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Volumn 9, Issue 7, 2013, Pages 444-454

Mechanism-based corrector combination restores ΔF508-CFTR folding and function

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; LUMACAFTOR; MEMBRANE PROTEIN; MEMBRANE SPANNING DOMAIN 1; MEMBRANE SPANNING DOMAIN 2; NUCLEOTIDE BINDING DOMAIN 1; NUCLEOTIDE BINDING DOMAIN 2; NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84879410121     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1253     Document Type: Article
Times cited : (336)

References (60)
  • 1
    • 50649123290 scopus 로고    scopus 로고
    • CFTR function and prospects for therapy
    • Riordan, J.R. CFTR function and prospects for therapy. Annu. Rev. Biochem. 77, 701-726 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 701-726
    • Riordan, J.R.1
  • 2
    • 55549094466 scopus 로고    scopus 로고
    • Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating
    • He, L. et al. Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating. J. Biol. Chem. 283, 26383-26390 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 26383-26390
    • He, L.1
  • 3
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • Serohijos, A.W. et al. Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function. Proc. Natl. Acad. Sci. USA 105, 3256-3261 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3256-3261
    • Serohijos, A.W.1
  • 4
    • 84879417365 scopus 로고    scopus 로고
    • Mechanisms of CFTR folding at the endoplasmic reticulum
    • Kim, S.J. & Skach, W.R. Mechanisms of CFTR folding at the endoplasmic reticulum. Front. Pharmacol. 3, 201 (2012).
    • (2012) Front. Pharmacol. , vol.3 , Issue.201
    • Kim, S.J.1    Skach, W.R.2
  • 5
    • 11444266284 scopus 로고    scopus 로고
    • The ΔF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • Du, K., Sharma, M. & Lukacs, G.L. The ΔF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR. Nat. Struct. Mol. Biol. 12, 17-25 (2005).
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 17-25
    • Du, K.1    Sharma, M.2    Lukacs, G.L.3
  • 6
    • 65249147217 scopus 로고    scopus 로고
    • Cooperative assembly and misfolding of CFTR domains in vivo
    • Du, K. & Lukacs, G.L. Cooperative assembly and misfolding of CFTR domains in vivo. Mol. Biol. Cell 20, 1903-1915 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1903-1915
    • Du, K.1    Lukacs, G.L.2
  • 7
    • 77954983869 scopus 로고    scopus 로고
    • Restoration of domain folding and interdomain assembly by second-site suppressors of the ΔF508 mutation in CFTR
    • He, L. et al. Restoration of domain folding and interdomain assembly by second-site suppressors of the ΔF508 mutation in CFTR. FASEB J. 24, 3103-3112 (2010).
    • (2010) FASEB J. , vol.24 , pp. 3103-3112
    • He, L.1
  • 8
    • 33845739839 scopus 로고    scopus 로고
    • Domain interdependence in the biosynthetic assembly of CFTR
    • Cui, L. et al. Domain interdependence in the biosynthetic assembly of CFTR. J. Mol. Biol. 365, 981-994 (2007).
    • (2007) J. Mol. Biol. , vol.365 , pp. 981-994
    • Cui, L.1
  • 10
    • 58149279835 scopus 로고    scopus 로고
    • Assembly and misassembly of cystic fibrosis transmembrane conductance regulator: Folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of membrane spanning domain (MSD) 1 and MSD2
    • Rosser, M.F., Grove, D.E., Chen, L. & Cyr, D.M. Assembly and misassembly of cystic fibrosis transmembrane conductance regulator: Folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of membrane spanning domain (MSD) 1 and MSD2. Mol. Biol. Cell 19, 4570-4579 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4570-4579
    • Rosser, M.F.1    Grove, D.E.2    Chen, L.3    Cyr, D.M.4
  • 12
    • 0346505482 scopus 로고    scopus 로고
    • New concepts of the pathogenesis of cystic fibrosis lung disease
    • Boucher, R.C. New concepts of the pathogenesis of cystic fibrosis lung disease. Eur. Respir. J. 23, 146-158 (2004).
