메뉴 건너뛰기




Volumn 17, Issue 7, 2013, Pages 889-900

Impaired surface expression and conductance of the KCNQ4 channel lead to sensorineural hearing loss

Author keywords

Hearing loss; KCNQ4; Molecular chaperone; Mutations; Potassium channel; Surface expression; Trafficking

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 90; KCNQ4 PROTEIN, HUMAN; POTASSIUM CHANNEL; POTASSIUM CHANNEL KCNQ;

EID: 84880822048     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/jcmm.12080     Document Type: Article
Times cited : (35)

References (62)
  • 2
    • 0034303612 scopus 로고    scopus 로고
    • Neuronal KCNQ potassium channels: physiology and role in disease
    • Jentsch TJ. Neuronal KCNQ potassium channels: physiology and role in disease. Nat Rev Neurosci. 2000; 1: 21-30.
    • (2000) Nat Rev Neurosci , vol.1 , pp. 21-30
    • Jentsch, T.J.1
  • 3
    • 45549105945 scopus 로고    scopus 로고
    • Kv7 (KCNQ) potassium channels that are mutated in human diseases
    • Brown DA. Kv7 (KCNQ) potassium channels that are mutated in human diseases. J Physiol. 2008; 586: 1781-3.
    • (2008) J Physiol , vol.586 , pp. 1781-1783
    • Brown, D.A.1
  • 4
    • 0034693298 scopus 로고    scopus 로고
    • Longitudinal gradients of KCNQ4 expression in spiral ganglion and cochlear hair cells correlate with progressive hearing loss in DFNA2
    • Beisel KW, Nelson NC, Delimont DC, et al. Longitudinal gradients of KCNQ4 expression in spiral ganglion and cochlear hair cells correlate with progressive hearing loss in DFNA2. Brain Res Mol Brain Res. 2000; 82: 137-49.
    • (2000) Brain Res Mol Brain Res , vol.82 , pp. 137-149
    • Beisel, K.W.1    Nelson, N.C.2    Delimont, D.C.3
  • 5
    • 27144540987 scopus 로고    scopus 로고
    • Differential expression of KCNQ4 in inner hair cells and sensory neurons is the basis of progressive high-frequency hearing loss
    • Beisel KW, Rocha-Sanchez SM, Morris KA, et al. Differential expression of KCNQ4 in inner hair cells and sensory neurons is the basis of progressive high-frequency hearing loss. J Neurosci. 2005; 25: 9285-93.
    • (2005) J Neurosci , vol.25 , pp. 9285-9293
    • Beisel, K.W.1    Rocha-Sanchez, S.M.2    Morris, K.A.3
  • 6
    • 0034636056 scopus 로고    scopus 로고
    • KCNQ4, a K+ channel mutated in a form of dominant deafness, is expressed in the inner ear and the central auditory pathway
    • Kharkovets T, Hardelin JP, Safieddine S, et al. KCNQ4, a K+ channel mutated in a form of dominant deafness, is expressed in the inner ear and the central auditory pathway. Proc Natl Acad Sci USA. 2000; 97: 4333-8.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4333-4338
    • Kharkovets, T.1    Hardelin, J.P.2    Safieddine, S.3
  • 7
    • 0033524936 scopus 로고    scopus 로고
    • KCNQ4, a novel potassium channel expressed in sensory outer hair cells, is mutated in dominant deafness
    • Kubisch C, Schroeder BC, Friedrich T, et al. KCNQ4, a novel potassium channel expressed in sensory outer hair cells, is mutated in dominant deafness. Cell. 1999; 96: 437-46.
    • (1999) Cell , vol.96 , pp. 437-446
    • Kubisch, C.1    Schroeder, B.C.2    Friedrich, T.3
  • 8
    • 34548090747 scopus 로고    scopus 로고
    • Dominant-negative inhibition of M-like potassium conductances in hair cells of the mouse inner ear
    • Holt JR, Stauffer EA, Abraham D, et al. Dominant-negative inhibition of M-like potassium conductances in hair cells of the mouse inner ear. J Neurosci. 2007; 27: 8940-51.
