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Volumn 5, Issue 4, 2008, Pages 553-561

Erratum (DOI:10.1016/j.hrthm.2008.01.020);Recurrent intrauterine fetal loss due to near absence of HERG: Clinical and functional characterization of a homozygous nonsense HERG Q1070X mutation

Author keywords

Electrophysiology; HERG; Long QT syndrome; Nonsense mediated decay; Sudden cardiac death

Indexed keywords

ION CHANNEL; POTASSIUM CHANNEL HERG;

EID: 40849097481     PISSN: 15475271     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.hrthm.2008.03.033     Document Type: Erratum
Times cited : (54)

References (29)
  • 1
    • 33748055152 scopus 로고    scopus 로고
    • Prevalence of the long QT syndrome
    • (abstr)
    • Crotti L., Stramba-Badiale M., Pedrazzini M., et al. Prevalence of the long QT syndrome. (abstr). Circulation 112 Suppl II (2005) 3097
    • (2005) Circulation , vol.112 , Issue.SUPPL. II , pp. 3097
    • Crotti, L.1    Stramba-Badiale, M.2    Pedrazzini, M.3
  • 2
    • 25144503454 scopus 로고    scopus 로고
    • Genetics of cardiac arrhythmias
    • Wilde A.A., and Bezzina C.R. Genetics of cardiac arrhythmias. Heart 91 (2005) 1352-1358
    • (2005) Heart , vol.91 , pp. 1352-1358
    • Wilde, A.A.1    Bezzina, C.R.2
  • 3
    • 0028914969 scopus 로고
    • A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome
    • Curran M.E., Splawski I., Timothy K.W., et al. A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome. Cell 80 (1995) 795-803
    • (1995) Cell , vol.80 , pp. 795-803
    • Curran, M.E.1    Splawski, I.2    Timothy, K.W.3
  • 4
    • 0029925480 scopus 로고    scopus 로고
    • Spectrum of HERG K+-channel dysfunction in an inherited cardiac arrhythmia
    • Sanguinetti M.C., Curran M.E., Spector P.S., et al. Spectrum of HERG K+-channel dysfunction in an inherited cardiac arrhythmia. Proc Natl Acad Sci U S A 93 (1996) 2208-2212
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 2208-2212
    • Sanguinetti, M.C.1    Curran, M.E.2    Spector, P.S.3
  • 5
    • 7244226352 scopus 로고    scopus 로고
    • Kr channels minimally comprise hERG 1a and 1b subunits
    • Kr channels minimally comprise hERG 1a and 1b subunits. J Biol Chem 279 (2004) 44690-44694
    • (2004) J Biol Chem , vol.279 , pp. 44690-44694
    • Jones, E.M.1    Roti Roti, E.C.2    Wang, J.3
  • 6
    • 0032825605 scopus 로고    scopus 로고
    • A plethora of mechanisms in the HERG-related long-QT syndrome: genetics meets electrophysiology
    • Roden D.M., and Balser J.R. A plethora of mechanisms in the HERG-related long-QT syndrome: genetics meets electrophysiology. Cardiovasc Res 44 (1999) 242-246
    • (1999) Cardiovasc Res , vol.44 , pp. 242-246
    • Roden, D.M.1    Balser, J.R.2
  • 7
    • 33644851751 scopus 로고    scopus 로고
    • Most LQT2 mutations reduce Kv11.1 (hERG) current by a class 2 (trafficking-deficient) mechanism
    • Anderson C.L., Delisle B.P., Anson B.D., et al. Most LQT2 mutations reduce Kv11.1 (hERG) current by a class 2 (trafficking-deficient) mechanism. Circulation 113 (2006) 365-373
    • (2006) Circulation , vol.113 , pp. 365-373
    • Anderson, C.L.1    Delisle, B.P.2    Anson, B.D.3
  • 8
    • 34347332362 scopus 로고    scopus 로고
    • Nonsense mutations in hERG cause a decrease in mutant mRNA transcripts by nonsense-mediated mRNA decay in human long QT syndrome
    • Gong Q., Zhang L., Vincent G.M., et al. Nonsense mutations in hERG cause a decrease in mutant mRNA transcripts by nonsense-mediated mRNA decay in human long QT syndrome. Circulation 116 (2007) 17-24
    • (2007) Circulation , vol.116 , pp. 17-24
    • Gong, Q.1    Zhang, L.2    Vincent, G.M.3
  • 9
    • 17144442716 scopus 로고    scopus 로고
    • Homozygosity for a HERG potassium channel mutation causes a severe form of long QT syndrome: identification of an apparent founder mutation in the Finns
    • Piippo K., Laitinen P., Swan H., et al. Homozygosity for a HERG potassium channel mutation causes a severe form of long QT syndrome: identification of an apparent founder mutation in the Finns. J Am Coll Cardiol 35 (2000) 1919-1925
    • (2000) J Am Coll Cardiol , vol.35 , pp. 1919-1925
    • Piippo, K.1    Laitinen, P.2    Swan, H.3
  • 10
    • 0242515866 scopus 로고    scopus 로고
