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Volumn 288, Issue 28, 2013, Pages 20734-20744

Sequence determinants of GLUT1 oligomerization: Analysis by homology-scanning mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD-BRAIN BARRIER; CO-IMMUNOPRECIPITATION ASSAYS; GLUCOSE TRANSPORTERS; HUMAN EMBRYONIC KIDNEYS; OLIGOMERIC STRUCTURE; OPTIMAL ASSOCIATION; SEQUENCE DETERMINANTS; TRANSMEMBRANE HELICES;

EID: 84880049245     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.469023     Document Type: Article
Times cited : (42)

References (51)
  • 1
    • 84862163151 scopus 로고    scopus 로고
    • Role of monosaccharide transport proteins in carbohydrate assimilation, distribution, metabolism, and homeostasis
    • Cura, A. J., and Carruthers, A. (2012) Role of monosaccharide transport proteins in carbohydrate assimilation, distribution, metabolism, and homeostasis. Compr. Physiol. 2, 863-914
    • (2012) Compr. Physiol. , vol.2 , pp. 863-914
    • Cura, A.J.1    Carruthers, A.2
  • 4
    • 0022360064 scopus 로고
    • Sequence and structure of a human glucose transporter
    • Mueckler, M., Caruso, C., Baldwin, S. A., Panico, M., Blench, I., Morris, H. R., Allard, W. J., Lienhard, G. E., and Lodish, H. F. (1985) Sequence and structure of a human glucose transporter. Science 229, 941-945 (Pubitemid 16248486)
    • (1985) Science , vol.229 , Issue.4717 , pp. 941-945
    • Mueckler, M.1    Caruso, C.2    Baldwin, S.A.3
  • 5
    • 0037207473 scopus 로고    scopus 로고
    • Regulation of amino acid and glucose transporters in endothelial and smooth muscle cells
    • Mann, G. E., Yudilevich, D. L., and Sobrevia, L. (2003) Regulation of amino acid and glucose transporters in endothelial and smooth muscle cells. Physiol. Rev. 83, 183-252 (Pubitemid 36459881)
    • (2003) Physiological Reviews , vol.83 , Issue.1 , pp. 183-252
    • Mann, G.E.1    Yudilevich, D.L.2    Sobrevia, L.3
  • 6
    • 34547624611 scopus 로고    scopus 로고
    • Supply and demand in cerebral energy metabolism: The role of nutrient transporters
    • DOI 10.1038/sj.jcbfm.9600521, PII 9600521
    • Simpson, I. A., Carruthers, A., and Vannucci, S. J. (2007) Supply and demand in cerebral energy metabolism. The role of nutrient transporters. J. Cereb. Blood Flow Metab. 27, 1766-1791 (Pubitemid 47624552)
    • (2007) Journal of Cerebral Blood Flow and Metabolism , vol.27 , Issue.11 , pp. 1766-1791
    • Simpson, I.A.1    Carruthers, A.2    Vannucci, S.J.3
  • 8
    • 0023224412 scopus 로고
    • Fourier transform infrared spectroscopic study of the structure and conformational changes of the human erythrocyte glucose transporter
    • Alvarez, J., Lee, D. C., Baldwin, S. A., and Chapman, D. (1987) Fourier transform infrared spectroscopic study of the structure and conformational changes of the human erythrocyte glucose transporter. J. Biol. Chem. 262, 3502-3509 (Pubitemid 17136446)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.8 , pp. 3502-3509
    • Alvarez, J.1    Lee, D.C.2    Baldwin, S.A.3    Chapman, D.4
  • 9
    • 0028131474 scopus 로고
    • Topology of the Glut 1 glucose transporter deduced from glycosylation scanning mutagenesis
    • Hresko, R. C., Kruse, M., Strube, M., and Mueckler, M. (1994) Topology of the Glut 1 glucose transporter deduced from glycosylation scanning mutagenesis. J. Biol. Chem. 269, 20482-20488 (Pubitemid 24260453)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.32 , pp. 20482-20488
    • Hresko, R.C.1    Kruse, M.2    Strube, M.3    Mueckler, M.4
  • 10
    • 61349105371 scopus 로고    scopus 로고
    • Analysis of glucose transporter topology and structural dynamics
    • Blodgett, D. M., Graybill, C., and Carruthers, A. (2008) Analysis of glucose transporter topology and structural dynamics. J. Biol. Chem. 283, 36416-36424
    • (2008) J. Biol. Chem. , vol.283 , pp. 36416-36424
    • Blodgett, D.M.1    Graybill, C.2    Carruthers, A.3
  • 11
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • DOI 10.1126/science.1087619
