메뉴 건너뛰기




Volumn 1757, Issue 9-10, 2006, Pages 1237-1248

The conserved substrate binding site of mitochondrial carriers

Author keywords

Bioinformatics; Mitochondrial carrier; Structure; Substrate binding; Transporter

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID; CARRIER PROTEIN; NUCLEOTIDE; OXOACID;

EID: 33748964653     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.03.021     Document Type: Article
Times cited : (125)

References (62)
  • 1
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): physiological and pathological implications
    • Palmieri F. The mitochondrial transporter family (SLC25): physiological and pathological implications. Pflugers Arch. 447 (2004) 689-709
    • (2004) Pflugers Arch. , vol.447 , pp. 689-709
    • Palmieri, F.1
  • 2
    • 1942468196 scopus 로고    scopus 로고
    • The role and structure of mitochondrial carriers
    • Kunji E.R. The role and structure of mitochondrial carriers. FEBS Lett. 564 (2004) 239-244
    • (2004) FEBS Lett. , vol.564 , pp. 239-244
    • Kunji, E.R.1
  • 3
    • 0020106115 scopus 로고
    • Complete amino acid sequence of the ADP/ATP carrier from beef heart mitochondria
    • Aquila H., Misra D., Eulitz M., and Klingenberg M. Complete amino acid sequence of the ADP/ATP carrier from beef heart mitochondria. Hoppe-Seyler Z. Physiol. Chem. 363 (1982) 345-349
    • (1982) Hoppe-Seyler Z. Physiol. Chem. , vol.363 , pp. 345-349
    • Aquila, H.1    Misra, D.2    Eulitz, M.3    Klingenberg, M.4
  • 4
    • 0024492693 scopus 로고
    • Two bovine genes for mitochondrial ADP/ATP translocase expressed differences in various tissues
    • Powell S.J., Medd S.M., Runswick M.J., and Walker J.E. Two bovine genes for mitochondrial ADP/ATP translocase expressed differences in various tissues. Biochemistry 28 (1989) 866-873
    • (1989) Biochemistry , vol.28 , pp. 866-873
    • Powell, S.J.1    Medd, S.M.2    Runswick, M.J.3    Walker, J.E.4
  • 5
    • 0025697055 scopus 로고
    • Sequence of the bovine 2-oxoglutarate/malate carrier protein: structural relationship to other mitochondrial transport proteins
    • Runswick M.J., Walker J.E., Bisaccia F., Iacobazzi V., and Palmieri F. Sequence of the bovine 2-oxoglutarate/malate carrier protein: structural relationship to other mitochondrial transport proteins. Biochemistry 29 (1990) 11033-11040
    • (1990) Biochemistry , vol.29 , pp. 11033-11040
    • Runswick, M.J.1    Walker, J.E.2    Bisaccia, F.3    Iacobazzi, V.4    Palmieri, F.5
  • 6
    • 0022124340 scopus 로고
    • The uncoupling protein from brown fat mitochondria is related to the mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of folding of the protein in the membrane
    • Aquila H., Link T.A., and Klingenberg M. The uncoupling protein from brown fat mitochondria is related to the mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of folding of the protein in the membrane. EMBO J. 4 (1985) 2369-2376
    • (1985) EMBO J. , vol.4 , pp. 2369-2376
    • Aquila, H.1    Link, T.A.2    Klingenberg, M.3
  • 7
    • 0023333813 scopus 로고
    • Sequence of the bovine mitochondrial phosphate carrier protein: structural relationship to ADP/ATP translocase and the brown fat mitochondria uncoupling protein
    • Runswick M.J., Powell S.J., Nyren P., and Walker J.E. Sequence of the bovine mitochondrial phosphate carrier protein: structural relationship to ADP/ATP translocase and the brown fat mitochondria uncoupling protein. EMBO J. 6 (1987) 1367-1373
    • (1987) EMBO J. , vol.6 , pp. 1367-1373
    • Runswick, M.J.1    Powell, S.J.2    Nyren, P.3    Walker, J.E.4
  • 8
    • 0020473533 scopus 로고