    • (2007) J Neurosci , vol.27 , pp. 8940-8951
    • Holt, J.R.1    Stauffer, E.A.2    Abraham, D.3
  • 9
    • 0038684768 scopus 로고    scopus 로고
    • Degeneration of sensory outer hair cells following pharmacological blockade of cochlear KCNQ channels in the adult guinea pig
    • Nouvian R, Ruel J, Wang J, et al. Degeneration of sensory outer hair cells following pharmacological blockade of cochlear KCNQ channels in the adult guinea pig. Eur J Neurosci. 2003; 17: 2553-62.
    • (2003) Eur J Neurosci , vol.17 , pp. 2553-2562
    • Nouvian, R.1    Ruel, J.2    Wang, J.3
  • 10
    • 0037444439 scopus 로고    scopus 로고
    • Resting potential and submembrane calcium concentration of inner hair cells in the isolated mouse cochlea are set by KCNQ-type potassium channels
    • Oliver D, Knipper M, Derst C, et al. Resting potential and submembrane calcium concentration of inner hair cells in the isolated mouse cochlea are set by KCNQ-type potassium channels. J Neurosci. 2003; 23: 2141-9.
    • (2003) J Neurosci , vol.23 , pp. 2141-2149
    • Oliver, D.1    Knipper, M.2    Derst, C.3
  • 11
    • 33748910482 scopus 로고    scopus 로고
    • Supporting sensory transduction: cochlear fluid homeostasis and the endocochlear potential
    • Wangemann P. Supporting sensory transduction: cochlear fluid homeostasis and the endocochlear potential. J Physiol. 2006; 576: 11-21.
    • (2006) J Physiol , vol.576 , pp. 11-21
    • Wangemann, P.1
  • 12
    • 70349916044 scopus 로고    scopus 로고
    • Potassium ion movement in the inner ear: insights from genetic disease and mouse models
    • Zdebik AA, Wangemann P, Jentsch TJ. Potassium ion movement in the inner ear: insights from genetic disease and mouse models. Physiology. 2009; 24: 307-16.
    • (2009) Physiology , vol.24 , pp. 307-316
    • Zdebik, A.A.1    Wangemann, P.2    Jentsch, T.J.3
  • 13
    • 32544435803 scopus 로고    scopus 로고
    • Mice with altered KCNQ4 K+ channels implicate sensory outer hair cells in human progressive deafness
    • Kharkovets T, Dedek K, Maier H, et al. Mice with altered KCNQ4 K+ channels implicate sensory outer hair cells in human progressive deafness. EMBO J. 2006; 25: 642-52.
    • (2006) EMBO J , vol.25 , pp. 642-652
    • Kharkovets, T.1    Dedek, K.2    Maier, H.3
  • 14
    • 84862001682 scopus 로고
    • DFNA2 Nonsyndromic Hearing Loss
    • Pagon RA, Bird TD, Dolan CR, Stephens K, Adam MP, editors. Seattle, WA: University of Washington;
    • Smith RJH, Hildebrand M. DFNA2 Nonsyndromic Hearing Loss. In: Pagon RA, Bird TD, Dolan CR, Stephens K, Adam MP, editors. GeneReviews. Seattle, WA: University of Washington; 1993.
    • (1993) GeneReviews
    • Smith, R.J.H.1    Hildebrand, M.2
  • 15
    • 0032810047 scopus 로고    scopus 로고
    • Mutations in the KCNQ4 gene are responsible for autosomal dominant deafness in four DFNA2 families
    • Coucke PJ, Van Hauwe P, Kelley PM, et al. Mutations in the KCNQ4 gene are responsible for autosomal dominant deafness in four DFNA2 families. Hum Mol Genet. 1999; 8: 1321-8.