    • Huang, Y., Lemieux, M. J., Song, J., Auer, M., and Wang, D. N. (2003) Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301, 616-620 (Pubitemid 36927940)
    • (2003) Science , vol.301 , Issue.5633 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.-N.5
  • 12
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • DOI 10.1126/science.1088196
    • 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 (Pubitemid 36927939)
    • (2003) Science , vol.301 , Issue.5633 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 13
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin, Y., He, X., Szewczyk, P., Nguyen, T., and Chang, G. (2006) Structure of the multidrug transporter EmrD from Escherichia coli. Science 312, 741-744
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 14
    • 84867657593 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of glucose transporters GLUT1-4
    • Sun, L., Zeng, X., Yan, C., Sun, X., Gong, X., Rao, Y., and Yan, N. (2012) Crystal structure of a bacterial homologue of glucose transporters GLUT1-4. Nature 490, 361-366
    • (2012) Nature , vol.490 , pp. 361-366
    • Sun, L.1    Zeng, X.2    Yan, C.3    Sun, X.4    Gong, X.5    Rao, Y.6    Yan, N.7
  • 15
    • 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
  • 16
    • 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
  • 17
    • 33845983649 scopus 로고    scopus 로고
    • Transmembrane segment 12 of the Glut1 glucose transporter is an outer helix and is not directly involved in the transport mechanism
    • DOI 10.1074/jbc.M608158200
    • Mueckler, M., and Makepeace, C. (2006) Transmembrane segment 12 of the Glut1 glucose transporter is an outer helix and is not directly involved in the transport mechanism. J. Biol. Chem. 281, 36993-36998 (Pubitemid 46042169)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 36993-36998
    • Mueckler, M.1    Makepeace, C.2
  • 18
    • 8744293151 scopus 로고    scopus 로고
    • Transmembrane segment 3 of the Glut1 glucose transporter is an outer helix
    • DOI 10.1074/jbc.M408632200
    • Mueckler, M., Roach, W., and Makepeace, C. (2004) Transmembrane segment 3 of the Glut1 glucose transporter is an outer helix. J. Biol. Chem. 279, 46876-46881 (Pubitemid 39518339)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46876-46881
    • Mueckler, M.1    Roach, W.2    Makepeace, C.3
  • 19
    • 0018871457 scopus 로고
    • Glucose transport carrier of human erythrocytes. Radiation-target size of glucose-sensitive cytochalasin B binding protein
    • Jung, C. Y., Hsu, T. L., Hah, J. S., Cha, C., and Haas, M. N. (1980) Glucose transport carrier of human erythrocytes. Radiation-target size of glucose-sensitive cytochalasin B binding protein. J. Biol. Chem. 255, 361-364 (Pubitemid 10112341)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.2 , pp. 361-364
    • Jung, C.Y.1    Hsu, T.L.2    Hah, J.S.3
  • 20
    • 0025738711 scopus 로고
    • Cholate-solubilized erythrocyte glucose transporters exist as a mixture of homodimers and homotetramers
    • Hebert, D. N., and Carruthers, A. (1991) Cholate-solubilized erythrocyte glucose transporters exist as a mixture of homodimers and homotetramers. Biochemistry 30, 4654-4658
    • (1991) Biochemistry , vol.30 , pp. 4654-4658
    • Hebert, D.N.1    Carruthers, A.2
  • 21
    • 0029131908 scopus 로고
    • Glucose transporter function is controlled by transporter oligomeric structure. A single, intramolecular disulfide promotes GLUT1 tetramerization
    • Zottola, R. J., Cloherty, E. K., Coderre, P. E., Hansen, A., Hebert, D. N., and Carruthers, A. (1995) Glucose transporter function is controlled by transporter oligomeric structure. A single, intramolecular disulfide promotes GLUT1 tetramerization. Biochemistry 34, 9734-9747
    • (1995) Biochemistry , vol.34 , pp. 9734-9747
    • Zottola, R.J.1    Cloherty, E.K.2    Coderre, P.E.3    Hansen, A.4    Hebert, D.N.5    Carruthers, A.6
  • 22
    • 0027082962 scopus 로고
