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Volumn 5, Issue 10, 2009, Pages

Integration of evolutionary features for the identification of functionally important residues in major facilitator superfamily transporters

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; COOPERATIVE COMMUNICATION; SUBSTRATES;

EID: 73549113828     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000522     Document Type: Article
Times cited : (16)

References (73)
  • 1
    • 38049148291 scopus 로고    scopus 로고
    • Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel
    • Sadovsky E, Yifrach O (2007) Principles underlying energetic coupling along an allosteric communication trajectory of a voltage-activated K+ channel. Proc Natl Acad Sci U S A 104: 19813-19818.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19813-19818
    • Sadovsky, E.1    Yifrach, O.2
  • 2
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: An algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T, Bell RE, Mayrose I, Glaser F, Ben-Tal N (2002) Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues. Bioinformatics 18 Suppl 1: S71-77.
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 3
    • 34548133728 scopus 로고    scopus 로고
    • Predicting functionally important residues from sequence conservation
    • Capra JA, Singh M (2007) Predicting functionally important residues from sequence conservation. Bioinformatics 23: 1875-1882.
    • (2007) Bioinformatics , vol.23 , pp. 1875-1882
    • Capra, J.A.1    Singh, M.2
  • 4
    • 33747150197 scopus 로고    scopus 로고
    • Protein binding site prediction using an empirical scoring function
    • Liang S, Zhang C, Liu S, Zhou Y (2006) Protein binding site prediction using an empirical scoring function. Nucleic Acids Res 34: 3698-3707.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3698-3707
    • Liang, S.1    Zhang, C.2    Liu, S.3    Zhou, Y.4
  • 6
    • 0042674397 scopus 로고    scopus 로고
    • Using a neural network and spatial clustering to predict the location of active sites in enzymes
    • Gutteridge A, Bartlett GJ, Thornton JM (2003) Using a neural network and spatial clustering to predict the location of active sites in enzymes. J Mol Biol 330: 719-734.
    • (2003) J Mol Biol , vol.330 , pp. 719-734
    • Gutteridge, A.1    Bartlett, G.J.2    Thornton, J.M.3
  • 7
    • 0034644783 scopus 로고    scopus 로고
    • Analysis and prediction of functional subtypes from protein sequence alignments
    • Hannenhalli SS, Russell RB (2000) Analysis and prediction of functional subtypes from protein sequence alignments. J Mol Biol 303: 61-76.
    • (2000) J Mol Biol , vol.303 , pp. 61-76
    • Hannenhalli, S.S.1    Russell, R.B.2
  • 8
  • 9
    • 36949019322 scopus 로고    scopus 로고
    • Detecting coevolution in and among protein domains
    • Yeang CH, Haussler D (2007) Detecting coevolution in and among protein domains. PLoS Comput Biol 3: e211.
    • (2007) PLoS Comput Biol , vol.3
    • Yeang, C.H.1    Haussler, D.2
  • 11
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless SW, Ranganathan R (1999) Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286: 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 13
    • 2442498470 scopus 로고    scopus 로고
    • On evolutionary conservation of thermodynamic coupling in proteins
    • Fodor AA, Aldrich RW (2004) On evolutionary conservation of thermodynamic coupling in proteins. J Biol Chem 279: 19046-19050.
    • (2004) J Biol Chem , vol.279 , pp. 19046-19050
    • Fodor, A.A.1    Aldrich, R.W.2
  • 14
    • 21444449871 scopus 로고    scopus 로고
    • FSSA: A novel method for identifying functional signatures from structural alignments
    • Wang K, Samudrala R (2005) FSSA: a novel method for identifying functional signatures from structural alignments. Bioinformatics 21: 2969-2977.
    • (2005) Bioinformatics , vol.21 , pp. 2969-2977
    • Wang, K.1    Samudrala, R.2
  • 15
    • 33746592898 scopus 로고    scopus 로고
    • Knowledge-based potentials in protein design
    • Poole AM, Ranganathan R (2006) Knowledge-based potentials in protein design. Curr Opin Struct Biol 16: 508-513.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 508-513
    • Poole, A.M.1    Ranganathan, R.2
  • 16
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey NM, Benkovic SJ (2008) Allosteric regulation and catalysis emerge via a common route. Nat Chem Biol 4: 474-482.
    • (2008) Nat Chem Biol , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 17
    • 35148894521 scopus 로고    scopus 로고
    • Predicting allosteric communication in myosin via a pathway of conserved residues
    • Tang S, Liao JC, Dunn AR, Altman RB, Spudich JA, et al. (2007) Predicting allosteric communication in myosin via a pathway of conserved residues. J Mol Biol 373: 1361-1373.
