메뉴 건너뛰기




Volumn 43, Issue 29, 2004, Pages 9289-9297

Homology modeling of the human microsomal glucose 6-phosphate transporter explains the mutations that cause the glycogen storage disease type Ib

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CONFORMATIONS; DISEASE CONTROL; ENZYMES; MATHEMATICAL MODELS;

EID: 3242729357     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049334h     Document Type: Article
Times cited : (26)

References (75)
  • 2
    • 0034976967 scopus 로고    scopus 로고
    • Molecular genetics of type 1 glycogen storage disease
    • Janecke, A. R., Mayatepek, E., and Utermann, G. (2001) Molecular genetics of type 1 glycogen storage disease, Mol. Genet. Metab. 73, 117-125.
    • (2001) Mol. Genet. Metab. , vol.73 , pp. 117-125
    • Janecke, A.R.1    Mayatepek, E.2    Utermann, G.3
  • 3
    • 0036086034 scopus 로고    scopus 로고
    • Type I glycogen storage diseases: Disorders of the glucose-6-phosphatase complex
    • Chou, J. Y., Matern, D., Mansfield, B. C., and Chen, Y. T. (2002) Type I glycogen storage diseases: disorders of the glucose-6-phosphatase complex, Curr. Mol. Med. 2, 121-143.
    • (2002) Curr. Mol. Med. , vol.2 , pp. 121-143
    • Chou, J.Y.1    Matern, D.2    Mansfield, B.C.3    Chen, Y.T.4
  • 4
    • 0036733379 scopus 로고    scopus 로고
    • The biochemistry and molecular biology of the glucose-6-phosphatase system
    • Foster, J. D., and Nordlie, R. C. (2002) The biochemistry and molecular biology of the glucose-6-phosphatase system, Exp. Biol. Med. 227, 601-608.
    • (2002) Exp. Biol. Med. , vol.227 , pp. 601-608
    • Foster, J.D.1    Nordlie, R.C.2
  • 5
    • 0033605362 scopus 로고    scopus 로고
    • Inactivation of the glucose 6-phosphate transporter causes glycogen storage disease type 1b
    • Hiraiwa, H., Pan, C. J., Lin, B., Moses, S. W., and Chou, J. Y. (1999) Inactivation of the glucose 6-phosphate transporter causes glycogen storage disease type 1b, J. Biol. Chem. 274, 5532-5536.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5532-5536
    • Hiraiwa, H.1    Pan, C.J.2    Lin, B.3    Moses, S.W.4    Chou, J.Y.5
  • 6
    • 0036899098 scopus 로고    scopus 로고
    • Structure-function analysis of the glucose-6-phosphate transporter deficient in glycogen storage disease type 1b
    • Chen, L. Y., Pan, C. J., Shieh, J. J., and Chou, J. Y. (2002) Structure-function analysis of the glucose-6-phosphate transporter deficient in glycogen storage disease type 1b, Hum. Mol. Genet. 11, 3199-3207.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 3199-3207
    • Chen, L.Y.1    Pan, C.J.2    Shieh, J.J.3    Chou, J.Y.4
  • 7
    • 0031448837 scopus 로고    scopus 로고
    • Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type 1b
    • Gerin, I., Veiga-da-Cunha, M., Achouri, Y., Collet, J. F., and Van Schaftingen, E. (1997) Sequence of a putative glucose 6-phosphate translocase, mutated in glycogen storage disease type 1b, FEBS Lett. 419, 235-238.
    • (1997) FEBS Lett. , vol.419 , pp. 235-238
    • Gerin, I.1    Veiga-Da-Cunha, M.2    Achouri, Y.3    Collet, J.F.4    Van Schaftingen, E.5
  • 8
    • 0033553477 scopus 로고    scopus 로고
    • Transmembrane topology of human glucose 6-phosphate transporter
    • Pan, C. J., Lin, B., and Chou, J. Y. (1999) Transmembrane topology of human glucose 6-phosphate transporter, J. Biol. Chem. 274, 13865-13869.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13865-13869
    • Pan, C.J.1    Lin, B.2    Chou, J.Y.3
  • 11
    • 0032509365 scopus 로고    scopus 로고
    • Functional symmetry of UhpT, the sugar phosphate transporter of Escherichia coli
    • Fann, M. C., and Maloney, P. C. (1998) Functional symmetry of UhpT, the sugar phosphate transporter of Escherichia coli, J Biol. Chem. 273, 33735-33740.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33735-33740
    • Fann, M.C.1    Maloney, P.C.2
  • 12
    • 0035810954 scopus 로고    scopus 로고
    • High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter
    • Auer, M., Kim, M. J., Lemieux, M. J., Villa, A., Song, J., Li, X. D., and Wang, D. N. (2001) High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter, Biochemistry 40, 6628-6635.