    • Glucose transporter oligomeric structure determines transporter function. Reversible redox-dependent interconversions of tetrameric and dimeric GLUT1
    • Hebert, D. N., and Carruthers, A. (1992) Glucose transporter oligomeric structure determines transporter function. Reversible redox-dependent interconversions of tetrameric and dimeric GLUT1. J. Biol. Chem. 267, 23829-23838 (Pubitemid 23088192)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.33 , pp. 23829-23838
    • Hebert, D.N.1    Carruthers, A.2
  • 23
    • 0035951093 scopus 로고    scopus 로고
    • The red blood cell glucose transporter presents multiple, nucleotide-sensitive sugar exit sites
    • DOI 10.1021/bi015586w
    • Cloherty, E. K., Levine, K. B., and Carruthers, A. (2001) The red blood cell glucose transporter presents multiple, nucleotide-sensitive sugar exit sites. Biochemistry 40, 15549-15561 (Pubitemid 34015182)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15549-15561
    • Cloherty, E.K.1    Levine, K.B.2    Carruthers, A.3
  • 24
    • 0033593017 scopus 로고    scopus 로고
    • The human erythrocyte sugar transporter presents two sugar import sites
    • Hamill, S., Cloherty, E. K., and Carruthers, A. (1999) The human erythrocyte sugar transporter presents two sugar import sites. Biochemistry 38, 16974-16983
    • (1999) Biochemistry , vol.38 , pp. 16974-16983
    • Hamill, S.1    Cloherty, E.K.2    Carruthers, A.3
  • 25
    • 0025732373 scopus 로고
    • Inhibitions of sugar transport produced by ligands binding at opposite sides of the membrane. Evidence for simultaneous occupation of the carrier by maltose and cytochalasin B
    • Carruthers, A., and Helgerson, A. L. (1991) Inhibitions of sugar transport produced by ligands binding at opposite sides of the membrane. Evidence for simultaneous occupation of the carrier by maltose and cytochalasin B. Biochemistry 30, 3907-3915
    • (1991) Biochemistry , vol.30 , pp. 3907-3915
    • Carruthers, A.1    Helgerson, A.L.2
  • 26
    • 0023189831 scopus 로고
    • Equilibrium ligand binding to the human erythrocyte sugar transporter. Evidence for two sugar-binding sites per carrier
    • Helgerson, A. L., and Carruthers, A. (1987) Equilibrium ligand binding to the human erythrocyte sugar transporter. Evidence for two sugar-binding sites per carrier. J. Biol. Chem. 262, 5464-5475 (Pubitemid 17104154)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.12 , pp. 5464-5475
    • Helgerson, A.L.1    Carruthers, A.2
  • 27
    • 0021816424 scopus 로고
    • Rapid kinetics of the glucose transporter from human erythrocytes. Detection and measurement of a half-turnover of the purified transporter
    • Appleman, J. R., and Lienhard, G. E. (1985) Rapid kinetics of the glucose transporter from human erythrocytes. Detection and measurement of a half-turnover of the purified transporter. J. Biol. Chem. 260, 4575-4578 (Pubitemid 15034588)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.8 , pp. 4575-4578
    • Appleman, J.R.1    Lienhard, G.E.2
  • 28
    • 0019814011 scopus 로고
    • Equilibria and kinetics of ligand binding to the human erythrocyte glucose transporter. Evidence for an alternating conformation model for transport
    • Gorga, F. R., and Lienhard, G. E. (1981) Equilibria and kinetics of ligand binding to the human erythrocyte glucose transporter. Evidence for an alternating conformation model for transport. Biochemistry 20, 5108-5113 (Pubitemid 12239136)
    • (1981) Biochemistry , vol.20 , Issue.18 , pp. 5108-5113
    • Gorga, F.R.1    Lienhard, G.E.2
  • 29
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. (1966) Simple allosteric model for membrane pumps. Nature 211, 969-970
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 30
    • 0016201985 scopus 로고
    • Testing and characterizing the simple carrier
    • Lieb, W. R., and Stein, W. D. (1974) Testing and characterizing the simple carrier. Biochim. Biophys. Acta 373, 178-196
    • (1974) Biochim. Biophys. Acta , vol.373 , pp. 178-196
    • Lieb, W.R.1    Stein, W.D.2
  • 31
    • 0031238676 scopus 로고    scopus 로고