    • Clinical, genetic, and biophysical characterization of a homozygous HERG mutation causing severe neonatal long QT syndrome
    • Johnson Jr. W.H., Yang P., Yang T., et al. Clinical, genetic, and biophysical characterization of a homozygous HERG mutation causing severe neonatal long QT syndrome. Pediatr Res 53 (2003) 744-748
    • (2003) Pediatr Res , vol.53 , pp. 744-748
    • Johnson Jr., W.H.1    Yang, P.2    Yang, T.3
  • 11
    • 0033592362 scopus 로고    scopus 로고
    • Homozygous premature truncation of the HERG protein: the human HERG knockout
    • Hoorntje T., Alders M., van Tintelen P., et al. Homozygous premature truncation of the HERG protein: the human HERG knockout. Circulation 100 (1999) 1264-1267
    • (1999) Circulation , vol.100 , pp. 1264-1267
    • Hoorntje, T.1    Alders, M.2    van Tintelen, P.3
  • 12
    • 0031948260 scopus 로고    scopus 로고
    • Genomic organization and mutational analysis of HERG, a gene responsible for familial long QT syndrome
    • Itoh T., Tanaka T., Nagai R., et al. Genomic organization and mutational analysis of HERG, a gene responsible for familial long QT syndrome. Hum Genet 102 (1998) 435-439
    • (1998) Hum Genet , vol.102 , pp. 435-439
    • Itoh, T.1    Tanaka, T.2    Nagai, R.3
  • 13
    • 0031437964 scopus 로고    scopus 로고
    • Suppression of neuronal and cardiac transient outward currents by viral gene transfer of dominant-negative Kv4.2 constructs
    • Johns D.C., Nuss H.B., and Marbán E. Suppression of neuronal and cardiac transient outward currents by viral gene transfer of dominant-negative Kv4.2 constructs. J Biol Chem 272 (1997) 31598-31603
    • (1997) J Biol Chem , vol.272 , pp. 31598-31603
    • Johns, D.C.1    Nuss, H.B.2    Marbán, E.3
  • 14
    • 33749001960 scopus 로고    scopus 로고
    • C-terminal HERG (LQT2) mutations disrupt IKr channel regulation through 14-3-3epsilon
    • Choe C.U., Schulze-Bahr E., Neu A., et al. C-terminal HERG (LQT2) mutations disrupt IKr channel regulation through 14-3-3epsilon. Hum Mol Genet 15 (2006) 2888-2902
    • (2006) Hum Mol Genet , vol.15 , pp. 2888-2902
    • Choe, C.U.1    Schulze-Bahr, E.2    Neu, A.3
  • 15
    • 0037090803 scopus 로고    scopus 로고
    • 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity
    • Kagan A., Melman Y.F., Krumerman A., et al. 14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity. EMBO J 21 (2002) 1889-1898
    • (2002) EMBO J , vol.21 , pp. 1889-1898
    • Kagan, A.1    Melman, Y.F.2    Krumerman, A.3
  • 16
    • 27644573433 scopus 로고    scopus 로고
    • Role of sequence variations in the human ether-a-go-go-related gene (HERG, KCNH2) in the Brugada syndrome
    • Verkerk A.O., Wilders R., Schulze-Bahr E., et al. Role of sequence variations in the human ether-a-go-go-related gene (HERG, KCNH2) in the Brugada syndrome. Cardiovasc Res 68 (2005) 441-453
    • (2005) Cardiovasc Res , vol.68 , pp. 441-453
    • Verkerk, A.O.1    Wilders, R.2    Schulze-Bahr, E.3
  • 17
    • 9644290757 scopus 로고    scopus 로고
    • Defective assembly and trafficking of mutant HERG channels with C-terminal truncations in long QT syndrome
    • Gong Q., Keeney D.R., Robinson J.C., et al. Defective assembly and trafficking of mutant HERG channels with C-terminal truncations in long QT syndrome. J Mol Cell Cardiol 37 (2004) 1225-1233
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 1225-1233
    • Gong, Q.1    Keeney, D.R.2    Robinson, J.C.3
  • 18
    • 0032516934 scopus 로고    scopus 로고
    • HERG channel dysfunction in human long QT syndrome: intracellular transport and functional defects
    • Zhou Z., Gong Q., Epstein M.L., et al. HERG channel dysfunction in human long QT syndrome: intracellular transport and functional defects. J Biol Chem 273 (1998) 21061-21066
    • (1998) J Biol Chem , vol.273 , pp. 21061-21066
    • Zhou, Z.1    Gong, Q.2    Epstein, M.L.3
  • 19
    • 0033600758 scopus 로고    scopus 로고
    • Deletion of protein kinase A phosphorylation sites in the HERG potassium channel inhibits activation shift by protein kinase A
    • Thomas D., Zhang W., Karle C.A., et al. Deletion of protein kinase A phosphorylation sites in the HERG potassium channel inhibits activation shift by protein kinase A. J Biol Chem 274 (2005) 27457-27462
    • (2005) J Biol Chem , vol.274 , pp. 27457-27462