    • (2001) Biochemistry , vol.40 , pp. 6628-6635
    • Auer, M.1    Kim, M.J.2    Lemieux, M.J.3    Villa, A.4    Song, J.5    Li, X.D.6    Wang, D.N.7
  • 13
    • 0029768915 scopus 로고    scopus 로고
    • Enzymatic and biochemical probes of residues external to the translocation pathway of UhpT, the sugar phosphate carrier of Escherichia coli
    • Matos, M., Fann, M. C., Yan, R. T., and Maloney, P. C. (1996) Enzymatic and biochemical probes of residues external to the translocation pathway of UhpT, the sugar phosphate carrier of Escherichia coli, J. Biol. Chem. 271, 18571-18575.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18571-18575
    • Matos, M.1    Fann, M.C.2    Yan, R.T.3    Maloney, P.C.4
  • 14
    • 0032528196 scopus 로고    scopus 로고
    • Identification of two essential arginine residues in UhpT, the sugar phosphate antiporter of Escherichia coli
    • Fann, M. C., Davies, A. H., Varadhachary, A., Kuroda, T., Sevier, C., Tsuchiya, T., and Maloney, P. C. (1998) Identification of two essential arginine residues in UhpT, the sugar phosphate antiporter of Escherichia coli, J. Membr. Biol. 164, 187-195.
    • (1998) J. Membr. Biol. , vol.164 , pp. 187-195
    • Fann, M.C.1    Davies, A.H.2    Varadhachary, A.3    Kuroda, T.4    Sevier, C.5    Tsuchiya, T.6    Maloney, P.C.7
  • 15
    • 0345276579 scopus 로고    scopus 로고
    • Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily
    • Lemieux, M. J., Song, J., Kim, M. J., Huang, Y., Villa, A., Auer, M., Li, X. D., and Wang, D. N. (2003) Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily, Protein Sci. 12, 2748-2756.
    • (2003) Protein Sci. , vol.12 , pp. 2748-2756
    • Lemieux, M.J.1    Song, J.2    Kim, M.J.3    Huang, Y.4    Villa, A.5    Auer, M.6    Li, X.D.7    Wang, D.N.8
  • 16
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • 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.
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 17
    • 0041766317 scopus 로고    scopus 로고
    • Structural biology. Breaching the barrier
    • Locher, K. P., Bass, R. B., and Rees, D. C. (2003) Structural biology. Breaching the barrier, Science 301, 603-604.
    • (2003) Science , vol.301 , pp. 603-604
    • Locher, K.P.1    Bass, R.B.2    Rees, D.C.3
  • 18
    • 0842334536 scopus 로고    scopus 로고
    • Whither structural biology?
    • Harrison, S. C. (2004) Whither structural biology?, Nat. Struct. Mol. Biol. 11, 12-15.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 12-15
    • Harrison, S.C.1
  • 19
    • 0037235663 scopus 로고    scopus 로고
    • Protein-based virtual screening of chemical databases. II. Are homology models of G-Protein Coupled Receptors suitable targets?
    • Bissantz, C., Bernard, P., Hibert, M., and Rognan, D. (2003) Protein-based virtual screening of chemical databases. II. Are homology models of G-Protein Coupled Receptors suitable targets? Proteins 50, 5-25.
    • (2003) Proteins , vol.50 , pp. 5-25
    • Bissantz, C.1    Bernard, P.2    Hibert, M.3    Rognan, D.4
  • 20
    • 0037382256 scopus 로고    scopus 로고
    • Filter flexibility in a mammalian K channel: Models and simulations of Kir6.2 mutants
    • Capener, C. E., Proks, P., Ashcroft, F. M., and Sansom, M. S. (2003) Filter flexibility in a mammalian K channel: models and simulations of Kir6.2 mutants, Biophys. J. 84, 2345-2356.