    • Internal sequence repeats and the path of polypeptide in mitochondrial ADP/ATP translocase
    • Saraste M., and Walker J.E. Internal sequence repeats and the path of polypeptide in mitochondrial ADP/ATP translocase. FEBS Lett. 144 (1982) 250-254
    • (1982) FEBS Lett. , vol.144 , pp. 250-254
    • Saraste, M.1    Walker, J.E.2
  • 10
    • 0032571303 scopus 로고    scopus 로고
    • Highly conserved charge-pair networks in the mitochondrial carrier family
    • Nelson D.R., Felix C.M., and Swanson J.M. Highly conserved charge-pair networks in the mitochondrial carrier family. J. Mol. Biol. 277 (1998) 285-308
    • (1998) J. Mol. Biol. , vol.277 , pp. 285-308
    • Nelson, D.R.1    Felix, C.M.2    Swanson, J.M.3
  • 11
    • 33644555509 scopus 로고    scopus 로고
    • Mitochondrial carriers have a common substrate binding site in the cytoplasmic state
    • Robinson A.J., and Kunji E.R.S. Mitochondrial carriers have a common substrate binding site in the cytoplasmic state. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 2617-2622
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2617-2622
    • Robinson, A.J.1    Kunji, E.R.S.2
  • 12
    • 33644513561 scopus 로고    scopus 로고
    • Identification of the Mitochondrial NAD+ Transporter in Saccharomyces cerevisiae
    • Todisco S., Agrimi G., Castegna A., and Palmieri F. Identification of the Mitochondrial NAD+ Transporter in Saccharomyces cerevisiae. J. Biol. Chem. 281 (2006) 1524-1531
    • (2006) J. Biol. Chem. , vol.281 , pp. 1524-1531
    • Todisco, S.1    Agrimi, G.2    Castegna, A.3    Palmieri, F.4
  • 13
    • 30744433627 scopus 로고    scopus 로고
    • Identification of a mitochondrial transporter for pyrimidine nucleotides in Saccharomyces cerevisiae: bacterial expression, reconstitution and functional characterization
    • Marobbio C.M., Di Noia M.A., and Palmieri F. Identification of a mitochondrial transporter for pyrimidine nucleotides in Saccharomyces cerevisiae: bacterial expression, reconstitution and functional characterization. Biochem. J. 393 (2006) 441-446
    • (2006) Biochem. J. , vol.393 , pp. 441-446
    • Marobbio, C.M.1    Di Noia, M.A.2    Palmieri, F.3
  • 14
    • 29644439674 scopus 로고    scopus 로고
    • The calcium-dependent ATP-Mg/Pi mitochondrial carrier is a target of glucose-induced calcium signalling in Saccharomyces cerevisiae
    • Cavero S., Traba J., Del Arco A., and Satrustegui J. The calcium-dependent ATP-Mg/Pi mitochondrial carrier is a target of glucose-induced calcium signalling in Saccharomyces cerevisiae. Biochem. J. 392 (2005) 537-544
    • (2005) Biochem. J. , vol.392 , pp. 537-544
    • Cavero, S.1    Traba, J.2    Del Arco, A.3    Satrustegui, J.4
  • 15
    • 2442650104 scopus 로고    scopus 로고
    • Identification of the mitochondrial GTP/GDP transporter in Saccharomyces cerevisiae
    • Vozza A., Blanco E., Palmieri L., and Palmieri F. Identification of the mitochondrial GTP/GDP transporter in Saccharomyces cerevisiae. J. Biol. Chem. 279 (2004) 20850-20857
    • (2004) J. Biol. Chem. , vol.279 , pp. 20850-20857
    • Vozza, A.1    Blanco, E.2    Palmieri, L.3    Palmieri, F.4
  • 16
    • 3142754128 scopus 로고    scopus 로고
    • Sal1p, a calcium-dependent carrier protein that suppresses an essential cellular function associated With the Aac2 isoform of ADP/ATP translocase in Saccharomyces cerevisiae
    • Chen X.J. Sal1p, a calcium-dependent carrier protein that suppresses an essential cellular function associated With the Aac2 isoform of ADP/ATP translocase in Saccharomyces cerevisiae. Genetics 167 (2004) 607-617
    • (2004) Genetics , vol.167 , pp. 607-617
    • Chen, X.J.1
  • 17
