메뉴 건너뛰기




Volumn 396, Issue 5, 2010, Pages 1181-1196

Model-Guided Mutagenesis Drives Functional Studies of Human NHA2, Implicated in Hypertension

Author keywords

CPA; Mechanism; Model structure; Mutagenesis; NHA2

Indexed keywords

ANTIPORTER; PROTEIN CPA2; PROTEIN NHA2; SODIUM PROTON EXCHANGE PROTEIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 77649273913     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.12.055     Document Type: Article
Times cited : (44)

References (54)
  • 1
    • 1242272754 scopus 로고    scopus 로고
    • Diversity of the mammalian sodium/proton exchanger SLC9 gene family
    • Orlowski J., Grinstein S. Diversity of the mammalian sodium/proton exchanger SLC9 gene family. Pflugers Arch. 2004, 447:549-565.
    • (2004) Pflugers Arch. , vol.447 , pp. 549-565
    • Orlowski, J.1    Grinstein, S.2
  • 5
    • 36749019169 scopus 로고    scopus 로고
    • + antiporter sharing evolutionary origins with bacterial NhaA may be a candidate gene for essential hypertension
    • + antiporter sharing evolutionary origins with bacterial NhaA may be a candidate gene for essential hypertension. Proc. Natl Acad. Sci. USA 2007, 104:18677-18681.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 18677-18681
    • Xiang, M.1    Feng, M.2    Muend, S.3    Rao, R.4
  • 6
    • 0018834154 scopus 로고
    • Increased sodium-lithium countertransport in red cells of patients with essential hypertension
    • Canessa M., Adragna N., Solomon H.S., Connolly T.M., Tosteson D.C. Increased sodium-lithium countertransport in red cells of patients with essential hypertension. N. Engl. J. Med. 1980, 302:772-776.
    • (1980) N. Engl. J. Med. , vol.302 , pp. 772-776
    • Canessa, M.1    Adragna, N.2    Solomon, H.S.3    Connolly, T.M.4    Tosteson, D.C.5
  • 10
    • 66249098083 scopus 로고    scopus 로고
    • Unlocking the molecular secrets of sodium-coupled transporters
    • Krishnamurthy H., Piscitelli C.L., Gouaux E. Unlocking the molecular secrets of sodium-coupled transporters. Nature 2009, 459:347-355.
    • (2009) Nature , vol.459 , pp. 347-355
    • Krishnamurthy, H.1    Piscitelli, C.L.2    Gouaux, E.3
  • 12
    • 33745714411 scopus 로고    scopus 로고
    • On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins
    • Forrest L.R., Tang C.L., Honig B. On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins. Biophys. J. 2006, 91:508-517.
    • (2006) Biophys. J. , vol.91 , pp. 508-517
    • Forrest, L.R.1    Tang, C.L.2    Honig, B.3
  • 13
  • 18
    • 0033654768 scopus 로고    scopus 로고
    • Hybrid fold recognition: combining sequence derived properties with evolutionary information
    • Fischer D. Hybrid fold recognition: combining sequence derived properties with evolutionary information. Pac. Symp. Biocomput. 2000, 119-130.
    • (2000) Pac. Symp. Biocomput. , pp. 119-130
    • Fischer, D.1
  • 19
    • 0344873345 scopus 로고    scopus 로고
    • On the role of structural information in remote homology detection and sequence alignment: new methods using hybrid sequence profiles
    • Tang C.L., Xie L., Koh I.Y., Posy S., Alexov E., Honig B. On the role of structural information in remote homology detection and sequence alignment: new methods using hybrid sequence profiles. J. Mol. Biol. 2003, 334:1043-1062.
    • (2003) J. Mol. Biol. , vol.334 , pp. 1043-1062
    • Tang, C.L.1    Xie, L.2    Koh, I.Y.3    Posy, S.4    Alexov, E.5    Honig, B.6
  • 20
    • 35448950945 scopus 로고    scopus 로고
    • Free energy determinants of peptide association with lipid bilayers
    • Kessel A., Ben-Tal N. Free energy determinants of peptide association with lipid bilayers. Curr. Top. Membr. 2002, 52:205-253.
    • (2002) Curr. Top. Membr. , vol.52 , pp. 205-253
    • Kessel, A.1    Ben-Tal, N.2
  • 21
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady G.E., Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics 2001, 17:849-850.
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 22
    • 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., Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 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
  • 23
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 1999, 292:195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 25
    • 34249683488 scopus 로고    scopus 로고
    • Membrane protein structure: prediction versus reality
    • Elofsson A., von Heijne G. Membrane protein structure: prediction versus reality. Annu. Rev. Biochem. 2007, 76:125-140.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 125-140
    • Elofsson, A.1    von Heijne, G.2
  • 27
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • Heijne G.V. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 1986, 5:3021-3027.
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Heijne, G.V.1
  • 28
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 1998, 7:1029-1038.
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 29
    • 33746586953 scopus 로고    scopus 로고
    • Progress in structure prediction of alpha-helical membrane proteins
    • Fleishman S.J., Ben-Tal N. Progress in structure prediction of alpha-helical membrane proteins. Curr. Opin. Struct. Biol. 2006, 16:496-504.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 496-504
    • Fleishman, S.J.1    Ben-Tal, N.2
  • 30
    • 13144249178 scopus 로고    scopus 로고