    • (2003) Biophys. J. , vol.84 , pp. 2345-2356
    • Capener, C.E.1    Proks, P.2    Ashcroft, F.M.3    Sansom, M.S.4
  • 21
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G., and Roth, C. B. (2001) Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters, Science 293, 1793-1800.
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 22
    • 0642272487 scopus 로고    scopus 로고
    • An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling
    • Stenham, D. R., Campbell, J. D., Sansom, M. S., Higgins, C. F., Kerr, I. D., and Linton, K. J. (2003) An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling, FASEB J. 17, 2287-2289.
    • (2003) FASEB J. , vol.17 , pp. 2287-2289
    • Stenham, D.R.1    Campbell, J.D.2    Sansom, M.S.3    Higgins, C.F.4    Kerr, I.D.5    Linton, K.J.6
  • 23
    • 0347683446 scopus 로고    scopus 로고
    • Molecular modeling correctly predicts the functional importance of Phe594 in transmembrane helix 11 of the multidrug resistance protein, MRP1 (ABCC1)
    • Campbell, J. D., Koike, K., Moreau, C., Sansom, M. S., Deeley, R. G., and Cole, S. P. (2004) Molecular modeling correctly predicts the functional importance of Phe594 in transmembrane helix 11 of the multidrug resistance protein, MRP1 (ABCC1), J. Biol. Chem. 279, 463-468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 463-468
    • Campbell, J.D.1    Koike, K.2    Moreau, C.3    Sansom, M.S.4    Deeley, R.G.5    Cole, S.P.6
  • 24
    • 0037426344 scopus 로고    scopus 로고
    • Extending the structure of an ABC transporter to atomic resolution: Modeling and simulation studies of MsbA
    • Campbell, J. D., Biggin, P. C., Baaden, M., and Sansom, M. S. (2003) Extending the structure of an ABC transporter to atomic resolution: modeling and simulation studies of MsbA, Biochemistry 42, 3666-3673.
    • (2003) Biochemistry , vol.42 , pp. 3666-3673
    • Campbell, J.D.1    Biggin, P.C.2    Baaden, M.3    Sansom, M.S.4
  • 25
    • 0042531543 scopus 로고    scopus 로고
    • A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure
    • Seigneuret, M., and Gamier-Suillerot, A. (2003) A structural model for the open conformation of the mdr1 P-glycoprotein based on the MsbA crystal structure, J. Biol. Chem. 278, 30115-30124.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30115-30124
    • Seigneuret, M.1    Gamier-Suillerot, A.2
  • 27
    • 0034623005 scopus 로고    scopus 로고
    • T-COFFEE: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and Heringa, J. (2000) T-COFFEE: A novel method for fast and accurate multiple sequence alignment, J. Mol. Biol. 302, 205-217.
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 28
    • 0034946186 scopus 로고    scopus 로고
    • A three-dimensional model of endothelin-converting enzyme (ECE) based on the X-ray structure of neutral endopeptidase 24.11 (NEP)
    • Bur, D., Dale, G. E., and Oefner, C. (2001) A three-dimensional model of endothelin-converting enzyme (ECE) based on the X-ray structure of neutral endopeptidase 24.11 (NEP), Protein Eng. 14, 337-341.
    • (2001) Protein Eng. , vol.14 , pp. 337-341
    • Bur, D.1    Dale, G.E.2    Oefner, C.3
  • 29
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane α-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzo, M., Wallin, E., Simon, I., von Heijne, G., and Elofsson, A. (1997) Prediction of transmembrane α-helices in prokaryotic membrane proteins: the dense alignment surface method, Protein Eng. 10, 673-676.
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 30
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnady, G. E., and Simon, I. (1998) Principles governing amino acid composition of integral membrane proteins: application to topology prediction, J. Mol. Biol. 283, 489-506.
    • (1998) J. Mol. Biol. , vol.283 , pp. 489-506
    • Tusnady, G.E.1    Simon, I.2
  • 31
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones, D. T., Taylor, W. R., and Thornton, J. M. (1994) A model recognition approach to the prediction of all-helical membrane protein structure and topology, Biochemistry 33, 3038-3049.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 32
    • 0028902788 scopus 로고
    • Transmembrane helices predicted at 95% accuracy
    • Rost, B., Casadio, R., Fariselli, P., and Sander, C. (1995) Transmembrane helices predicted at 95% accuracy, Protein Sci. 4, 521-533.