    • (2007) J Mol Biol , vol.373 , pp. 1361-1373
    • Tang, S.1    Liao, J.C.2    Dunn, A.R.3    Altman, R.B.4    Spudich, J.A.5
  • 18
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel GM, Lockless SW, Wall MA, Ranganathan R (2003) Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 10: 59-69.
    • (2003) Nat Struct Biol , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 21
    • 4143061717 scopus 로고    scopus 로고
    • Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: Members of the major facilitator superfamily
    • Abramson J, Kaback HR, Iwata S (2004) Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: members of the major facilitator superfamily. Curr Opin Struct Biol 14: 413-419.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 413-419
    • Abramson, J.1    Kaback, H.R.2    Iwata, S.3
  • 22
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, et al. (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
  • 23
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y, Lemieux MJ, Song J, Auer M, Wang DN (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
  • 24
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin Y, He X, Szewczyk P, Nguyen T, 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
  • 25
    • 0042430540 scopus 로고    scopus 로고
    • Multidrug-exporting secondary transporters
    • Murakami S, Yamaguchi A (2003) Multidrug-exporting secondary transporters. Curr Opin Struct Biol 13: 443-452.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 443-452
    • Murakami, S.1    Yamaguchi, A.2
  • 26
    • 23344451687 scopus 로고    scopus 로고
    • Structure, function, and evolution of transient and obligate protein-protein interactions
    • Mintseris J, Weng Z (2005) Structure, function, and evolution of transient and obligate protein-protein interactions. Proc Natl Acad Sci U S A 102: 10930-10935.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10930-10935
    • Mintseris, J.1    Weng, Z.2
  • 28
    • 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, Kaback HR (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
  • 29
    • 33745461893 scopus 로고    scopus 로고
    • Residues crucial for maintaining short paths in network communication mediate signaling in proteins
    • del Sol A, Fujihashi H, Amoros D, Nussinov R (2006) Residues crucial for maintaining short paths in network communication mediate signaling in proteins. Mol Syst Biol 2: 2006 0019.
    • (2006) Mol Syst Biol , vol.2 , pp. 0019
    • del Sol, A.1    Fujihashi, H.2    Amoros, D.3    Nussinov, R.4
  • 30
    • 0026757193 scopus 로고
    • Possible salt bridges between transmembrane alpha-helices of the lactose carrier of Escherichia coli
    • Lee JI, Hwang PP, Hansen C, Wilson TH (1992) Possible salt bridges between transmembrane alpha-helices of the lactose carrier of Escherichia coli. J Biol Chem 267: 20758-20764.
    • (1992) J Biol Chem , vol.267 , pp. 20758-20764
    • Lee, J.I.1    Hwang, P.P.2    Hansen, C.3    Wilson, T.H.4
  • 31
    • 4444328639 scopus 로고    scopus 로고
    • Lactose permease as a paradigm for membrane transport proteins (Review)
    • Abramson J, Iwata S, Kaback HR (2004) Lactose permease as a paradigm for membrane transport proteins (Review). Mol Membr Biol 21: 227-236.
    • (2004) Mol Membr Biol , vol.21 , pp. 227-236
    • Abramson, J.1    Iwata, S.2    Kaback, H.R.3
  • 33
    • 0034609514 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix X
    • Venkatesan P, Hu Y, Kaback HR (2000) Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix X. Biochemistry 39: 10656-10661.
    • (2000) Biochemistry , vol.39 , pp. 10656-10661
    • Venkatesan, P.1    Hu, Y.2    Kaback, H.R.3
  • 34
    • 0031056670 scopus 로고    scopus 로고
    • The role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis
    • Frillingos S, Ujwal ML, Sun J, Kaback HR (1997) The role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis. Protein Sci 6: 431-437.
    • (1997) Protein Sci , vol.6 , pp. 431-437
    • Frillingos, S.1    Ujwal, M.L.2    Sun, J.3    Kaback, H.R.4
  • 35
    • 33745045462 scopus 로고    scopus 로고
    • Conservation of residues involved in sugar/H(+) symport by the sucrose permease of Escherichia coli relative to lactose permease
    • Vadyvaloo V, Smirnova IN, Kasho VN, Kaback HR (2006) Conservation of residues involved in sugar/H(+) symport by the sucrose permease of Escherichia coli relative to lactose permease. J Mol Biol 358: 1051-1059.
