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Volumn 49, Issue 41, 2010, Pages 8937-8943

Role of isoleucine-554 in lithium binding by the Na+/ dicarboxylate cotransporter NaDC1

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING SITES; CARBOXYLATION; CELL MEMBRANES; POSITIVE IONS; SODIUM;

EID: 77957914813     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100600j     Document Type: Article
Times cited : (4)

References (30)
  • 1
    • 0033428109 scopus 로고    scopus 로고
    • A functional phylogenetic system for the classification of transport proteins
    • Saier, M. H. (1999) A functional phylogenetic system for the classification of transport proteins J. Cell Biochem. Suppl. 32-33) 84-94
    • (1999) J. Cell Biochem. Suppl. , Issue.32-33 , pp. 84-94
    • Saier, M.H.1
  • 2
    • 29944444676 scopus 로고    scopus 로고
    • Molecular properties of the SLC13 family of dicarboxylate and sulfate transporters
    • Pajor, A. M. (2006) Molecular properties of the SLC13 family of dicarboxylate and sulfate transporters Pfluegers Arch. 451, 597-605
    • (2006) Pfluegers Arch. , vol.451 , pp. 597-605
    • Pajor, A.M.1
  • 5
    • 0037432531 scopus 로고    scopus 로고
    • Classification of 29 families of secondary transport proteins into a single structural class using hydropathy profile analysis
    • Lolkema, J. S. and Slotboom, D. J. (2003) Classification of 29 families of secondary transport proteins into a single structural class using hydropathy profile analysis J. Mol. Biol. 327, 901-909
    • (2003) J. Mol. Biol. , vol.327 , pp. 901-909
    • Lolkema, J.S.1    Slotboom, D.J.2
  • 12
    • 12344273080 scopus 로고    scopus 로고
    • The "transport specificity ratio": A structure-function tool to search the protein fold for loci that control transition state stability in membrane transport catalysis
    • King, S. C. (2004) The "transport specificity ratio": a structure-function tool to search the protein fold for loci that control transition state stability in membrane transport catalysis BMC Biochem. 5, 16
    • (2004) BMC Biochem. , vol.5 , pp. 16
    • King, S.C.1
  • 15
    • 3242891271 scopus 로고    scopus 로고
    • ConPred II: A consensus prediction method for obtaining transmembrane topology models with high reliability
    • Arai, M., Mitsuke, H., Ikeda, M., Xia, J. X., Kikuchi, T., Satake, M., and Shimizu, T. (2004) ConPred II: a consensus prediction method for obtaining transmembrane topology models with high reliability Nucleic Acids Res. 32, W390-W393
    • (2004) Nucleic Acids Res. , vol.32
    • Arai, M.1    Mitsuke, H.2    Ikeda, M.3    Xia, J.X.4    Kikuchi, T.5    Satake, M.6    Shimizu, T.7
  • 16
    • 0034664957 scopus 로고    scopus 로고
    • Role of cationic amino acids in the Na/dicarboxylate co-transporter, NaDC-1
    • Pajor, A. M., Kahn, E. S., and Gangula, R. (2000) Role of cationic amino acids in the Na/dicarboxylate co-transporter, NaDC-1 Biochem. J. 350, 677-683
    • (2000) Biochem. J. , vol.350 , pp. 677-683
    • Pajor, A.M.1    Kahn, E.S.2    Gangula, R.3
  • 17
    • 0035839457 scopus 로고    scopus 로고
    • +/dicarboxylate cotransporter
    • +/dicarboxylate cotransporter J. Biol. Chem. 276, 29961-29968
    • (2001) J. Biol. Chem. , vol.276 , pp. 29961-29968
    • Pajor, A.M.1
  • 19
    • 0030475519 scopus 로고    scopus 로고
    • +/dicarboxylate cotransporter using anti-fusion protein antibodies
    • +/dicarboxylate cotransporter using anti-fusion protein antibodies Am. J. Physiol. Cell Physiol. 271, C1808-C1816
    • (1996) Am. J. Physiol. Cell Physiol. , vol.271
    • Pajor, A.M.1    Sun, N.2
  • 20