    • (2004) Eur. Respir. J. , vol.23 , pp. 146-158
    • Boucher, R.C.1
  • 13
    • 84868255280 scopus 로고    scopus 로고
    • Proinflammatory cytokine secretion is suppressed by TMEM16A or CFTR channel activity in human cystic fibrosis bronchial epithelia
    • Veit, G. et al. Proinflammatory cytokine secretion is suppressed by TMEM16A or CFTR channel activity in human cystic fibrosis bronchial epithelia. Mol. Biol. Cell 23, 4188-4202 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4188-4202
    • Veit, G.1
  • 14
    • 81755163563 scopus 로고    scopus 로고
    • Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809
    • Van Goor, F. et al. Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809. Proc. Natl. Acad. Sci. USA 108, 18843-18848 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 18843-18848
    • Van Goor, F.1
  • 15
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning, G.M. et al. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358, 761-764 (1992).
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1
  • 16
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • Sato, S., Ward, C.L., Krouse, M.E., Wine, J.J. & Kopito, R.R. Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J. Biol. Chem. 271, 635-638 (1996).
    • (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
  • 17
    • 24644464284 scopus 로고    scopus 로고
    • Small-molecule correctors of defective ΔF508-CFTR cellular processing identified by high-throughput screening
    • Pedemonte, N. et al. Small-molecule correctors of defective ΔF508-CFTR cellular processing identified by high-throughput screening. J. Clin. Invest. 115, 2564-2571 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 2564-2571
    • Pedemonte, N.1
  • 18
    • 41149113942 scopus 로고    scopus 로고
    • Enhanced cell-surface stability of rescued ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) by pharmacological chaperones
    • Varga, K. et al. Enhanced cell-surface stability of rescued ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) by pharmacological chaperones. Biochem. J. 410, 555-564 (2008).
    • (2008) Biochem. J. , vol.410 , pp. 555-564
    • Varga, K.1
  • 19
    • 84873397801 scopus 로고    scopus 로고
    • Novel pharmacological strategies to treat cystic fibrosis
    • Hanrahan, J.W., Sampson, H.M. & Thomas, D.Y. Novel pharmacological strategies to treat cystic fibrosis. Trends Pharmacol. Sci. 34, 119-125 (2013).
    • (2013) Trends Pharmacol. Sci. , vol.34 , pp. 119-125
    • Hanrahan, J.W.1    Sampson, H.M.2    Thomas, D.Y.3
  • 20
    • 73249114731 scopus 로고    scopus 로고
    • Rescue of CF airway epithelial cell function in vitro by a CFTR potentiator VX-770
    • Van Goor, F. et al. Rescue of CF airway epithelial cell function in vitro by a CFTR potentiator, VX-770. Proc. Natl. Acad. Sci. USA 106, 18825-18830 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 18825-18830
    • Van Goor, F.1
  • 21
    • 84855202429 scopus 로고    scopus 로고
    • Results of a phase IIa study of VX-809, an investigational CFTR corrector compound, in subjects with cystic fibrosis homozygous for the F508del-CFTR mutation
    • Clancy, J.P. et al. Results of a phase IIa study of VX-809, an investigational CFTR corrector compound, in subjects with cystic fibrosis homozygous for the F508del-CFTR mutation. Thorax 67, 12-18 (2012).
    • (2012) Thorax , vol.67 , pp. 12-18
    • Clancy, J.P.1
  • 22
    • 79951829938 scopus 로고    scopus 로고
    • Identification of a NBD1-binding pharmacological chaperone that corrects the trafficking defect of F508del-CFTR
    • Sampson, H.M. et al. Identification of a NBD1-binding pharmacological chaperone that corrects the trafficking defect of F508del-CFTR. Chem. Biol. 18, 231-242 (2011).
    • (2011) Chem. Biol. , vol.18 , pp. 231-242
    • Sampson, H.M.1
  • 23
    • 0042317083 scopus 로고    scopus 로고
    • Mammalian osmolytes and S-nitrosoglutathione promote ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) protein maturation and function
    • Howard, M. et al. Mammalian osmolytes and S-nitrosoglutathione promote ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) protein maturation and function. J. Biol. Chem. 278, 35159-35167 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 35159-35167
    • Howard, M.1
  • 25
    • 77957302946 scopus 로고    scopus 로고
    • Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1
    • Protasevich, I. et al. Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1. Protein Sci. 19, 1917-1931 (2010).
    • (2010) Protein Sci. , vol.19 , pp. 1917-1931
    • Protasevich, I.1
  • 26
    • 77957309337 scopus 로고    scopus 로고
    • Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis
    • Wang, C. et al. Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis. Protein Sci. 19, 1932-1947 (2010).