    • Thomas, D.1    Zhang, W.2    Karle, C.A.3
  • 20
    • 0032837376 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in health and disease
    • Frischmeyer P.A., and Dietz H.C. Nonsense-mediated mRNA decay in health and disease. Hum Mol Genet 8 (1999) 1893-1900
    • (1999) Hum Mol Genet , vol.8 , pp. 1893-1900
    • Frischmeyer, P.A.1    Dietz, H.C.2
  • 21
    • 3542995089 scopus 로고    scopus 로고
    • Nonsense-mediated decay approaches the clinic
    • Holbrook J.A., Neu-Yilik G., Hentze M.W., et al. Nonsense-mediated decay approaches the clinic. Nat Genet 36 (2004) 801-808
    • (2004) Nat Genet , vol.36 , pp. 801-808
    • Holbrook, J.A.1    Neu-Yilik, G.2    Hentze, M.W.3
  • 22
    • 0032104190 scopus 로고    scopus 로고
    • A rule for termination-codon position within intron-containing genes: when nonsense affects RNA abundance
    • Nagy E., and Maquat L.E. A rule for termination-codon position within intron-containing genes: when nonsense affects RNA abundance. Trends Biochem Sci 23 (1998) 198-199
    • (1998) Trends Biochem Sci , vol.23 , pp. 198-199
    • Nagy, E.1    Maquat, L.E.2
  • 23
    • 1642406757 scopus 로고    scopus 로고
    • Expression and role of the ether-a-go-go-related (MERG1A) potassium-channel protein during preimplantation mouse development
    • Winston N.J., Johnson M.H., McConnell J.M., et al. Expression and role of the ether-a-go-go-related (MERG1A) potassium-channel protein during preimplantation mouse development. Biol Reprod 70 (2004) 1070-1079
    • (2004) Biol Reprod , vol.70 , pp. 1070-1079
    • Winston, N.J.1    Johnson, M.H.2    McConnell, J.M.3
  • 24
    • 0037371841 scopus 로고    scopus 로고
    • Selective knockout of mouse ERG1 B potassium channel eliminates I(Kr) in adult ventricular myocytes and elicits episodes of abrupt sinus bradycardia
    • Lees-Miller J.P., Guo J., Somers J.R., et al. Selective knockout of mouse ERG1 B potassium channel eliminates I(Kr) in adult ventricular myocytes and elicits episodes of abrupt sinus bradycardia. Mol Cell Biol 23 (2003) 1856-1862
    • (2003) Mol Cell Biol , vol.23 , pp. 1856-1862
    • Lees-Miller, J.P.1    Guo, J.2    Somers, J.R.3
  • 25
    • 0037453021 scopus 로고    scopus 로고
    • Drugs that induce repolarization abnormalities cause bradycardia in zebrafish
    • Milan D.J., Peterson T.A., Ruskin J.N., et al. Drugs that induce repolarization abnormalities cause bradycardia in zebrafish. Circulation 107 (2003) 1355-1358
    • (2003) Circulation , vol.107 , pp. 1355-1358
    • Milan, D.J.1    Peterson, T.A.2    Ruskin, J.N.3
  • 26
    • 0034739399 scopus 로고    scopus 로고
    • A knockout may not always be a knockout
    • (letter)
    • London B. A knockout may not always be a knockout. (letter). Circulation 102 (2000) E122
    • (2000) Circulation , vol.102
    • London, B.1
  • 27
    • 33847360602 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay affects nonsense transcript levels and governs response of cystic fibrosis patients to gentamicin
    • Linde L., Boelz S., Nissim-Rafinia M., et al. Nonsense-mediated mRNA decay affects nonsense transcript levels and governs response of cystic fibrosis patients to gentamicin. J Clin Invest 117 (2007) 683-692
    • (2007) J Clin Invest , vol.117 , pp. 683-692
    • Linde, L.1    Boelz, S.2    Nissim-Rafinia, M.3
  • 28
    • 23944526782 scopus 로고    scopus 로고
    • A novel approach to identify Duchenne muscular dystrophy patients for aminoglycoside antibiotics therapy
    • Kimura S., Ito K., Miyagi T., et al. A novel approach to identify Duchenne muscular dystrophy patients for aminoglycoside antibiotics therapy. Brain Dev 27 (2005) 400-405
    • (2005) Brain Dev , vol.27 , pp. 400-405
    • Kimura, S.1    Ito, K.2    Miyagi, T.3
  • 29
    • 2442527864 scopus 로고    scopus 로고
    • Aminoglycoside-mediated rescue of a disease-causing nonsense mutation in the V2 vasopressin receptor gene in vitro and in vivo
    • Sangkuhl K., Schulz A., Rompler H., et al. Aminoglycoside-mediated rescue of a disease-causing nonsense mutation in the V2 vasopressin receptor gene in vitro and in vivo. Hum Mol Genet 13 (2004) 893-903
    • (2004) Hum Mol Genet , vol.13 , pp. 893-903
    • Sangkuhl, K.1    Schulz, A.2    Rompler, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.