    • Physiological characterization of Saccharomyces cerevisiae kha1 deletion mutants
    • Maresova L., Sychrova H. Physiological characterization of Saccharomyces cerevisiae kha1 deletion mutants. Mol. Microbiol. 2005, 55:588-600.
    • (2005) Mol. Microbiol. , vol.55 , pp. 588-600
    • Maresova, L.1    Sychrova, H.2
  • 32
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie J.U. Solving the membrane protein folding problem. Nature 2005, 438:581-589.
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 36
    • 68049148763 scopus 로고    scopus 로고
    • Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli
    • Olkhova E., Kozachkov L., Padan E., Michel H. Combined computational and biochemical study reveals the importance of electrostatic interactions between the "pH sensor" and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli. Proteins: Struct., Funct., Bioinf. 2009, 76:548-559.
    • (2009) Proteins: Struct., Funct., Bioinf. , vol.76 , pp. 548-559
    • Olkhova, E.1    Kozachkov, L.2    Padan, E.3    Michel, H.4
  • 39
    • 0032500509 scopus 로고    scopus 로고
    • + antiporter as well as the growth phenotype of Escherichia coli
    • + antiporter as well as the growth phenotype of Escherichia coli. J. Biol. Chem. 1998, 273:26470-26476.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26470-26476
    • Rimon, A.1    Gerchman, Y.2    Kariv, Z.3    Padan, E.4
  • 41
    • 0030809240 scopus 로고    scopus 로고
    • + in the c subunit of the ATP synthase from Propionigenium modestum
    • + in the c subunit of the ATP synthase from Propionigenium modestum. Biochemistry 1997, 36:9185-9194.
    • (1997) Biochemistry , vol.36 , pp. 9185-9194
    • Kaim, G.1    Wehrle, F.2    Gerike, U.3    Dimroth, P.4
  • 46
    • 33747184794 scopus 로고    scopus 로고
    • Prediction of transmembrane helix orientation in polytopic membrane proteins
    • Adamian L., Liang J. Prediction of transmembrane helix orientation in polytopic membrane proteins. BMC Struct. Biol. 2006, 6:13.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 13
    • Adamian, L.1    Liang, J.2
  • 47
    • 0027497369 scopus 로고
    • Modeling alpha-helical transmembrane domains: the calculation and use of substitution tables for lipid-facing residues
    • Donnelly D., Overington J.P., Ruffle S.V., Nugent J.H., Blundell T.L. Modeling alpha-helical transmembrane domains: the calculation and use of substitution tables for lipid-facing residues. Protein Sci. 1993, 2:55-70.
    • (1993) Protein Sci. , vol.2 , pp. 55-70
    • Donnelly, D.1    Overington, J.P.2    Ruffle, S.V.3    Nugent, J.H.4    Blundell, T.L.5
  • 48
    • 4644273133 scopus 로고    scopus 로고
    • An automatic method for predicting transmembrane protein structures using cryo-EM and evolutionary data
    • Fleishman S.J., Harrington S., Friesner R.A., Honig B., Ben-Tal N. An automatic method for predicting transmembrane protein structures using cryo-EM and evolutionary data. Biophys. J. 2004, 87:3448-3459.
    • (2004) Biophys. J. , vol.87 , pp. 3448-3459
    • Fleishman, S.J.1    Harrington, S.2    Friesner, R.A.3    Honig, B.4    Ben-Tal, N.5
  • 49
    • 0035182559 scopus 로고    scopus 로고
    • Substitution rates in alpha-helical transmembrane proteins
    • Stevens T.J., Arkin I.T. Substitution rates in alpha-helical transmembrane proteins. Protein Sci. 2001, 10:2507-2517.
    • (2001) Protein Sci. , vol.10 , pp. 2507-2517
    • Stevens, T.J.1    Arkin, I.T.2
  • 50
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity
    • Edgar R.C. MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinf. 2004, 5:113.
    • (2004) BMC Bioinf. , vol.5 , pp. 113
    • Edgar, R.C.1
  • 51
    • 18844426792 scopus 로고    scopus 로고
    • Site-specific evolutionary rate inference: taking phylogenetic uncertainty into account
    • Mayrose I., Mitchell A., Pupko T. Site-specific evolutionary rate inference: taking phylogenetic uncertainty into account. J. Mol. Evol. 2005, 60:345-353.
    • (2005) J. Mol. Evol. , vol.60 , pp. 345-353
    • Mayrose, I.1    Mitchell, A.2    Pupko, T.3
  • 52
    • 10744220076 scopus 로고    scopus 로고
    • Using multiple structure alignments, fast model building, and energetic analysis in fold recognition and homology modeling
    • Petrey D., Xiang Z., Tang C.L., Xie L., Gimpelev M., Mitros T., et al. Using multiple structure alignments, fast model building, and energetic analysis in fold recognition and homology modeling. Proteins 2003, 53:430-435.
    • (2003) Proteins , vol.53 , pp. 430-435
    • Petrey, D.1    Xiang, Z.2    Tang, C.L.3    Xie, L.4    Gimpelev, M.5    Mitros, T.6
  • 53
    • 0021143010 scopus 로고
    • Dual system for potassium transport in Saccharomyces cerevisiae
    • Rodriguez-Navarro A., Ramos J. Dual system for potassium transport in Saccharomyces cerevisiae. J. Bacteriol. 1984, 159:940-945.
    • (1984) J. Bacteriol. , vol.159 , pp. 940-945
    • Rodriguez-Navarro, A.1    Ramos, J.2
  • 54
    • 0028607143 scopus 로고
    • Regulated degradation of the transcription factor Gcn4
    • Kornitzer D., Raboy B., Kulka R.G., Fink G.R. Regulated degradation of the transcription factor Gcn4. EMBO J. 1994, 13:6021-6030.
    • (1994) EMBO J. , vol.13 , pp. 6021-6030
    • Kornitzer, D.1    Raboy, B.2    Kulka, R.G.3    Fink, G.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.