    • Glucose transporter proteins in brain: Delivery of glucose to neurons and glia
    • DOI 10.1002/(SICI)1098-1136(199709)21:1<2::AID-GLI
    • Vannucci, S. J., Maher, F., and Simpson, I. A. (1997) Glucose transporter proteins in brain. Delivery of glucose to neurons and glia. Glia 21, 2-21 (Pubitemid 27389636)
    • (1997) GLIA , vol.21 , Issue.1 , pp. 2-21
    • Vannucci, S.J.1    Maher, F.2    Simpson, I.A.3
  • 32
    • 0026447087 scopus 로고
    • Mammalian facilitative glucose transporters. Evidence for similar substrate recognition sites in functionally monomeric proteins
    • Burant, C. F., and Bell, G. I. (1992) Mammalian facilitative glucose transporters. Evidence for similar substrate recognition sites in functionally monomeric proteins. Biochemistry 31, 10414-10420
    • (1992) Biochemistry , vol.31 , pp. 10414-10420
    • Burant, C.F.1    Bell, G.I.2
  • 35
    • 84871131879 scopus 로고    scopus 로고
    • Sequence determinants of GLUT1-mediated accelerated-exchange transport. Analysis by homology-scanning mutagenesis
    • Vollers, S. S., and Carruthers, A. (2012) Sequence determinants of GLUT1-mediated accelerated-exchange transport. Analysis by homology-scanning mutagenesis. J. Biol. Chem. 287, 42533-42544
    • (2012) J. Biol. Chem. , vol.287 , pp. 42533-42544
    • Vollers, S.S.1    Carruthers, A.2
  • 36
    • 17144408367 scopus 로고    scopus 로고
    • Properties of the human erythrocyte glucose transport protein are determined by cellular context
    • DOI 10.1021/bi0477541
    • Levine, K. B., Robichaud, T. K., Hamill, S., Sultzman, L. A., and Carruthers, A. (2005) Properties of the human erythrocyte glucose transport protein are determined by cellular context. Biochemistry 44, 5606-5616 (Pubitemid 40525098)
    • (2005) Biochemistry , vol.44 , Issue.15 , pp. 5606-5616
    • Levine, K.B.1    Robichaud, T.K.2    Hamill, S.3    Sultzman, L.A.4    Carruthers, A.5
  • 37
    • 0037159240 scopus 로고    scopus 로고
    • Molecular determinants of sugar transport regulation by ATP
    • DOI 10.1021/bi0258997
    • Levine, K. B., Cloherty, E. K., Hamill, S., and Carruthers, A. (2002) Molecular determinants of sugar transport regulation by ATP. Biochemistry 41, 12629-12638 (Pubitemid 35192492)
    • (2002) Biochemistry , vol.41 , Issue.42 , pp. 12629-12638
    • Levine, K.B.1    Cloherty, E.K.2    Hamill, S.3    Carruthers, A.4
  • 38
    • 84867592518 scopus 로고    scopus 로고
    • AMP kinase regulation of sugar transport in brain capillary endothelial cells during acute metabolic stress
    • Cura, A. J., and Carruthers, A. (2012) AMP kinase regulation of sugar transport in brain capillary endothelial cells during acute metabolic stress. Am. J. Physiol. Cell Physiol. 303, C806-C814
    • (2012) Am. J. Physiol. Cell Physiol. , vol.303
    • Cura, A.J.1    Carruthers, A.2
  • 39
    • 77952064131 scopus 로고    scopus 로고
    • Acute modulation of sugar transport in brain capillary endothelial cell cultures during activation of the metabolic stress pathway
    • Cura, A. J., and Carruthers, A. (2010) Acute modulation of sugar transport in brain capillary endothelial cell cultures during activation of the metabolic stress pathway. J. Biol. Chem. 285, 15430-15439
    • (2010) J. Biol. Chem. , vol.285 , pp. 15430-15439
    • Cura, A.J.1    Carruthers, A.2
  • 40
  • 41
    • 12344321851 scopus 로고    scopus 로고
    • Predicting the three-dimensional structure of the human facilitative glucose transporter Glut1 by a novel evolutionary homology strategy: Insights on the molecular mechanism of substrate migration, and binding for glucose and inhibitory molecules
    • DOI 10.1529/biophysj.104.047886
    • Salas-Burgos, A., Iserovich, P., Zuniga, F., Vera, J. C., and Fischbarg, J. (2004) Predicting the three-dimensional structure of the human facilitative glucose transporter glut1 by a novel evolutionary homology strategy. Insights on the molecular mechanism of substrate migration, and binding sites for glucose and inhibitory molecules. Biophys. J. 87, 2990-2999 (Pubitemid 40468559)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 2990-2999