    • (2010) Protein Sci. , vol.19 , pp. 1932-1947
    • Wang, C.1
  • 27
    • 84862908028 scopus 로고    scopus 로고
    • Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function
    • Rabeh, W.M. et al. Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function. Cell 148, 150-163 (2012).
    • (2012) Cell , vol.148 , pp. 150-163
    • Rabeh, W.M.1
  • 28
    • 84862909346 scopus 로고    scopus 로고
    • Requirements for efficient correction of ΔF508 CFTR revealed by analyses of evolved sequences
    • Mendoza, J.L. et al. Requirements for efficient correction of ΔF508 CFTR revealed by analyses of evolved sequences. Cell 148, 164-174 (2012).
    • (2012) Cell , vol.148 , pp. 164-174
    • Mendoza, J.L.1
  • 29
    • 77952399647 scopus 로고    scopus 로고
    • Correction of the Δphe508 cystic fibrosis transmembrane conductance regulator trafficking defect by the bioavailable compound glafenine
    • Robert, R. et al. Correction of the Δphe508 cystic fibrosis transmembrane conductance regulator trafficking defect by the bioavailable compound glafenine. Mol. Pharmacol. 77, 922-930 (2010).
    • (2010) Mol. Pharmacol. , vol.77 , pp. 922-930
    • Robert, R.1
  • 30
    • 77955025743 scopus 로고    scopus 로고
    • The V510D suppressor mutation stabilizes ΔF508-CFTR at the cell surface
    • Loo, T.W., Bartlett, M.C. & Clarke, D.M. The V510D suppressor mutation stabilizes ΔF508-CFTR at the cell surface. Biochemistry 49, 6352-6357 (2010).
    • (2010) Biochemistry , vol.49 , pp. 6352-6357
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 31
    • 0027153083 scopus 로고
    • Identification of revertants for the cystic fibrosis ΔF508 mutation using STE6-CFTR chimeras in yeast
    • Teem, J.L. et al. Identification of revertants for the cystic fibrosis ΔF508 mutation using STE6-CFTR chimeras in yeast. Cell 73, 335-346 (1993).
    • (1993) Cell , vol.73 , pp. 335-346
    • Teem, J.L.1
  • 32
    • 79955368563 scopus 로고    scopus 로고
    • Dual activity of aminoarylthiazoles on the trafficking and gating defects of the cystic fibrosis transmembrane conductance regulator chloride channel caused by cystic fibrosis mutations
    • Pedemonte, N. et al. Dual activity of aminoarylthiazoles on the trafficking and gating defects of the cystic fibrosis transmembrane conductance regulator chloride channel caused by cystic fibrosis mutations. J. Biol. Chem. 286, 15215-15226 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 15215-15226
    • Pedemonte, N.1
  • 33
    • 80053179441 scopus 로고    scopus 로고
    • Cyanoquinolines with independent corrector and potentiator activities restore ΔPhe508-cystic fibrosis transmembrane conductance regulator chloride channel function in cystic fibrosis
    • Phuan, P.W. et al. Cyanoquinolines with independent corrector and potentiator activities restore ΔPhe508-cystic fibrosis transmembrane conductance regulator chloride channel function in cystic fibrosis. Mol. Pharmacol. 80, 683-693 (2011).
    • (2011) Mol. Pharmacol. , vol.80 , pp. 683-693
    • Phuan, P.W.1
  • 34
    • 33745240417 scopus 로고    scopus 로고
    • F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive
    • Hegedus, T. et al. F508del CFTR with two altered RXR motifs escapes from ER quality control but its channel activity is thermally sensitive. Biochim. Biophys. Acta 1758, 565-572 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 565-572
    • Hegedus, T.1
  • 35
    • 84860271643 scopus 로고    scopus 로고
    • Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR
    • Aleksandrov, A.A. et al. Allosteric modulation balances thermodynamic stability and restores function of ΔF508 CFTR. J. Mol. Biol. 419, 41-60 (2012).
    • (2012) J. Mol. Biol. , vol.419 , pp. 41-60
    • Aleksandrov, A.A.1
  • 36
    • 84864258150 scopus 로고    scopus 로고
    • New model of cystic fibrosis transmembrane conductance regulator proposes active channel-like conformation
    • Dalton, J., Kalid, O., Schushan, M., Ben-Tal, N. & Villa-Freixa, J. New model of cystic fibrosis transmembrane conductance regulator proposes active channel-like conformation. J. Chem. Inf. Model. 52, 1842-1853 (2012).
