y, et al. Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa. J Biol Chem 2003;278:14,442–14,450.
    • Noorwez SM, Kuksa V, Imanishi Y, et al. Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa. J Biol Chem 2003;278:14,442–14,450.
    • (2018) Applied Energy
  • 122
    • 85049320746 scopus 로고    scopus 로고
    • Noorwez SM, Malhotra R, McDowell JH, Smith KA, Krebs MP, Kaushal S. Retinoids assist the cellular folding of the autosomal dominant retinitis pigmentosa opsin mutant P23H. J Biol Chem 2004;279:16,278–16,284.
    • Noorwez SM, Malhotra R, McDowell JH, Smith KA, Krebs MP, Kaushal S. Retinoids assist the cellular folding of the autosomal dominant retinitis pigmentosa opsin mutant P23H. J Biol Chem 2004;279:16,278–16,284.
    • (2018) Applied Energy
  • 124
    • 0000401592 scopus 로고    scopus 로고
    • Protein origami: Therapeutic rescue of misfolded gene products
    • Conn PM, Leaños-Miranda A, Janovick JA. Protein origami: therapeutic rescue of misfolded gene products. Mol Intervent 2002;2:308–316.
    • (2002) Mol Intervent , vol.2 , pp. 308-316
    • Conn, P.M.1    Leaños-Miranda, A.2    Janovick, J.A.3
  • 125
    • 0026686623 scopus 로고
    • Thermodynamic measurements of the contributions of helix-connecting loops and of retinal to the stability of bacteriorhodopsin
    • Kahn TW, Sturtevant JM, Engelman DM. Thermodynamic measurements of the contributions of helix-connecting loops and of retinal to the stability of bacteriorhodopsin. Biochemistry 1992;31:8829–8839.
    • (1992) Biochemistry , vol.31 , pp. 8829-8839
    • Kahn, T.W.1    Sturtevant, J.M.2    Engelman, D.M.3
  • 127
    • 0038309550 scopus 로고    scopus 로고
    • Protein stability induced by ligand binding correlates with changes in protein flexibility
    • Celej MS, Montich GG, Fidelio GD. Protein stability induced by ligand binding correlates with changes in protein flexibility. Protein Sci 2003;12:1496–1506.
    • (2003) Protein Sci , vol.12 , pp. 1496-1506
    • Celej, M.S.1    Montich, G.G.2    Fidelio, G.D.3
  • 128
    • 0036895451 scopus 로고    scopus 로고
    • Enzyme replacement and enhancement therapies: Lessons from lysosomal disorders
    • Desnick RJ, Schuchman EH. Enzyme replacement and enhancement therapies: lessons from lysosomal disorders. Nat Rev Genet 2002;3:954–966.
    • (2002) Nat Rev Genet , vol.3 , pp. 954-966
    • Desnick, R.J.1    Schuchman, E.H.2
  • 129
    • 0043235841 scopus 로고    scopus 로고
    • A contradictory treatment for lysosomal storage disorders: Inhibitors enhance mutant enzyme activity
    • Fan JQ. A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity. Trends Pharmacol Sci 2003;24:355–360.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 355-360
    • Fan, J.Q.1
  • 130
    • 0038637206 scopus 로고    scopus 로고
    • Dominant-negative action of disease-causing gonadotropin-releasing hormone receptor (GnRHR) mutants: A trait that potentially coevolved with decreased plasma membrane expression of GnRHR in humans
    • Leaños-Miranda A, Ulloa-Aguirre A, Ji TH, Janovick JA, Conn PM. Dominant-negative action of disease-causing gonadotropin-releasing hormone receptor (GnRHR) mutants: a trait that potentially coevolved with decreased plasma membrane expression of GnRHR in humans. J Clin Endocrinol Metab 2003;88:3360–3367.
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 3360-3367
    • Leaños-Miranda, A.1    Ulloa-Aguirre, A.2    Ji, T.H.3    Janovick, J.A.4    Conn, P.M.5


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