메뉴 건너뛰기




Volumn 86, Issue 1 I, 2004, Pages 224-234

Histidines Are Responsible for Zinc Potentiation of the Current in KDC1 Carrot Channels

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CADMIUM; DIMER; HISTIDINE; INWARDLY RECTIFYING POTASSIUM CHANNEL; LEAD; METAL; NICKEL; POTASSIUM CHANNEL; ZINC;

EID: 0346688717     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74098-9     Document Type: Article
Times cited : (18)

References (31)
  • 1
    • 0003646725 scopus 로고
    • MacMillan Publishing Company, Collier MacMillan Publishers, New York, London
    • Brady, N. C. 1984. The Nature and Properties of Soil. Ninth Ed. MacMillan Publishing Company, Collier MacMillan Publishers, New York, London.
    • (1984) The Nature and Properties of Soil. Ninth Ed.
    • Brady, N.C.1
  • 2
    • 0025013362 scopus 로고
    • Geometry of interaction of metal ions with histidines residues in protein
    • Chakrabarti, P. 1990. Geometry of interaction of metal ions with histidines residues in protein. Prot. Eng. 4:57-63.
    • (1990) Prot. Eng. , vol.4 , pp. 57-63
    • Chakrabarti, P.1
  • 3
    • 0033136273 scopus 로고    scopus 로고
    • 2+ inhibition of the NMDA receptor
    • 2+ inhibition of the NMDA receptor. Neuron. 23:171-180.
    • (1999) Neuron , vol.23 , pp. 171-180
    • Choi, Y.B.1    Lipton, S.A.2
  • 4
    • 0026409452 scopus 로고
    • Structural biology of zinc
    • Christianson, D. W. 1991. Structural biology of zinc. Adv. Protein Chem. 42:281-355.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 281-355
    • Christianson, D.W.1
  • 11
    • 0028806749 scopus 로고
    • Inward rectifier potassium channels in plants differ from their animal counterparts in response to voltage and channel modulators
    • Hedrich R., O. Moran, E. Conti, H. Bush, D. Becker, F. Gambale, I. Dreyer, A. Kuch, K. Neuwinger, and K. Palme. 1995. Inward rectifier potassium channels in plants differ from their animal counterparts in response to voltage and channel modulators. Eur. Biophys. J. 24:107-115.
    • (1995) Eur. Biophys. J. , vol.24 , pp. 107-115
    • Hedrich, R.1    Moran, O.2    Conti, E.3    Bush, H.4    Becker, D.5    Gambale, F.6    Dreyer, I.7    Kuch, A.8    Neuwinger, K.9    Palme, K.10
  • 12
    • 0026560616 scopus 로고
    • The aromatic binding site for tetraethylammonium ion on potassium channels
    • Heginbotham, L., and R. MacKinnon. 1992. The aromatic binding site for tetraethylammonium ion on potassium channels. Neuron. 8:483-491.
    • (1992) Neuron , vol.8 , pp. 483-491
    • Heginbotham, L.1    MacKinnon, R.2
  • 14
    • 0032720838 scopus 로고    scopus 로고
    • 2+ requires histidine residues in the S3-S4 linker and in the channel pore
    • 2+ requires histidine residues in the S3-S4 linker and in the channel pore. Planta. 209:543-546.
    • (1999) Planta , vol.209 , pp. 543-546
    • Hoth, S.1    Hedrich, R.2
  • 18
    • 0032051941 scopus 로고    scopus 로고
    • The genetic effects of environmental lead
    • Johnson, F. M. 1998. The genetic effects of environmental lead. Mutat. Res. 410:123-140.
    • (1998) Mutat. Res. , vol.410 , pp. 123-140
    • Johnson, F.M.1
  • 19
    • 0026485457 scopus 로고
    • + channel determined by construction of multimeric cDNAs
    • + channel determined by construction of multimeric cDNAs. Neuron. 9:861-871.
    • (1992) Neuron , vol.9 , pp. 861-871
    • Liman, E.R.1    Tytgat, J.2    Hess, P.3
  • 20
    • 0033120016 scopus 로고    scopus 로고
    • Structure/function relationships in nickel metallobiochemistry
    • Maroney, M. J. 1999. Structure/function relationships in nickel metallobiochemistry. Curr. Opin. Chem. Biol. 3:188-199.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 188-199
    • Maroney, M.J.1
  • 22
    • 0005406274 scopus 로고    scopus 로고
    • Assembly of Shaker K-channels from random mixture of subunits carrying different mutations
    • R. Latorre and J. C. Sáez, editors. Plenum Press, New York and London
    • Naranjo, D. 1997. Assembly of Shaker K-channels from random mixture of subunits carrying different mutations. In From Ion Channel to Cell-to-Cell Conversation. R. Latorre and J. C. Sáez, editors. Plenum Press, New York and London. 35-65.
    • (1997) From Ion Channel to Cell-to-Cell Conversation , pp. 35-65
    • Naranjo, D.1
  • 24
    • 0023160262 scopus 로고    scopus 로고
    • Lead in ancient human bones and its relevance to historical developments of social problems with lead
    • Patterson, C. C., H. Shirahata, and J. E. Ericson. 1998. Lead in ancient human bones and its relevance to historical developments of social problems with lead. Sci. Tot. Environ. 61:167-200.
    • (1998) Sci. Tot. Environ. , vol.61 , pp. 167-200
    • Patterson, C.C.1    Shirahata, H.2    Ericson, J.E.3
  • 27
    • 0027099840 scopus 로고
    • Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA
    • Schachtman, D. P., J. I. Schroeder, W. J. Lucas, J. A. Anderson, and R. F. Gaber. 1992. Expression of an inward-rectifying potassium channel by the Arabidopsis KAT1 cDNA. Science. 258:1654-1658.
    • (1992) Science , vol.258 , pp. 1654-1658
    • Schachtman, D.P.1    Schroeder, J.I.2    Lucas, W.J.3    Anderson, J.A.4    Gaber, R.F.5
  • 28
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee. B. L., and K. H. Falchuck. 1993. The biochemical basis of zinc physiology. Physiol. Rev. 73:79-118.
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuck, K.H.2
  • 29
    • 0028025197 scopus 로고
    • Level of expression in Xenopus oocytes affects some characteristics of a plant inward-rectifying voltage-gated K+ channel
    • Véry, A. A., C. Bosseux, F. Gaymard, H. Sentenac, and J. B. Thibaud. 1994. Level of expression in Xenopus oocytes affects some characteristics of a plant inward-rectifying voltage-gated K+ channel. Pflugers Arch. 428:422-424.
    • (1994) Pflugers Arch. , vol.428 , pp. 422-424
    • Véry, A.A.1    Bosseux, C.2    Gaymard, F.3    Sentenac, H.4    Thibaud, J.B.5
  • 30
    • 0028883463 scopus 로고
    • A single histidine residue is essential for zinc inhibition of GABAr1 receptor
    • Wang, T. L., A. Hackam, W. B. Guggino, and G. R. Cutting. 1995. A single histidine residue is essential for zinc inhibition of GABAr1 receptor. J. Neurosc. 15:7684-7691.
    • (1995) J. Neurosc. , vol.15 , pp. 7684-7691
    • Wang, T.L.1    Hackam, A.2    Guggino, W.B.3    Cutting, G.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.