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 1842-1853
    • Dalton, J.1    Kalid, O.2    Schushan, M.3    Ben-Tal, N.4    Villa-Freixa, J.5
  • 37
    • 78651264296 scopus 로고    scopus 로고
    • Small molecule correctors of F508del-CFTR discovered by structure-based virtual screening
    • Kalid, O. et al. Small molecule correctors of F508del-CFTR discovered by structure-based virtual screening. J. Comput. Aided Mol. Des. 24, 971-991 (2010).
    • (2010) J. Comput. Aided Mol. Des. , vol.24 , pp. 971-991
    • Kalid, O.1
  • 38
    • 84873436500 scopus 로고    scopus 로고
    • Correctors of ΔF508 CFTR restore global conformational maturation without thermally stabilizing the mutant protein
    • He, L. et al. Correctors of ΔF508 CFTR restore global conformational maturation without thermally stabilizing the mutant protein. FASEB J. 27, 536-545 (2013).
    • (2013) FASEB J. , vol.27 , pp. 536-545
    • He, L.1
  • 39
    • 78149270037 scopus 로고    scopus 로고
    • The cystic fibrosis-causing mutation ΔF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis
    • Thibodeau, P.H. et al. The cystic fibrosis-causing mutation ΔF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis. J. Biol. Chem. 285, 35825-35835 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 35825-35835
    • Thibodeau, P.H.1
  • 40
    • 70350236409 scopus 로고    scopus 로고
    • Mechanisms for rescue of correctable folding defects in CFTRΔF508
    • Grove, D.E., Rosser, M.F., Ren, H.Y., Naren, A.P. & Cyr, D.M. Mechanisms for rescue of correctable folding defects in CFTRΔF508. Mol. Biol. Cell 20, 4059-4069 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4059-4069
    • Grove, D.E.1    Rosser, M.F.2    Ren, H.Y.3    Naren, A.P.4    Cyr, D.M.5
  • 41
    • 0031915434 scopus 로고    scopus 로고
    • Limited proteolysis as a probe for arrested conformational maturation of ΔF508 CFTR
    • Zhang, F., Kartner, N. & Lukacs, G.L. Limited proteolysis as a probe for arrested conformational maturation of ΔF508 CFTR. Nat. Struct. Biol. 5, 180-183 (1998).
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 180-183
    • Zhang, F.1    Kartner, N.2    Lukacs, G.L.3
  • 42
    • 53549097399 scopus 로고    scopus 로고
    • Potent S-cis-locked bithiazole correctors of ΔF508 cystic fibrosis transmembrane conductance regulator cellular processing for cystic fibrosis therapy
    • Yu, G.J. et al. Potent S-cis-locked bithiazole correctors of ΔF508 cystic fibrosis transmembrane conductance regulator cellular processing for cystic fibrosis therapy. J. Med. Chem. 51, 6044-6054 (2008).
    • (2008) J. Med. Chem. , vol.51 , pp. 6044-6054
    • Yu, G.J.1
  • 43
    • 77955086020 scopus 로고    scopus 로고
    • Regulatory insertion removal restores maturation, stability and function of ΔF508 CFTR
    • Aleksandrov, A.A. et al. Regulatory insertion removal restores maturation, stability and function of ΔF508 CFTR. J. Mol. Biol. 401, 194-210 (2010).
    • (2010) J. Mol. Biol. , vol.401 , pp. 194-210
    • Aleksandrov, A.A.1
  • 44
    • 77449160593 scopus 로고    scopus 로고
    • Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry
    • Lewis, H.A. et al. Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry. J. Mol. Biol. 396, 406-430 (2010).
    • (2010) J. Mol. Biol. , vol.396 , pp. 406-430
    • Lewis, H.A.1
  • 45
    • 84879409164 scopus 로고    scopus 로고
    • A functional CFTR assay using primary cystic fibrosis intestinal organoids
    • in the press
    • Dekkers, J. et al. A functional CFTR assay using primary cystic fibrosis intestinal organoids. Nat. Med. (in the press).
    • Nat. Med
    • Dekkers, J.1
  • 46
    • 0347065355 scopus 로고    scopus 로고
    • Organic solutes rescue the functional defect in ΔF508 cystic fibrosis transmembrane conductance regulator
    • Zhang, X.M. et al. Organic solutes rescue the functional defect in ΔF508 cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 278, 51232-51242 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 51232-51242
    • Zhang, X.M.1
  • 47
    • 34548154971 scopus 로고    scopus 로고
    • Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutants
    • Wang, Y., Loo, T.W., Bartlett, M.C. & Clarke, D.M. Additive effect of multiple pharmacological chaperones on maturation of CFTR processing mutants. Biochem. J. 406, 257-263 (2007).