    • (1995) Protein Sci. , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 33
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes, J. Mol. Biol. 305, 567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 34
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning proteins segments
    • Hofmann, K., and Stoffel, W. (1993) TMbase - a database of membrane spanning proteins segments, Biol. Chem. Hoppe-Seyler 374, 166-171.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166-171
    • Hofmann, K.1    Stoffel, W.2
  • 35
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M. G., and von Heijne, G. (1994) TopPred II: an improved software for membrane protein structure predictions, Comput. Appl. Biosci. 10, 685-686.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 36
    • 0344406716 scopus 로고    scopus 로고
    • Reliability measures for membrane protein topology prediction algorithms
    • Melen, K., Krogh, A., and von Heijne, G. (2003) Reliability measures for membrane protein topology prediction algorithms, J. Mol. Biol. 327, 735-744.
    • (2003) J. Mol. Biol. , vol.327 , pp. 735-744
    • Melen, K.1    Krogh, A.2    Von Heijne, G.3
  • 37
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints, J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 38
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy, R., Bowie, J. U., and Eisenberg, D. (1992) Assessment of protein models with three-dimensional profiles, Nature 356, 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 39
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • Rodriguez, R., Chinea, G., Lopez, N., Pons, T., and Vriend, G. (1998) Homology modeling, model and software evaluation: three related resources, Bioinformatics 14, 523-528.
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 41
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt, G. J., and Jones, T. A. (1994) Detection, delineation, measurement and display of cavities in macromolecular structures, Acta Crystallogr. D50, 178-185.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 42
    • 0025945775 scopus 로고
    • Proline residues in transmembrane helices: Structural or dynamic role?
    • Williams, K. A., and Deber, C. M. (1991) Proline residues in transmembrane helices: structural or dynamic role? Biochemistry 30, 8919-8923.
    • (1991) Biochemistry , vol.30 , pp. 8919-8923
    • Williams, K.A.1    Deber, C.M.2
  • 43
    • 0037136435 scopus 로고    scopus 로고
    • Genomic analysis of membrane protein families: Abundance and conserved motifs
    • Liu, Y., Engelman, D. M., and Gerstein, M. (2002) Genomic analysis of membrane protein families: abundance and conserved motifs, Genome Biol. 3, 1-12.
    • (2002) Genome Biol. , vol.3 , pp. 1-12
    • Liu, Y.1    Engelman, D.M.2    Gerstein, M.3
  • 44
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C., and Lesk, A. M. (1986) The relation between the divergence of sequence and structure in proteins, EMBO J. 5, 823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 45
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander, C., and Schneider, R. (1991) Database of homology-derived protein structures and the structural meaning of sequence alignment, Proteins 9, 56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 46
    • 0027485083 scopus 로고
    • Comparison of conformational characteristics in structurally similar protein pairs
    • Flores, T. P., Orengo, C. A., Moss, D. S., and Thornton, J. M. (1993) Comparison of conformational characteristics in structurally similar protein pairs, Protein Sci. 2, 1811-1826.
    • (1993) Protein Sci. , vol.2 , pp. 1811-1826
    • Flores, T.P.1    Orengo, C.A.2    Moss, D.S.3    Thornton, J.M.4
  • 48
    • 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
  • 50
    • 0037373068 scopus 로고    scopus 로고
    • Structural model for 12-helix transporters belonging to the major facilitator superfamily
    • Hirai, T., Heymann, J. A., Maloney, P. C., and Subramaniam, S. (2003) Structural model for 12-helix transporters belonging to the major facilitator superfamily, J. Bacteriol. 185, 1712-1718.
    • (2003) J. Bacteriol. , vol.185 , pp. 1712-1718
    • Hirai, T.1    Heymann, J.A.2    Maloney, P.C.3    Subramaniam, S.4
  • 51
    • 0023148307 scopus 로고
    • Mammalian and bacterial sugar transport proteins are homologous
    • Maiden, M. C., Davis, E. O., Baldwin, S. A., Moore, D. C., and Henderson, P. J. (1987) Mammalian and bacterial sugar transport proteins are homologous, Nature 325, 641-643.