    • (1999) Hum Mol Genet , vol.8 , pp. 1321-1328
    • Coucke, P.J.1    Van Hauwe, P.2    Kelley, P.M.3
  • 16
    • 0036123214 scopus 로고    scopus 로고
    • Longitudinal and cross-sectional phenotype analysis in a new, large Dutch DFNA2/KCNQ4 family
    • De Leenheer EM, Huygen PL, Coucke PJ, et al. Longitudinal and cross-sectional phenotype analysis in a new, large Dutch DFNA2/KCNQ4 family. Ann Otol Rhinol Laryngol. 2002; 111: 267-74.
    • (2002) Ann Otol Rhinol Laryngol , vol.111 , pp. 267-274
    • De Leenheer, E.M.1    Huygen, P.L.2    Coucke, P.J.3
  • 17
    • 0036438148 scopus 로고    scopus 로고
    • Audiologic evidence for further genetic heterogeneity at DFNA2
    • Stern RE, Lalwani AK. Audiologic evidence for further genetic heterogeneity at DFNA2. Acta Otolaryngol. 2002; 122: 730-5.
    • (2002) Acta Otolaryngol , vol.122 , pp. 730-735
    • Stern, R.E.1    Lalwani, A.K.2
  • 18
    • 79953874274 scopus 로고    scopus 로고
    • Audioprofile-directed successful mutation analysis in a DFNA2/KCNQ4 (p.Leu274His) family
    • de Heer AM, Schraders M, Oostrik J, et al. Audioprofile-directed successful mutation analysis in a DFNA2/KCNQ4 (p.Leu274His) family. Ann Otol Rhinol Laryngol. 2011; 120: 243-8.
    • (2011) Ann Otol Rhinol Laryngol , vol.120 , pp. 243-248
    • de Heer, A.M.1    Schraders, M.2    Oostrik, J.3
  • 19
    • 79951681986 scopus 로고    scopus 로고
    • Pathogenic effects of a novel mutation (c.664_681del) in KCNQ4 channels associated with auditory pathology
    • Baek JI, Park HJ, Park K, et al. Pathogenic effects of a novel mutation (c.664_681del) in KCNQ4 channels associated with auditory pathology. Biochim Biophys Acta. 2011; 1812: 536-43.
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 536-543
    • Baek, J.I.1    Park, H.J.2    Park, K.3
  • 20
    • 78751681805 scopus 로고    scopus 로고
    • Autosomal dominant progressive sensorineural hearing loss due to a novel mutation in the KCNQ4 gene
    • Arnett J, Emery SB, Kim TB, et al. Autosomal dominant progressive sensorineural hearing loss due to a novel mutation in the KCNQ4 gene. Arch Otolaryngol Head Neck Surg. 2011; 137: 54-9.
    • (2011) Arch Otolaryngol Head Neck Surg , vol.137 , pp. 54-59
    • Arnett, J.1    Emery, S.B.2    Kim, T.B.3
  • 21
    • 57449102040 scopus 로고    scopus 로고
    • Audioprofile-directed screening identifies novel mutations in KCNQ4 causing hearing loss at the DFNA2 locus
    • Hildebrand MS, Tack D, McMordie SJ, et al. Audioprofile-directed screening identifies novel mutations in KCNQ4 causing hearing loss at the DFNA2 locus. Genet Med. 2008; 10: 797-804.
    • (2008) Genet Med , vol.10 , pp. 797-804
    • Hildebrand, M.S.1    Tack, D.2    McMordie, S.J.3
  • 22
    • 33845715168 scopus 로고    scopus 로고
    • Identification of novel mutations in the KCNQ4 gene of patients with nonsyndromic deafness from Taiwan
    • Su CC, Yang JJ, Shieh JC, et al. Identification of novel mutations in the KCNQ4 gene of patients with nonsyndromic deafness from Taiwan. Audiol Neurootol. 2007; 12: 20-6.
    • (2007) Audiol Neurootol , vol.12 , pp. 20-26
    • Su, C.C.1    Yang, J.J.2    Shieh, J.C.3
  • 23
    • 33745005751 scopus 로고    scopus 로고
    • A novel KCNQ4 one-base deletion in a large pedigree with hearing loss: implication for the genotype-phenotype correlation
    • Kamada F, Kure S, Kudo T, et al. A novel KCNQ4 one-base deletion in a large pedigree with hearing loss: implication for the genotype-phenotype correlation. J Hum Genet. 2006; 51: 455-60.