    • (2006) J Mol Biol , vol.358 , pp. 1051-1059
    • Vadyvaloo, V.1    Smirnova, I.N.2    Kasho, V.N.3    Kaback, H.R.4
  • 36
    • 34248194465 scopus 로고    scopus 로고
    • Lactose permease H+-lactose symporter: Mechanical switch or Brownian ratchet?
    • Naftalin RJ, Green N, Cunningham P (2007) Lactose permease H+-lactose symporter: mechanical switch or Brownian ratchet? Biophys J 92: 3474-3491.
    • (2007) Biophys J , vol.92 , pp. 3474-3491
    • Naftalin, R.J.1    Green, N.2    Cunningham, P.3
  • 37
    • 0032492717 scopus 로고    scopus 로고
    • Proximity of helices VIII (Ala273) and IX (Met299) in the lactose permease of Escherichia coli
    • Wang Q, Voss J, Hubbell WL, Kaback HR (1998) Proximity of helices VIII (Ala273) and IX (Met299) in the lactose permease of Escherichia coli. Biochemistry 37: 4910-4915.
    • (1998) Biochemistry , vol.37 , pp. 4910-4915
    • Wang, Q.1    Voss, J.2    Hubbell, W.L.3    Kaback, H.R.4
  • 38
    • 4143072800 scopus 로고    scopus 로고
    • The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily
    • Lemieux MJ, Huang Y, Wang DN (2004) The structural basis of substrate translocation by the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily. Curr Opin Struct Biol 14: 405-412.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 405-412
    • Lemieux, M.J.1    Huang, Y.2    Wang, D.N.3
  • 39
    • 53849119555 scopus 로고    scopus 로고
    • Ins and outs of major facilitator superfamily antiporters
    • Law CJ, Maloney PC, Wang DN (2008) Ins and outs of major facilitator superfamily antiporters. Annu Rev Microbiol 62: 289-305.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 289-305
    • Law, C.J.1    Maloney, P.C.2    Wang, D.N.3
  • 42
    • 2942580743 scopus 로고    scopus 로고
    • An evolutionarily conserved network of amino acids mediates gating in voltage-dependent potassium channels
    • Fleishman SJ, Yifrach O, Ben-Tal N (2004) An evolutionarily conserved network of amino acids mediates gating in voltage-dependent potassium channels. J Mol Biol 340: 307-318.
    • (2004) J Mol Biol , vol.340 , pp. 307-318
    • Fleishman, S.J.1    Yifrach, O.2    Ben-Tal, N.3
  • 43
    • 33644873454 scopus 로고    scopus 로고
    • TCDB: The Transporter Classification Database for membrane transport protein analyses and information
    • Saier MH, Jr, Tran CV, Barabote RD (2006) TCDB: the Transporter Classification Database for membrane transport protein analyses and information. Nucleic Acids Res 34: D181-186.
    • (2006) Nucleic Acids Res , vol.34
    • Saier Jr, M.H.1    Tran, C.V.2    Barabote, R.D.3
  • 44
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution
    • Kolbe M, Besir H, Essen LO, Oesterhelt D (2000) Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution. Science 288: 1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 45
    • 47249110343 scopus 로고    scopus 로고
    • Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter
    • Gerber S, Comellas-Bigler M, Goetz BA, Locher KP (2008) Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321: 246-250.
    • (2008) Science , vol.321 , pp. 246-250
    • Gerber, S.1    Comellas-Bigler, M.2    Goetz, B.A.3    Locher, K.P.4
  • 46
    • 0038076054 scopus 로고    scopus 로고
    • X-ray structure of a voltage-dependent K+ channel
    • Jiang Y, Lee A, Chen J, Ruta V, Cadene M, et al. (2003) X-ray structure of a voltage-dependent K+ channel. Nature 423: 33-41.
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Ruta, V.4    Cadene, M.5
  • 47
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima C, Nomura H, Tsuda T (2004) Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432: 361-368.
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 48
    • 73549122924 scopus 로고    scopus 로고
    • Devos DM, E. Pazos, F. Valencia, A (2002) Multiple Sequence Alignments Information in Structure and Function Prediction: IOS Press publishers. pp 83-94.
    • Devos DM, E. Pazos, F. Valencia, A (2002) Multiple Sequence Alignments Information in Structure and Function Prediction: IOS Press publishers. pp 83-94.
  • 49
    • 0001895697 scopus 로고
    • Evolutionary divergence and convergence in proteins
    • New York: Evolving genes and proteins Academic Press. pp
    • Zuckerkandl EaP, L (1965) Evolutionary divergence and convergence in proteins. In: Evolving genes and proteins. New York: Evolving genes and proteins Academic Press. pp 97-166.