    • (2007) Biochem. J. , vol.406 , pp. 257-263
    • Wang, Y.1    Loo, T.W.2    Bartlett, M.C.3    Clarke, D.M.4
  • 49
    • 84862874979 scopus 로고    scopus 로고
    • Thermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: Protection by single suppressor mutations and inhibiting channel activity
    • Liu, X., O'Donnell, N., Landstrom, A., Skach, W.R. & Dawson, D.C. Thermal instability of ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR) channel function: Protection by single suppressor mutations and inhibiting channel activity. Biochemistry 51, 5113-5124 (2012).
    • (2012) Biochemistry , vol.51 , pp. 5113-5124
    • Liu, X.1    O'Donnell, N.2    Landstrom, A.3    Skach, W.R.4    Dawson, D.C.5
  • 50
    • 66849129301 scopus 로고    scopus 로고
    • A small-molecule modulator interacts directly with ΔPhe508-CFTR to modify its ATPase activity and conformational stability
    • Wellhauser, L. et al. A small-molecule modulator interacts directly with ΔPhe508-CFTR to modify its ATPase activity and conformational stability. Mol. Pharmacol. 75, 1430-1438 (2009).
    • (2009) Mol. Pharmacol. , vol.75 , pp. 1430-1438
    • Wellhauser, L.1
  • 51
    • 84868243529 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator (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. Cystic fibrosis transmembrane conductance regulator (CFTR) potentiator VX-770 (Ivacaftor) opens the defective channel gate of mutant CFTR in a phosphorylation-dependent but ATP-independent manner. J. Biol. Chem. 287, 36639-36649 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 36639-36649
    • Eckford, P.D.1    Li, C.2    Ramjeesingh, M.3    Bear, C.E.4
  • 52
    • 77955607650 scopus 로고    scopus 로고
    • Peripheral protein quality control removes unfolded CFTR from the plasma membrane
    • Okiyoneda, T. et al. Peripheral protein quality control removes unfolded CFTR from the plasma membrane. Science 329, 805-810 (2010).
    • (2010) Science , vol.329 , pp. 805-810
    • Okiyoneda, T.1
  • 53
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe, P.K. & Long, F.A. Use of glass electrodes to measure acidities in deuterium oxide. J. Phys. Chem. 64, 188-190 (1960).
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-190
    • Glasoe, P.K.1    Long, F.A.2
  • 54
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales, T.E. & Engen, J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25, 158-170 (2006).
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 55
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • Cornell, W.D. et al. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117, 5179-5197 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1
  • 56
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang, J., Cieplak, P. & Kollmann, P.A. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 21, 1049-1074 (2000).
    • (2000) J Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollmann, P.A.3
  • 57
    • 0346882663 scopus 로고    scopus 로고
    • ModLoop: Automated modeling of loops in protein structures
    • Fiser, A. & Sali, A. ModLoop: Automated modeling of loops in protein structures. Bioinformatics 19, 2500-2501 (2003).
    • (2003) Bioinformatics , vol.19 , pp. 2500-2501
    • Fiser, A.1    Sali, A.2
  • 58
    • 7544226311 scopus 로고    scopus 로고
    • Prodrg: A tool for high-throughput crystallography of protein-ligand complexes
    • Schüttelkopf, A.W. & van Aalten, D.M. PRODRG: A tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 60, 1355-1363 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1355-1363
    • Schüttelkopf, A.W.1    Van Aalten, D.M.2
  • 59
    • 70349932423 scopus 로고    scopus 로고
    • AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility
    • Morris, G.M. et al. AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. J. Comput. Chem. 30, 2785-2791 (2009).
    • (2009) J. Comput. Chem. , vol.30 , pp. 2785-2791
    • Morris, G.M.1
  • 60
    • 80054857419 scopus 로고    scopus 로고
    • Long-term expansion of epithelial organoids from human colon, adenoma, adenocarcinoma, and Barrett's epithelium
    • Sato, T. et al. Long-term expansion of epithelial organoids from human colon, adenoma, adenocarcinoma, and Barrett's epithelium. Gastroenterology 141, 1762-1772 (2011).
    • (2011) Gastroenterology , vol.141 , pp. 1762-1772
    • Sato, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.