    • (2006) J Hum Genet , vol.51 , pp. 455-460
    • Kamada, F.1    Kure, S.2    Kudo, T.3
  • 24
    • 12344264009 scopus 로고    scopus 로고
    • Phenotype determination guides swift genotyping of a DFNA2/KCNQ4 family with a hot spot mutation (W276S)
    • Topsakal V, Pennings RJ, te Brinke H, et al. Phenotype determination guides swift genotyping of a DFNA2/KCNQ4 family with a hot spot mutation (W276S). Otol Neurotol. 2005; 26: 52-8.
    • (2005) Otol Neurotol , vol.26 , pp. 52-58
    • Topsakal, V.1    Pennings, R.J.2    te Brinke, H.3
  • 25
    • 0036304870 scopus 로고    scopus 로고
    • A mutational hot spot in the KCNQ4 gene responsible for autosomal dominant hearing impairment
    • Van Camp G, Coucke PJ, Akita J, et al. A mutational hot spot in the KCNQ4 gene responsible for autosomal dominant hearing impairment. Hum Mutat. 2002; 20: 15-9.
    • (2002) Hum Mutat , vol.20 , pp. 15-19
    • Van Camp, G.1    Coucke, P.J.2    Akita, J.3
  • 26
    • 0034937052 scopus 로고    scopus 로고
    • Clinical and genetic features of nonsyndromic autosomal dominant sensorineural hearing loss: KCNQ4 is a gene responsible in Japanese
    • Akita J, Abe S, Shinkawa H, et al. Clinical and genetic features of nonsyndromic autosomal dominant sensorineural hearing loss: KCNQ4 is a gene responsible in Japanese. J Hum Genet. 2001; 46: 355-61.
    • (2001) J Hum Genet , vol.46 , pp. 355-361
    • Akita, J.1    Abe, S.2    Shinkawa, H.3
  • 27
    • 0034640646 scopus 로고    scopus 로고
    • Mutations in the KCNQ4 K+ channel gene, responsible for autosomal dominant hearing loss, cluster in the channel pore region
    • Van Hauwe P, Coucke PJ, Ensink RJ, et al. Mutations in the KCNQ4 K+ channel gene, responsible for autosomal dominant hearing loss, cluster in the channel pore region. Am J Med Genet. 2000; 93: 184-7.
    • (2000) Am J Med Genet , vol.93 , pp. 184-187
    • Van Hauwe, P.1    Coucke, P.J.2    Ensink, R.J.3
  • 28
    • 0032794410 scopus 로고    scopus 로고
    • Novel mutation in the KCNQ4 gene in a large kindred with dominant progressive hearing loss
    • Talebizadeh Z, Kelley PM, Askew JW, et al. Novel mutation in the KCNQ4 gene in a large kindred with dominant progressive hearing loss. Hum Mutat. 1999; 14: 493-501.
    • (1999) Hum Mutat , vol.14 , pp. 493-501
    • Talebizadeh, Z.1    Kelley, P.M.2    Askew, J.W.3
  • 29
    • 38949121742 scopus 로고    scopus 로고
    • A novel KCNQ4 pore-region mutation (p.G296S) causes deafness by impairing cell-surface channel expression
    • Mencia A, Gonzalez-Nieto D, Modamio-Hoybjor S, et al. A novel KCNQ4 pore-region mutation (p.G296S) causes deafness by impairing cell-surface channel expression. Hum Genet. 2008; 123: 41-53.
    • (2008) Hum Genet , vol.123 , pp. 41-53
    • Mencia, A.1    Gonzalez-Nieto, D.2    Modamio-Hoybjor, S.3
  • 30
    • 84858125876 scopus 로고    scopus 로고
    • In silico modeling of the pore region of a KCNQ4 missense mutant from a patient with hearing loss
    • Namba K, Mutai H, Kaneko H, et al. In silico modeling of the pore region of a KCNQ4 missense mutant from a patient with hearing loss. BMC Res Notes. 2012; 5: 145.