    • (1965) Evolving genes and proteins , pp. 97-166
    • Zuckerkandl EaP, L.1
  • 50
    • 41949130566 scopus 로고    scopus 로고
    • Salt-bridge dynamics control substrate-induced conformational change in the membrane transporter GlpT
    • Law CJ, Almqvist J, Bernstein A, Goetz RM, Huang Y, et al. (2008) Salt-bridge dynamics control substrate-induced conformational change in the membrane transporter GlpT. J Mol Biol 378: 828-839.
    • (2008) J Mol Biol , vol.378 , pp. 828-839
    • Law, C.J.1    Almqvist, J.2    Bernstein, A.3    Goetz, R.M.4    Huang, Y.5
  • 51
    • 50149112602 scopus 로고    scopus 로고
    • Direct analysis of cooperativity in multisubunit allosteric proteins
    • Zandany N, Ovadia M, Orr I, Yifrach O (2008) Direct analysis of cooperativity in multisubunit allosteric proteins. Proc Natl Acad Sci U S A 105: 11697-11702.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11697-11702
    • Zandany, N.1    Ovadia, M.2    Orr, I.3    Yifrach, O.4
  • 52
    • 0029877893 scopus 로고    scopus 로고
    • Inter-ring communication is disrupted in the GroEL mutant Arg13RGly; Ala126RVal with known crystal structure
    • Aharoni A, Horovitz A (1996) Inter-ring communication is disrupted in the GroEL mutant Arg13RGly; Ala126RVal with known crystal structure. J Mol Biol 258: 732-735.
    • (1996) J Mol Biol , vol.258 , pp. 732-735
    • Aharoni, A.1    Horovitz, A.2
  • 53
    • 0027314946 scopus 로고
    • The N terminus of the molecular chaperonin GroEL is a crucial structural element for its assembly
    • Horovitz A, Bochkareva ES, Girshovich AS (1993) The N terminus of the molecular chaperonin GroEL is a crucial structural element for its assembly. J Biol Chem 268: 9957-9959.
    • (1993) J Biol Chem , vol.268 , pp. 9957-9959
    • Horovitz, A.1    Bochkareva, E.S.2    Girshovich, A.S.3
  • 54
    • 34548815693 scopus 로고    scopus 로고
    • Modular architecture of protein structures and allosteric communications: Potential implications for signaling proteins and regulatory linkages
    • Del Sol A, Arauzo-Bravo MJ, Amoros D, Nussinov R (2007) Modular architecture of protein structures and allosteric communications: potential implications for signaling proteins and regulatory linkages. Genome Biol 8: R92.
    • (2007) Genome Biol , vol.8
    • Del Sol, A.1    Arauzo-Bravo, M.J.2    Amoros, D.3    Nussinov, R.4
  • 55
    • 0037076369 scopus 로고    scopus 로고
    • Changing the lactose permease of Escherichia coli into a galactose-specific symporter
    • Guan L, Sahin-Toth M, Kaback HR (2002) Changing the lactose permease of Escherichia coli into a galactose-specific symporter. Proc Natl Acad Sci U S A 99: 6613-6618.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 6613-6618
    • Guan, L.1    Sahin-Toth, M.2    Kaback, H.R.3
  • 56
    • 33645320817 scopus 로고    scopus 로고
    • Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY
    • Mirza O, Guan L, Verner G, Iwata S, Kaback HR (2006) Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY. EMBO J 25: 1177-1183.
    • (2006) EMBO J , vol.25 , pp. 1177-1183
    • Mirza, O.1    Guan, L.2    Verner, G.3    Iwata, S.4    Kaback, H.R.5
  • 57
    • 33748499821 scopus 로고    scopus 로고
    • Promiscuity in multidrug recognition and transport: The bacterial MFS Mdr transporters
    • Lewinson O, Adler J, Sigal N, Bibi E (2006) Promiscuity in multidrug recognition and transport: the bacterial MFS Mdr transporters. Mol Microbiol 61: 277-284.
    • (2006) Mol Microbiol , vol.61 , pp. 277-284
    • Lewinson, O.1    Adler, J.2    Sigal, N.3    Bibi, E.4
  • 58
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 59
    • 3042681902 scopus 로고    scopus 로고
    • ConSeq: The identification of functionally and structurally important residues in protein sequences
    • Berezin C, Glaser F, Rosenberg J, Paz I, Pupko T, et al. (2004) ConSeq: the identification of functionally and structurally important residues in protein sequences. Bioinformatics 20: 1322-1324.