    • Salas-Burgos, A.1    Iserovich, P.2    Zuniga, F.3    Vera, J.C.4    Fischbarg, J.5
  • 42
    • 28144456581 scopus 로고    scopus 로고
    • A modified, dual reporter TOXCAT system for monitoring homodimerization of transmembrane segments of proteins
    • DOI 10.1016/j.bbrc.2005.11.022, PII S0006291X05025337
    • Lis, M., and Blumenthal, K. (2006) A modified, dual reporter TOXCAT system for monitoring homodimerization of transmembrane segments of proteins. Biochem. Biophys. Res. Commun. 339, 321-324 (Pubitemid 41697552)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.1 , pp. 321-324
    • Lis, M.1    Blumenthal, K.2
  • 43
    • 0035850793 scopus 로고    scopus 로고
    • Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library
    • DOI 10.1006/jmbi.2001.5007
    • Leeds, J. A., Boyd, D., Huber, D. R., Sonoda, G. K., Luu, H. T., Engelman, D. M., and Beckwith, J. (2001) Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library. J. Mol. Biol. 313, 181-195 (Pubitemid 33001174)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.1 , pp. 181-195
    • Leeds, J.A.1    Boyd, D.2    Huber, D.R.3    Sonoda, G.K.4    Luu, H.T.5    Engelman, D.M.6    Beckwith, J.7
  • 44
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif. A framework for transmembrane helix-helix association
    • Russ, W. P., and Engelman, D. M. (2000) The GxxxG motif. A framework for transmembrane helix-helix association. J. Mol. Biol. 296, 911-919
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 46
    • 78650171241 scopus 로고    scopus 로고
    • Design, function and structure of a monomeric ClC transporter
    • Robertson, J. L., Kolmakova-Partensky, L., and Miller, C. (2010) Design, function and structure of a monomeric ClC transporter. Nature 468, 844-847
    • (2010) Nature , vol.468 , pp. 844-847
    • Robertson, J.L.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 47
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography: Oligomeric stability and origin of heterogeneity
    • Casey, J. R., and Reithmeier, R. A. (1991) Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity. J. Biol. Chem. 266, 15726-15737 (Pubitemid 21907719)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.24 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.F.2
  • 48
    • 32144455716 scopus 로고    scopus 로고
    • r cell line
    • DOI 10.1016/j.bbamcr.2005.12.006, PII S016748890500279X
    • Olczak, M., and Guillen, E. (2006) Characterization of a mutation and an alternative splicing of UDP-galactose transporter in MDCK-RCAr cell line. Biochim. Biophys. Acta 1763, 82-92 (Pubitemid 43208735)
    • (2006) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1763 , Issue.1 , pp. 82-92
    • Olczak, M.1    Guillen, E.2
  • 49
    • 0031711820 scopus 로고    scopus 로고
    • Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus
    • DOI 10.1146/annurev.biochem.67.1.49
    • Hirschberg, C. B., Robbins, P. W., and Abeijon, C. (1998) Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem. 67, 49-69 (Pubitemid 28411123)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 49-69
    • Hirschberg, C.B.1    Robbins, P.W.2    Abeijon, C.3
  • 50
    • 84873509603 scopus 로고    scopus 로고
    • Single particle electron microscopy analysis of the bovine anion exchanger 1 reveals a flexible linker connecting the cytoplasmic and membrane domains
    • Jiang, J., Magilnick, N., Tsirulnikov, K., Abuladze, N., Atanasov, I., Ge, P., Narla, M., Pushkin, A., Zhou, Z. H., and Kurtz, I. (2013) Single particle electron microscopy analysis of the bovine anion exchanger 1 reveals a flexible linker connecting the cytoplasmic and membrane domains. PLoS One 8, e55408
    • (2013) PLoS One , vol.8
    • Jiang, J.1    Magilnick, N.2    Tsirulnikov, K.3    Abuladze, N.4    Atanasov, I.5    Ge, P.6    Narla, M.7    Pushkin, A.8    Zhou, Z.H.9    Kurtz, I.10


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