    • 0344442851 scopus 로고    scopus 로고
    • Identification and functional reconstitution of yeast mitochondrial carrier for S-adenosylmethionine
    • Marobbio C.M., Agrimi G., Lasorsa F.M., and Palmieri F. Identification and functional reconstitution of yeast mitochondrial carrier for S-adenosylmethionine. EMBO J. 22 (2003) 5975-5982
    • (2003) EMBO J. , vol.22 , pp. 5975-5982
    • Marobbio, C.M.1    Agrimi, G.2    Lasorsa, F.M.3    Palmieri, F.4
  • 19
    • 0036845261 scopus 로고    scopus 로고
    • Identification and reconstitution of the yeast mitochondrial transporter for thiamine pyrophosphate
    • Marobbio C.M., Vozza A., Harding M., Bisaccia F., Palmieri F., and Walker J.E. Identification and reconstitution of the yeast mitochondrial transporter for thiamine pyrophosphate. EMBO J. 21 (2002) 5653-5661
    • (2002) EMBO J. , vol.21 , pp. 5653-5661
    • Marobbio, C.M.1    Vozza, A.2    Harding, M.3    Bisaccia, F.4    Palmieri, F.5    Walker, J.E.6
  • 20
    • 0034986438 scopus 로고    scopus 로고
    • Characterization of a Saccharomyces cerevisiae gene that encodes a mitochondrial phosphate transporter-like protein
    • Takabatake R., Siddique A.B., Kouchi H., Izui K., and Hata S. Characterization of a Saccharomyces cerevisiae gene that encodes a mitochondrial phosphate transporter-like protein. J. Biochem. (Tokyo) 129 (2001) 827-833
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 827-833
    • Takabatake, R.1    Siddique, A.B.2    Kouchi, H.3    Izui, K.4    Hata, S.5
  • 21
    • 0035903573 scopus 로고    scopus 로고
    • Identification and functional reconstitution of the yeast peroxisomal adenine nucleotide transporter
    • Palmieri L., Rottensteiner H., Girzalsky W., Scarcia P., Palmieri F., and Erdmann R. Identification and functional reconstitution of the yeast peroxisomal adenine nucleotide transporter. EMBO J. 20 (2001) 5049-5059
    • (2001) EMBO J. , vol.20 , pp. 5049-5059
    • Palmieri, L.1    Rottensteiner, H.2    Girzalsky, W.3    Scarcia, P.4    Palmieri, F.5    Erdmann, R.6
  • 22
    • 0035910408 scopus 로고    scopus 로고
    • Identification in Saccharomyces cerevisiae of two isoforms of a novel mitochondrial transporter for 2-oxoadipate and 2-oxoglutarate
    • Palmieri L., Agrimi G., Runswick M.J., Fearnley I.M., Palmieri F., and Walker J.E. Identification in Saccharomyces cerevisiae of two isoforms of a novel mitochondrial transporter for 2-oxoadipate and 2-oxoglutarate. J. Biol. Chem. 276 (2001) 1916-1922
    • (2001) J. Biol. Chem. , vol.276 , pp. 1916-1922
    • Palmieri, L.1    Agrimi, G.2    Runswick, M.J.3    Fearnley, I.M.4    Palmieri, F.5    Walker, J.E.6
  • 25
    • 0030664759 scopus 로고    scopus 로고
    • Identification of the yeast ACR1 gene product as a succinate-fumarate transporter essential for growth on ethanol or acetate
    • Palmieri L., Lasorsa F.M., De Palma A., Palmieri F., Runswick M.J., and Walker J.E. Identification of the yeast ACR1 gene product as a succinate-fumarate transporter essential for growth on ethanol or acetate. FEBS Lett. 417 (1997) 114-118
    • (1997) FEBS Lett. , vol.417 , pp. 114-118
    • Palmieri, L.1    Lasorsa, F.M.2    De Palma, A.3    Palmieri, F.4    Runswick, M.J.5    Walker, J.E.6
  • 26
    • 0030825368 scopus 로고    scopus 로고
    • Identification of the yeast ARG-11 gene as a mitochondrial ornithine carrier involved in arginine biosynthesis
    • Palmieri L., De Marco V., Iacobazzi V., Palmieri F., Runswick M.J., and Walker J.E. Identification of the yeast ARG-11 gene as a mitochondrial ornithine carrier involved in arginine biosynthesis. FEBS Lett. 410 (1997) 447-451
    • (1997) FEBS Lett. , vol.410 , pp. 447-451