    • (2004) Bioinformatics , vol.20 , pp. 1322-1324
    • Berezin, C.1    Glaser, F.2    Rosenberg, J.3    Paz, I.4    Pupko, T.5
  • 60
    • 0033550256 scopus 로고    scopus 로고
    • Effective use of sequence correlation and conservation in fold recognition
    • Olmea O, Rost B, Valencia A (1999) Effective use of sequence correlation and conservation in fold recognition. J Mol Biol 293: 1221-1239.
    • (1999) J Mol Biol , vol.293 , pp. 1221-1239
    • Olmea, O.1    Rost, B.2    Valencia, A.3
  • 61
    • 3543089710 scopus 로고    scopus 로고
    • A perturbation-based method for calculating explicit likelihood of evolutionary co-variance in multiple sequence alignments
    • Dekker JP, Fodor A, Aldrich RW, Yellen G (2004) A perturbation-based method for calculating explicit likelihood of evolutionary co-variance in multiple sequence alignments. Bioinformatics 20: 1565-1572.
    • (2004) Bioinformatics , vol.20 , pp. 1565-1572
    • Dekker, J.P.1    Fodor, A.2    Aldrich, R.W.3    Yellen, G.4
  • 63
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt GJ, Jones TA (1994) Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr D Biol Crystallogr 50: 178-185.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 64
    • 34247891656 scopus 로고    scopus 로고
    • Controlling the false-positive rate in multilocus genome scans for selection
    • Thornton KR, Jensen JD (2007) Controlling the false-positive rate in multilocus genome scans for selection. Genetics 175: 737-750.
    • (2007) Genetics , vol.175 , pp. 737-750
    • Thornton, K.R.1    Jensen, J.D.2
  • 65
    • 13444280419 scopus 로고    scopus 로고
    • PDB-TM: Selection and membrane localization of transmembrane proteins in the protein data bank
    • Tusnady GE, Dosztanyi Z, Simon I (2005) PDB-TM: selection and membrane localization of transmembrane proteins in the protein data bank. Nucleic Acids Res 33: D275-278.
    • (2005) Nucleic Acids Res , vol.33
    • Tusnady, G.E.1    Dosztanyi, Z.2    Simon, I.3
  • 67
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D, Tsai CJ, Nussinov R (1997) Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng 10: 999-1012.
    • (1997) Protein Eng , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 68
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM (1994) Satisfying hydrogen bonding potential in proteins. J Mol Biol 238: 777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 70
    • 0028574138 scopus 로고
    • The role of transmembrane domain III in the lactose permease of Escherichia coli
    • Sahin-Toth M, Frillingos S, Bibi E, Gonzalez A, Kaback HR (1994) The role of transmembrane domain III in the lactose permease of Escherichia coli. Protein Sci 3: 2302-2310.
    • (1994) Protein Sci , vol.3 , pp. 2302-2310
    • Sahin-Toth, M.1    Frillingos, S.2    Bibi, E.3    Gonzalez, A.4    Kaback, H.R.5
  • 71
    • 33645537372 scopus 로고    scopus 로고
    • Ermolova N, Madhvani RV, Kaback HR (2006) Site-directed alkylation of cysteine replacements in the lactose permease of Escherichia coli: helices I, III, VI, and XI. Biochemistry 45: 4182-4189.
    • Ermolova N, Madhvani RV, Kaback HR (2006) Site-directed alkylation of cysteine replacements in the lactose permease of Escherichia coli: helices I, III, VI, and XI. Biochemistry 45: 4182-4189.
  • 72
    • 0034609555 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix VII
    • Venkatesan P, Kwaw I, Hu Y, Kaback HR (2000) Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: helix VII. Biochemistry 39: 10641-10648.
    • (2000) Biochemistry , vol.39 , pp. 10641-10648
    • Venkatesan, P.1    Kwaw, I.2    Hu, Y.3    Kaback, H.R.4
  • 73
    • 0024368803 scopus 로고
    • A five-residue sequence near the carboxyl terminus of the polytopic membrane protein lac permease is required for stability within the membrane
    • Roepe PD, Zbar RI, Sarkar HK, Kaback HR (1989) A five-residue sequence near the carboxyl terminus of the polytopic membrane protein lac permease is required for stability within the membrane. Proc Natl Acad Sci U S A 86: 3992-3996.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 3992-3996
    • Roepe, P.D.1    Zbar, R.I.2    Sarkar, H.K.3    Kaback, H.R.4


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