    • (1987) Nature , vol.325 , pp. 641-643
    • Maiden, M.C.1    Davis, E.O.2    Baldwin, S.A.3    Moore, D.C.4    Henderson, P.J.5
  • 52
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi, A. J. (2000) Protein glucosylation and its role in protein folding, Annu. Rev. Biochem. 69, 69-93.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 53
    • 0035979713 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins: Determinants and dynamics
    • Goder, V., and Spiess, M. (2001) Topogenesis of membrane proteins: determinants and dynamics, FEBS Lett. 504, 87-93.
    • (2001) FEBS Lett. , vol.504 , pp. 87-93
    • Goder, V.1    Spiess, M.2
  • 54
    • 0031711820 scopus 로고    scopus 로고
    • Transporters of nucleotide sugars, ATP, and nucleotide sulfate in the endoplasmic reticulum and Golgi apparatus
    • 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.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 49-69
    • Hirschberg, C.B.1    Robbins, P.W.2    Abeijon, C.3
  • 56
    • 0037106481 scopus 로고    scopus 로고
    • The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70
    • Farinha, C. M., Nogueira, P., Mendes, F., Penque, D., and Amaral, M. D. (2002) The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70, Biochem. J. 366, 797-806.
    • (2002) Biochem. J. , vol.366 , pp. 797-806
    • Farinha, C.M.1    Nogueira, P.2    Mendes, F.3    Penque, D.4    Amaral, M.D.5
  • 59
    • 0000071066 scopus 로고    scopus 로고
    • Dissimilatory pathways for sugars, polyols and carboxylates
    • (Neidhardt, F. C., Curtiss, R. I., Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M., and Umbarger, H. E., Eds.), ASM Press, Washington, DC
    • Lin, E. C. C. (1996) Dissimilatory pathways for sugars, polyols and carboxylates, in Escheriachia coli and Salmonella: Cellular and Molecular Biology (Neidhardt, F. C., Curtiss, R. I., Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M., and Umbarger, H. E., Eds.) pp 307-342, ASM Press, Washington, DC.
    • (1996) Escheriachia Coli and Salmonella: Cellular and Molecular Biology , pp. 307-342
    • Lin, E.C.C.1
  • 61
    • 0034798447 scopus 로고    scopus 로고
    • Structural analysis of the GLUT1 facilitative glucose transporter
    • Hruz, P. W., and Mueckler, M. M. (2001) Structural analysis of the GLUT1 facilitative glucose transporter, Mol. Membr. Biol. 18, 183-193.
    • (2001) Mol. Membr. Biol. , vol.18 , pp. 183-193
    • Hruz, P.W.1    Mueckler, M.M.2
  • 62
    • 0032528196 scopus 로고    scopus 로고
    • Identification of two essential arginine residues in UhpT, the sugar phosphate antiporter of Escherichia coli
    • Fann, M., Davies, A. H., Varadhachary, A., Kuroda, T., Sevier, C., Tsuchiya, T., and Maloney, P. C. (1998) Identification of two essential arginine residues in UhpT, the sugar phosphate antiporter of Escherichia coli, J. Membr. Biol. 164, 187-195.
    • (1998) J. Membr. Biol. , vol.164 , pp. 187-195
    • Fann, M.1    Davies, A.H.2    Varadhachary, A.3    Kuroda, T.4    Sevier, C.5    Tsuchiya, T.6    Maloney, P.C.7
  • 63
    • 0742288411 scopus 로고    scopus 로고
    • The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors
    • Yohannan, S., Faham, S., Yang, D., Whitelegge, J. P., and Bowie, J. U. (2004) The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors, Proc. Natl. Acad. Sci. U.S.A. 101, 959-963.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 959-963
    • Yohannan, S.1    Faham, S.2    Yang, D.3    Whitelegge, J.P.4    Bowie, J.U.5
  • 64
    • 0035979146 scopus 로고    scopus 로고
    • The Cα-H⋯O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes, A., Ubarretxena-Belandia, I., and Engelman, D. M. (2001) The Cα-H⋯O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions, Proc. Natl. Acad. Sci. U.S.A. 98, 9056-9061.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 65
    • 0032509102 scopus 로고    scopus 로고
    • Proline-induced disruption of a transmembrane α-helix in its natural environment