    • Palmieri, L.1    De Marco, V.2    Iacobazzi, V.3    Palmieri, F.4    Runswick, M.J.5    Walker, J.E.6
  • 27
    • 0031041238 scopus 로고    scopus 로고
    • Identification of a novel gene encoding the yeast mitochondrial dicarboxylate transport protein via overexpression, purification, and characterization of its protein product
    • Kakhniashvili D., Mayor J.A., Gremse D.A., Xu Y., and Kaplan R.S. Identification of a novel gene encoding the yeast mitochondrial dicarboxylate transport protein via overexpression, purification, and characterization of its protein product. J. Biol. Chem. 272 (1997) 4516-4521
    • (1997) J. Biol. Chem. , vol.272 , pp. 4516-4521
    • Kakhniashvili, D.1    Mayor, J.A.2    Gremse, D.A.3    Xu, Y.4    Kaplan, R.S.5
  • 28
    • 0025282180 scopus 로고
    • A third ADP/ATP translocator gene in yeast
    • Kolarov J., Kolarova N., and Nelson N. A third ADP/ATP translocator gene in yeast. J. Biol. Chem. 265 (1990) 12711-12716
    • (1990) J. Biol. Chem. , vol.265 , pp. 12711-12716
    • Kolarov, J.1    Kolarova, N.2    Nelson, N.3
  • 29
    • 0024288852 scopus 로고
    • Separate genes encode functionally equivalent ADP/ATP carrier proteins in Saccharomyces cerevisiae. Isolation and analysis of AAC2
    • Lawson J.E., and Douglas M.G. Separate genes encode functionally equivalent ADP/ATP carrier proteins in Saccharomyces cerevisiae. Isolation and analysis of AAC2. J. Biol. Chem. 263 (1988) 14812-14818
    • (1988) J. Biol. Chem. , vol.263 , pp. 14812-14818
    • Lawson, J.E.1    Douglas, M.G.2
  • 30
    • 0034053925 scopus 로고    scopus 로고
    • Yeast mitochondrial carriers: bacterial expression, biochemical identification and metabolic significance
    • Palmieri L., Runswick M.J., Fiermonte G., Walker J.E., and Palmieri F. Yeast mitochondrial carriers: bacterial expression, biochemical identification and metabolic significance. J. Bioenerg. Biomembranes 32 (2000) 67-77
    • (2000) J. Bioenerg. Biomembranes , vol.32 , pp. 67-77
    • Palmieri, L.1    Runswick, M.J.2    Fiermonte, G.3    Walker, J.E.4    Palmieri, F.5
  • 31
    • 0027264495 scopus 로고
    • Abundant bacterial expression and reconstitution of an intrinsic membrane-transport protein from bovine mitochondria
    • Fiermonte G., Walker J.E., and Palmieri F. Abundant bacterial expression and reconstitution of an intrinsic membrane-transport protein from bovine mitochondria. Biochem. J. 294 pt. 1 (1993) 293-299
    • (1993) Biochem. J. , vol.294 , Issue.PART 1 , pp. 293-299
    • Fiermonte, G.1    Walker, J.E.2    Palmieri, F.3
  • 32
    • 28844468525 scopus 로고    scopus 로고
    • Functional expression of eukaryotic membrane proteins in Lactococcus lactis
    • Monne M., Chan K.W., Slotboom D.J., and Kunji E.R. Functional expression of eukaryotic membrane proteins in Lactococcus lactis. Protein Sci. 14 (2005) 3048-3056
    • (2005) Protein Sci. , vol.14 , pp. 3048-3056
    • Monne, M.1    Chan, K.W.2    Slotboom, D.J.3    Kunji, E.R.4
  • 33
    • 0028917910 scopus 로고
    • High level expression and characterization of the mitochondrial citrate transport protein from the yeast Saccharomyces cerevisiae
    • Kaplan R.S., Mayor J.A., Gremse D.A., and Wood D.O. High level expression and characterization of the mitochondrial citrate transport protein from the yeast Saccharomyces cerevisiae. J. Biol. Chem. 270 (1995) 4108-4114
    • (1995) J. Biol. Chem. , vol.270 , pp. 4108-4114
    • Kaplan, R.S.1    Mayor, J.A.2    Gremse, D.A.3    Wood, D.O.4
  • 34
    • 0030590885 scopus 로고    scopus 로고
    • Identification by bacterial expression and functional reconstitution of the yeast genomic sequence encoding the mitochondrial dicarboxylate carrier protein