    • (2012) BMC Res Notes , vol.5 , pp. 145
    • Namba, K.1    Mutai, H.2    Kaneko, H.3
  • 31
    • 58149357419 scopus 로고    scopus 로고
    • KCNQ4 mutations associated with nonsyndromic progressive sensorineural hearing loss
    • Nie L. KCNQ4 mutations associated with nonsyndromic progressive sensorineural hearing loss. Curr Opin Otolaryngol Head Neck Surg. 2008; 16: 441-4.
    • (2008) Curr Opin Otolaryngol Head Neck Surg , vol.16 , pp. 441-444
    • Nie, L.1
  • 32
    • 78651402896 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of autosomal dominant form of progressive hearing loss, DFNA2
    • Kim HJ, Lv P, Sihn CR, et al. Cellular and molecular mechanisms of autosomal dominant form of progressive hearing loss, DFNA2. J Biol Chem. 2011; 286: 1517-27.
    • (2011) J Biol Chem , vol.286 , pp. 1517-1527
    • Kim, H.J.1    Lv, P.2    Sihn, C.R.3
  • 33
    • 84858197815 scopus 로고    scopus 로고
    • Restoration of ion channel function in deafness-causing KCNQ4 mutants by synthetic channel openers
    • Leitner MG, Feuer A, Ebers O, et al. Restoration of ion channel function in deafness-causing KCNQ4 mutants by synthetic channel openers. Br J Pharmacol. 2012; 165: 2244-59.
    • (2012) Br J Pharmacol , vol.165 , pp. 2244-2259
    • Leitner, M.G.1    Feuer, A.2    Ebers, O.3
  • 34
    • 84874215357 scopus 로고    scopus 로고
    • Distinct roles of molecular chaperones HSP90alpha and HSP90beta in the biogenesis of KCNQ4 channels
    • Gao Y, Yechikov S, Vazquez AE, et al. Distinct roles of molecular chaperones HSP90alpha and HSP90beta in the biogenesis of KCNQ4 channels. PLoS ONE. 2013; 8: e57282.
    • (2013) PLoS ONE , vol.8
    • Gao, Y.1    Yechikov, S.2    Vazquez, A.E.3
  • 35
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol. 2010; 11: 515-28.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 36
    • 33644817936 scopus 로고    scopus 로고
    • Association between Hsp90 and the ClC-2 chloride channel upregulates channel function
    • Hinzpeter A, Lipecka J, Brouillard F, et al. Association between Hsp90 and the ClC-2 chloride channel upregulates channel function. Am J Physiol Cell Physiol. 2006; 290: C45-56.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Hinzpeter, A.1    Lipecka, J.2    Brouillard, F.3
  • 37
    • 2442464375 scopus 로고    scopus 로고
    • Role of the cytosolic chaperones Hsp70 and Hsp90 in maturation of the cardiac potassium channel HERG
    • Ficker E, Dennis AT, Wang L, et al. Role of the cytosolic chaperones Hsp70 and Hsp90 in maturation of the cardiac potassium channel HERG. Circ Res. 2003; 92: e87-100.
    • (2003) Circ Res , vol.92
    • Ficker, E.1    Dennis, A.T.2    Wang, L.3
  • 38
    • 84862004190 scopus 로고    scopus 로고
    • The hERG channel is dependent upon the Hsp90alpha isoform for maturation and trafficking
    • Peterson LB, Eskew JD, Vielhauer GA, et al. The hERG channel is dependent upon the Hsp90alpha isoform for maturation and trafficking. Mol Pharm. 2012; 9: 1841-6.
    • (2012) Mol Pharm , vol.9 , pp. 1841-1846
    • Peterson, L.B.1    Eskew, J.D.2    Vielhauer, G.A.3
  • 39
    • 77953507086 scopus 로고    scopus 로고
    • Role of Hsp90 in biogenesis of the beta-cell ATP-sensitive potassium channel complex
    • Yan FF, Pratt EB, Chen PC, et al. Role of Hsp90 in biogenesis of the beta-cell ATP-sensitive potassium channel complex. Mol Biol Cell. 2010; 21: 1945-54.