    • Nilsson, I., Saaf, A., Whitley, P., Gafvelin, G., Waller, C., and von Heijne, G. (1998) Proline-induced disruption of a transmembrane α-helix in its natural environment, J. Mol. Biol. 284, 1165-1175.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1165-1175
    • Nilsson, I.1    Saaf, A.2    Whitley, P.3    Gafvelin, G.4    Waller, C.5    Von Heijne, G.6
  • 66
    • 0026670486 scopus 로고
    • Metaltetracycline/H+ antiporter of Escherichia coli encoded by transposon Tn10. The role of a conserved sequence motif, GXXXXRX-GRR, in a putative cytoplasmic loop between helices 2 and 3
    • Yamaguchi, A., Someya, Y., and Sawai, T. (1992) Metaltetracycline/H+ antiporter of Escherichia coli encoded by transposon Tn10. The role of a conserved sequence motif, GXXXXRX-GRR, in a putative cytoplasmic loop between helices 2 and 3, J. Biol. Chem. 267, 19155-19162.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19155-19162
    • Yamaguchi, A.1    Someya, Y.2    Sawai, T.3
  • 67
    • 0027460297 scopus 로고
    • Metal-tetracycline/H+ antiporter of Escherichia coli encoded by transposon Tn10. The structural resemblance and functional difference in the role of the duplicated sequence motif between hydrophobic segments 2 and 3 and segments 8 and 9
    • Yamaguchi, A., Kimura, T., Someya, Y., and Sawai, T. (1993) Metal-tetracycline/H+ antiporter of Escherichia coli encoded by transposon Tn10. The structural resemblance and functional difference in the role of the duplicated sequence motif between hydrophobic segments 2 and 3 and segments 8 and 9, J. Biol. Chem. 268, 6496-6504.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6496-6504
    • Yamaguchi, A.1    Kimura, T.2    Someya, Y.3    Sawai, T.4
  • 68
    • 0028999357 scopus 로고
    • The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in hydrophilic loop 2/3 of the lactose permease
    • Jessen-Marshall, A. E., Paul, N. J., and Brooker, R. J. (1995) The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in hydrophilic loop 2/3 of the lactose permease, J. Biol. Chem. 270, 16251-16257.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16251-16257
    • Jessen-Marshall, A.E.1    Paul, N.J.2    Brooker, R.J.3
  • 69
    • 0033609831 scopus 로고    scopus 로고
    • A conserved amino acid motif (R-X-G-R-R) in the Glut1 glucose transporter is an important determinant of membrane topology
    • Sato, M., and Mueckler, M. (1999) A conserved amino acid motif (R-X-G-R-R) in the Glut1 glucose transporter is an important determinant of membrane topology, J. Biol. Chem. 274, 24721-24725.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24721-24725
    • Sato, M.1    Mueckler, M.2
  • 70
    • 0033850218 scopus 로고    scopus 로고
    • Mutational analysis of GLUT1 (SLC2A1) in glut-1 deficiency syndrome
    • Wang, D., Kranz-Eble, P., and De Vivo, D. C. (2000) Mutational analysis of GLUT1 (SLC2A1) in glut-1 deficiency syndrome, Hum. Mutat. 16, 224-231.
    • (2000) Hum. Mutat. , vol.16 , pp. 224-231
    • Wang, D.1    Kranz-Eble, P.2    De Vivo, D.C.3
  • 71
    • 0034602172 scopus 로고    scopus 로고
    • Structural requirements for the stability and microsomal transport activity of the human glucose 6-phosphate transporter
    • Chen, L. Y., Lin, B., Pan, C. J., Hiraiwa, H., and Chou, J. Y. (2000) Structural requirements for the stability and microsomal transport activity of the human glucose 6-phosphate transporter, J. Biol. Chem. 275, 34280-34286.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34280-34286
    • Chen, L.Y.1    Lin, B.2    Pan, C.J.3    Hiraiwa, H.4    Chou, J.Y.5
  • 73
    • 0347988157 scopus 로고    scopus 로고
    • Destabilizing mutations promote membrane protein misfolding
    • Nagy, J. K., and Sanders, C. R. (2004) Destabilizing mutations promote membrane protein misfolding, Biochemistry 43, 19-25.
    • (2004) Biochemistry , vol.43 , pp. 19-25
    • Nagy, J.K.1    Sanders, C.R.2
  • 74
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • Guerois, R., Nielsen, J. E., and Serrano, L. (2002) Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations, J. Mol. Biol. 320, 369-387.
    • (2002) J. Mol. Biol. , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.