    • Palmieri L., Palmieri F., Runswick M.J., and Walker J.E. Identification by bacterial expression and functional reconstitution of the yeast genomic sequence encoding the mitochondrial dicarboxylate carrier protein. FEBS Lett. 399 (1996) 299-302
    • (1996) FEBS Lett. , vol.399 , pp. 299-302
    • Palmieri, L.1    Palmieri, F.2    Runswick, M.J.3    Walker, J.E.4
  • 35
    • 0027978913 scopus 로고
    • Yeast mitochondrial phosphate transport protein expressed in Escherichia coli. Site-directed mutations at threonine-43 and at a similar location in the second tandem repeat (isoleucine-141)
    • Wohlrab H., and Briggs C. Yeast mitochondrial phosphate transport protein expressed in Escherichia coli. Site-directed mutations at threonine-43 and at a similar location in the second tandem repeat (isoleucine-141). Biochemistry 33 (1994) 9371-9375
    • (1994) Biochemistry , vol.33 , pp. 9371-9375
    • Wohlrab, H.1    Briggs, C.2
  • 36
    • 0029984499 scopus 로고    scopus 로고
    • FLX1 codes for a carrier protein involved in maintaining a proper balance of flavin nucleotides in yeast mitochondria
    • Tzagoloff A., Jang J., Glerum D.M., and Wu M. FLX1 codes for a carrier protein involved in maintaining a proper balance of flavin nucleotides in yeast mitochondria. J. Biol. Chem. 271 (1996) 7392-7397
    • (1996) J. Biol. Chem. , vol.271 , pp. 7392-7397
    • Tzagoloff, A.1    Jang, J.2    Glerum, D.M.3    Wu, M.4
  • 37
    • 0035144432 scopus 로고    scopus 로고
    • The yeast mitochondrial carrier Leu5p and its human homologue Graves' disease protein are required for accumulation of coenzyme A in the matrix
    • Prohl C., Pelzer W., Diekert K., Kmita H., Bedekovics T., Kispal G., and Lill R. The yeast mitochondrial carrier Leu5p and its human homologue Graves' disease protein are required for accumulation of coenzyme A in the matrix. Mol. Cell. Biol. 21 (2001) 1089-1097
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1089-1097
    • Prohl, C.1    Pelzer, W.2    Diekert, K.3    Kmita, H.4    Bedekovics, T.5    Kispal, G.6    Lill, R.7
  • 39
    • 21244448393 scopus 로고    scopus 로고
    • Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis
    • Zhang Y., Lyver E.R., Knight S.A., Lesuisse E., and Dancis A. Frataxin and mitochondrial carrier proteins, Mrs3p and Mrs4p, cooperate in providing iron for heme synthesis. J. Biol. Chem. 280 (2005) 19794-19807
    • (2005) J. Biol. Chem. , vol.280 , pp. 19794-19807
    • Zhang, Y.1    Lyver, E.R.2    Knight, S.A.3    Lesuisse, E.4    Dancis, A.5
  • 40
    • 0141791031 scopus 로고    scopus 로고
    • Identification of the mitochondrial pyruvate carrier in Saccharomyces cerevisiae
    • Hildyard J.C., and Halestrap A.P. Identification of the mitochondrial pyruvate carrier in Saccharomyces cerevisiae. Biochem. J. 374 (2003) 607-611
    • (2003) Biochem. J. , vol.374 , pp. 607-611
    • Hildyard, J.C.1    Halestrap, A.P.2
  • 41
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp
    • Dougherty D.A. Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 271 (1996) 163-168
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 42
    • 31344462177 scopus 로고    scopus 로고
    • Conformational diversity of ligands bound to proteins
    • Stockwell G.R., and Thornton J.M. Conformational diversity of ligands bound to proteins. J. Mol. Biol. 356 (2006) 928-944
    • (2006) J. Mol. Biol. , vol.356 , pp. 928-944
    • Stockwell, G.R.1    Thornton, J.M.2
  • 44