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure-function relationships in polytopic membrane proteins
    • Frillingos, S., Sahin-Toth, M., Wu, J., and Kaback, H. R. (1998) Cys-scanning mutagenesis: a novel approach to structure-function relationships in polytopic membrane proteins FASEB J. 12, 1281-1299
    • (1998) FASEB J. , vol.12 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Toth, M.2    Wu, J.3    Kaback, H.R.4
  • 21
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R., and Iwata, S. (2003) Structure and mechanism of the lactose permease of Escherichia coli Science 301, 610-615
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 22
    • 67649616342 scopus 로고    scopus 로고
    • Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis
    • Mueckler, M. and Makepeace, C. (2009) Model of the exofacial substrate-binding site and helical folding of the human Glut1 glucose transporter based on scanning mutagenesis Biochemistry 48, 5934-5942
    • (2009) Biochemistry , vol.48 , pp. 5934-5942
    • Mueckler, M.1    Makepeace, C.2
  • 23
    • 45549092587 scopus 로고    scopus 로고
    • Transmembrane segment 6 of the Glut1 glucose transporter is an outer helix and contains amino acid side chains essential for transport activity
    • Mueckler, M. and Makepeace, C. (2008) Transmembrane segment 6 of the Glut1 glucose transporter is an outer helix and contains amino acid side chains essential for transport activity J. Biol. Chem. 283, 11550-11555
    • (2008) J. Biol. Chem. , vol.283 , pp. 11550-11555
    • Mueckler, M.1    Makepeace, C.2
  • 25
    • 0020632429 scopus 로고
    • Kinetics of sodium succinate cotransport across renal brush-border membranes
    • Wright, S. H., Hirayama, B., Kaunitz, J. D., Kippen, I., and Wright, E. M. (1983) Kinetics of sodium succinate cotransport across renal brush-border membranes J. Biol. Chem. 258, 5456-5462
    • (1983) J. Biol. Chem. , vol.258 , pp. 5456-5462
    • Wright, S.H.1    Hirayama, B.2    Kaunitz, J.D.3    Kippen, I.4    Wright, E.M.5
  • 26
    • 0003518480 scopus 로고
    • John Wiley and Sons, New York.
    • Segel, I. H. (1975) Enzyme kinetics, John Wiley and Sons, New York.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 27
    • 0042828877 scopus 로고    scopus 로고
    • Human sodium-coupled citrate transporter, the orthologue of Drosophila Indy, as a novel target for lithium action
    • Inoue, K., Zhuang, L., Maddox, D. M., Smith, S. B., and Ganapathy, V. (2003) Human sodium-coupled citrate transporter, the orthologue of Drosophila Indy, as a novel target for lithium action Biochem. J. 374, 21-26
    • (2003) Biochem. J. , vol.374 , pp. 21-26
    • Inoue, K.1    Zhuang, L.2    Maddox, D.M.3    Smith, S.B.4    Ganapathy, V.5
  • 29
    • 0029041792 scopus 로고
    • Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states
    • Grunewald, M. and Kanner, B. (1995) Conformational changes monitored on the glutamate transporter GLT-1 indicate the existence of two neurotransmitter-bound states J. Biol. Chem. 270, 17017-17024
    • (1995) J. Biol. Chem. , vol.270 , pp. 17017-17024
    • Grunewald, M.1    Kanner, B.2
  • 30
    • 33746839659 scopus 로고    scopus 로고
    • Identification of a lithium interaction site in the gamma-aminobutyric acid (GABA) transporter GAT-1
    • Zhou, Y., Zomot, E., and Kanner, B. I. (2006) Identification of a lithium interaction site in the gamma-aminobutyric acid (GABA) transporter GAT-1 J. Biol. Chem. 281, 22092-22099
    • (2006) J. Biol. Chem. , vol.281 , pp. 22092-22099
    • Zhou, Y.1    Zomot, E.2    Kanner, B.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.