    • (2010) Mol Biol Cell , vol.21 , pp. 1945-1954
    • Yan, F.F.1    Pratt, E.B.2    Chen, P.C.3
  • 40
    • 36749056453 scopus 로고    scopus 로고
    • hERG channel trafficking: novel targets in drug-induced long QT syndrome
    • Dennis A, Wang L, Wan X, et al. hERG channel trafficking: novel targets in drug-induced long QT syndrome. Biochem Soc Trans. 2007; 35: 1060-3.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1060-1063
    • Dennis, A.1    Wang, L.2    Wan, X.3
  • 41
    • 84861705454 scopus 로고    scopus 로고
    • A422T mutation in HERG potassium channel retained in ER is rescurable by pharmacologic or molecular chaperones
    • Guo J, Zhang X, Hu Z, et al. A422T mutation in HERG potassium channel retained in ER is rescurable by pharmacologic or molecular chaperones. Biochem Biophys Res Commun. 2012; 422: 305-10.
    • (2012) Biochem Biophys Res Commun , vol.422 , pp. 305-310
    • Guo, J.1    Zhang, X.2    Hu, Z.3
  • 42
    • 51349113842 scopus 로고    scopus 로고
    • Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epithelia
    • Sun F, Mi Z, Condliffe SB, et al. Chaperone displacement from mutant cystic fibrosis transmembrane conductance regulator restores its function in human airway epithelia. FASEB J. 2008; 22: 3255-63.
    • (2008) FASEB J , vol.22 , pp. 3255-3263
    • Sun, F.1    Mi, Z.2    Condliffe, S.B.3
  • 43
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • Wang X, Venable J, LaPointe P, et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell. 2006; 127: 803-15.
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1    Venable, J.2    LaPointe, P.3
  • 44
    • 59649109803 scopus 로고    scopus 로고
    • Hsp90 inhibitor partially corrects nephrogenic diabetes insipidus in a conditional knock-in mouse model of aquaporin-2 mutation
    • Yang B, Zhao D, Verkman AS. Hsp90 inhibitor partially corrects nephrogenic diabetes insipidus in a conditional knock-in mouse model of aquaporin-2 mutation. FASEB J. 2009; 23: 503-12.
    • (2009) FASEB J , vol.23 , pp. 503-512
    • Yang, B.1    Zhao, D.2    Verkman, A.S.3
  • 45
    • 2142661025 scopus 로고    scopus 로고
    • KCNQ4 channels expressed in mammalian cells: functional characteristics and pharmacology
    • Sogaard R, Ljungstrom T, Pedersen KA, et al. KCNQ4 channels expressed in mammalian cells: functional characteristics and pharmacology. Am J Physiol Cell Physiol. 2001; 280: C859-66.
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Sogaard, R.1    Ljungstrom, T.2    Pedersen, K.A.3
  • 46
    • 0036193888 scopus 로고    scopus 로고
    • Potassium channel ontogeny
    • Deutsch C. Potassium channel ontogeny. Annu Rev Physiol. 2002; 64: 19-46.
    • (2002) Annu Rev Physiol , vol.64 , pp. 19-46
    • Deutsch, C.1
  • 48
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol. 2009; 16: 574-81.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 49
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms
    • Buchberger A, Bukau B, Sommer T. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol Cell. 2010; 40: 238-52.
    • (2010) Mol Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 50
    • 77955049339 scopus 로고    scopus 로고
    • Quality and quantity control at the endoplasmic reticulum
    • Hegde RS, Ploegh HL. Quality and quantity control at the endoplasmic reticulum. Curr Opin Cell Biol. 2010; 22: 437-46.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 437-446
    • Hegde, R.S.1    Ploegh, H.L.2
  • 51
    • 0031962461 scopus 로고    scopus 로고
    • Nonsyndromic autosomal dominant progressive sensorineural hearing loss: audiologic analysis of a pedigree linked to DFNA2
    • Kunst H, Marres H, Huygen P, et al. Nonsyndromic autosomal dominant progressive sensorineural hearing loss: audiologic analysis of a pedigree linked to DFNA2. Laryngoscope. 1998; 108: 74-80.