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., and Gay N.J. Distantly related sequences in the alpha-and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1 (1982) 945-951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 45
    • 0023710441 scopus 로고
    • Mapping of the nucleotide-binding sites in the ADP/ATP carrier of beef heart mitochondria by photolabeling with 2-azido[alpha-32P]adenosine diphosphate
    • Dalbon P., Brandolin G., Boulay F., Hoppe J., and Vignais P.V. Mapping of the nucleotide-binding sites in the ADP/ATP carrier of beef heart mitochondria by photolabeling with 2-azido[alpha-32P]adenosine diphosphate. Biochemistry 27 (1988) 5141-5149
    • (1988) Biochemistry , vol.27 , pp. 5141-5149
    • Dalbon, P.1    Brandolin, G.2    Boulay, F.3    Hoppe, J.4    Vignais, P.V.5
  • 46
    • 0030456168 scopus 로고    scopus 로고
    • Probing the role of positive residues in the ADP/ATP carrier from yeast. The effect of six arginine mutations of oxidative phosphorylation and AAC expression
    • Muller V., Basset G., Nelson D.R., and Klingenberg M. Probing the role of positive residues in the ADP/ATP carrier from yeast. The effect of six arginine mutations of oxidative phosphorylation and AAC expression. Biochemistry 35 (1996) 16132-16143
    • (1996) Biochemistry , vol.35 , pp. 16132-16143
    • Muller, V.1    Basset, G.2    Nelson, D.R.3    Klingenberg, M.4
  • 47
    • 4043146497 scopus 로고    scopus 로고
    • A mutation inactivating the mitochondrial inner membrane folate transporter creates a glycine requirement for survival of Chinese hamster cells
    • McCarthy E.A., Titus S.A., Taylor S.M., Jackson-Cook C., and Moran R.G. A mutation inactivating the mitochondrial inner membrane folate transporter creates a glycine requirement for survival of Chinese hamster cells. J. Biol. Chem. 279 (2004) 33829-33836
    • (2004) J. Biol. Chem. , vol.279 , pp. 33829-33836
    • McCarthy, E.A.1    Titus, S.A.2    Taylor, S.M.3    Jackson-Cook, C.4    Moran, R.G.5
  • 48
    • 0030480093 scopus 로고    scopus 로고
    • Probing the role of positive residues in the ADP/ATP carrier from yeast. The effect of six arginine mutations on transport and the four ATP versus ADP exchange modes
    • Heidkamper D., Muller V., Nelson D.R., and Klingenberg M. Probing the role of positive residues in the ADP/ATP carrier from yeast. The effect of six arginine mutations on transport and the four ATP versus ADP exchange modes. Biochemistry 35 (1996) 16144-16152
    • (1996) Biochemistry , vol.35 , pp. 16144-16152
    • Heidkamper, D.1    Muller, V.2    Nelson, D.R.3    Klingenberg, M.4
  • 49
    • 0034629438 scopus 로고    scopus 로고
    • The yeast mitochondrial citrate transport protein. Probing the roles of cysteines, Arg(181), and Arg(189) in transporter function
    • Xu Y., Kakhniashvili D.A., Gremse D.A., Wood D.O., Mayor J.A., Walters D.E., and Kaplan R.S. The yeast mitochondrial citrate transport protein. Probing the roles of cysteines, Arg(181), and Arg(189) in transporter function. J. Biol. Chem. 275 (2000) 7117-7124
    • (2000) J. Biol. Chem. , vol.275 , pp. 7117-7124
    • Xu, Y.1    Kakhniashvili, D.A.2    Gremse, D.A.3    Wood, D.O.4    Mayor, J.A.5    Walters, D.E.6    Kaplan, R.S.7
  • 50
    • 0035951096 scopus 로고    scopus 로고
    • The mitochondrial oxoglutarate carrier: cysteine-scanning mutagenesis of transmembrane domain IV and sensitivity of Cys mutants to sulfhydryl reagents
    • Stipani V., Cappello A.R., Daddabbo L., Natuzzi D., Miniero D.V., Stipani I., and Palmieri F. The mitochondrial oxoglutarate carrier: cysteine-scanning mutagenesis of transmembrane domain IV and sensitivity of Cys mutants to sulfhydryl reagents. Biochemistry 40 (2001) 15805-15810
    • (2001) Biochemistry , vol.40 , pp. 15805-15810
    • Stipani, V.1    Cappello, A.R.2    Daddabbo, L.3    Natuzzi, D.4    Miniero, D.V.5    Stipani, I.6    Palmieri, F.7
  • 51
    • 0014421614 scopus 로고
    • Adenine nucleotide translocation of mitochondria. 1. Specificity and control
    • Pfaff E., and Klingenberg M. Adenine nucleotide translocation of mitochondria. 1. Specificity and control. Eur. J. Biochem. 6 (1968) 66-79
    • (1968) Eur. J. Biochem. , vol.6 , pp. 66-79
    • Pfaff, E.1    Klingenberg, M.2
  • 53
    • 0026611345 scopus 로고
    • ATP-Mg/Pi carrier activity in rat liver mitochondria
    • Nosek M.T., and Aprille J.R. ATP-Mg/Pi carrier activity in rat liver mitochondria. Arch. Biochem. Biophys. 296 (1992) 691-697
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 691-697
    • Nosek, M.T.1    Aprille, J.R.2
  • 54
    • 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. Structure and mechanism of the lactose permease of Escherichia coli. Science 301 (2003) 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
  • 55
    • 29344450131 scopus 로고    scopus 로고
    • X-ray structure of the EmrE multidrug transporter in complex with a substrate
    • Pornillos O., Chen Y.J., Chen A.P., and Chang G. X-ray structure of the EmrE multidrug transporter in complex with a substrate. Science 310 (2005) 1950-1953
    • (2005) Science , vol.310 , pp. 1950-1953
    • Pornillos, O.1    Chen, Y.J.2    Chen, A.P.3    Chang, G.4
  • 56
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na(+)/Cl(-)-dependent neurotransmitter transporters
    • Yamashita A., Singh S.K., Kawate T., Jin Y., and Gouaux E. Crystal structure of a bacterial homologue of Na(+)/Cl(-)-dependent neurotransmitter transporters. Nature 437 (2005) 215-223
    • (2005) Nature , vol.437 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 57
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool D., Boudker O., Jin Y., and Gouaux E. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431 (2004) 811-818
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 58
    • 0034697284 scopus 로고    scopus 로고
    • The yeast mitochondrial citrate transport protein. Probing the secondary structure of transmembrane domain iv and identification of residues that likely comprise a portion of the citrate translocation pathway
    • Kaplan R.S., Mayor J.A., Brauer D., Kotaria R., Walters D.E., and Dean A.M. The yeast mitochondrial citrate transport protein. Probing the secondary structure of transmembrane domain iv and identification of residues that likely comprise a portion of the citrate translocation pathway. J. Biol. Chem. 275 (2000) 12009-12016
    • (2000) J. Biol. Chem. , vol.275 , pp. 12009-12016
    • Kaplan, R.S.1    Mayor, J.A.2    Brauer, D.3    Kotaria, R.4    Walters, D.E.5    Dean, A.M.6
  • 60
    • 0024600466 scopus 로고
    • Molecular aspects of the adenine nucleotide carrier from mitochondria
    • Klingenberg M. Molecular aspects of the adenine nucleotide carrier from mitochondria. Arch. Biochem. Biophys. 270 (1989) 1-14
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 1-14
    • Klingenberg, M.1
  • 61
    • 0000122573 scopus 로고
    • PHYLIP - phylogeny inference package (version 3.2)
    • Felsenstein J. PHYLIP - phylogeny inference package (version 3.2). Cladisitics 5 (1989) 164-166
    • (1989) Cladisitics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 62
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones D.T., Taylor W.R., and Thornton J.M. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8 (1992) 275-282
    • (1992) Comput. Appl. Biosci. , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.