    • (1998) Laryngoscope , vol.108 , pp. 74-80
    • Kunst, H.1    Marres, H.2    Huygen, P.3
  • 52
    • 0025762715 scopus 로고
    • Determination of the subunit stoichiometry of a voltage-activated potassium channel
    • MacKinnon R. Determination of the subunit stoichiometry of a voltage-activated potassium channel. Nature. 1991; 350: 232-5.
    • (1991) Nature , vol.350 , pp. 232-235
    • MacKinnon, R.1
  • 53
    • 58849142004 scopus 로고    scopus 로고
    • Expression and localization of K channels KCNQ2 and KCNQ3 in the mammalian cochlea
    • Jin Z, Liang GH, Cooper EC, et al. Expression and localization of K channels KCNQ2 and KCNQ3 in the mammalian cochlea. Audiol Neurootol. 2009; 14: 98-105.
    • (2009) Audiol Neurootol , vol.14 , pp. 98-105
    • Jin, Z.1    Liang, G.H.2    Cooper, E.C.3
  • 54
    • 57649187089 scopus 로고    scopus 로고
    • Homomeric and heteromeric assembly of KCNQ (Kv7) K+ channels assayed by total internal reflection fluorescence/fluorescence resonance energy transfer and patch clamp analysis
    • Bal M, Zhang J, Zaika O, et al. Homomeric and heteromeric assembly of KCNQ (Kv7) K+ channels assayed by total internal reflection fluorescence/fluorescence resonance energy transfer and patch clamp analysis. J Biol Chem. 2008; 283: 30668-76.
    • (2008) J Biol Chem , vol.283 , pp. 30668-30676
    • Bal, M.1    Zhang, J.2    Zaika, O.3
  • 55
    • 34548258321 scopus 로고    scopus 로고
    • Roles of alternative splicing in the functional properties of inner ear-specific KCNQ4 channels
    • Xu T, Nie L, Zhang Y, et al. Roles of alternative splicing in the functional properties of inner ear-specific KCNQ4 channels. J Biol Chem. 2007; 282: 23899-909.
    • (2007) J Biol Chem , vol.282 , pp. 23899-23909
    • Xu, T.1    Nie, L.2    Zhang, Y.3
  • 56
    • 33748999299 scopus 로고    scopus 로고
    • KCNQ4: a gene for age-related hearing impairment?
    • Van Eyken E, Van Laer L, Fransen E, et al. KCNQ4: a gene for age-related hearing impairment? Hum Mutat. 2006; 27: 1007-16.
    • (2006) Hum Mutat , vol.27 , pp. 1007-1016
    • Van Eyken, E.1    Van Laer, L.2    Fransen, E.3
  • 57
    • 24944456875 scopus 로고    scopus 로고
    • Protein misfolding, aggregation, and degradation in disease
    • Gregersen N, Bolund L, Bross P. Protein misfolding, aggregation, and degradation in disease. Mol Biotechnol. 2005; 31: 141-50.
    • (2005) Mol Biotechnol , vol.31 , pp. 141-150
    • Gregersen, N.1    Bolund, L.2    Bross, P.3
  • 59
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature. 2011; 475: 324-32.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 60
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • Loo MA, Jensen TJ, Cui L, et al. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J. 1998; 17: 6879-87.
    • (1998) EMBO J , vol.17 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3
  • 61
    • 74249109889 scopus 로고    scopus 로고
    • To fold or not to fold: modulation and consequences of Hsp90 inhibition
    • Peterson LB, Blagg BS. To fold or not to fold: modulation and consequences of Hsp90 inhibition. Future Med Chem. 2009; 1: 267-83.
    • (2009) Future Med Chem , vol.1 , pp. 267-283
    • Peterson, L.B.1    Blagg, B.S.2
  • 62
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch C, Sangster TA, Lindquist S. Hsp90 as a capacitor of phenotypic variation. Nature. 2002; 417: 618-24.
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.