메뉴 건너뛰기




Volumn 1814, Issue 12, 2011, Pages 1854-1861

Molecular evolution and selection pressure in alpha-class carbonic anhydrase family members

Author keywords

Carbonic anhydrase; Molecular evolution; Negative selection; Protein interaction

Indexed keywords

AMINO ACID; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE I; CARBONATE DEHYDRATASE II; CARBONATE DEHYDRATASE III; CARBONATE DEHYDRATASE IV; CARBONATE DEHYDRATASE IX; CARBONATE DEHYDRATASE V; CARBONATE DEHYDRATASE VA; CARBONATE DEHYDRATASE VB; CARBONATE DEHYDRATASE VI; CARBONATE DEHYDRATASE XII; CARBONATE DEHYDRATASE XIII; CARBONATE DEHYDRATASE XIV; CARBONATE DEHYDRATASE XV; CARBONIC ANHYDRASE ALPHA; CARBONIC ANHYDRASE RELATED PROTEIN VIII; CARBONIC ANHYDRASE RELATED PROTEIN X; CARBONIC ANHYDRASE RELATED PROTEIN XI; HISTIDINE DERIVATIVE; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE G; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE Z1; UNCLASSIFIED DRUG; ZINC BINDING PROTEIN; ZINC COFACTOR;

EID: 81755179391     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.07.007     Document Type: Article
Times cited : (7)

References (77)
  • 1
    • 0030076314 scopus 로고    scopus 로고
    • Functional diversity, conservation, and convergence in the evolution of the α-, β-, and γ-carbonic anhydrase gene families
    • DOI 10.1006/mpev.1996.0006
    • D. Hewett-Emmett, and R.E. Tashian Functional diversity, conservation, and convergence in the evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene families Mol. Phylogenet. Evol. 5 1996 50 77 (Pubitemid 126316997)
    • (1996) Molecular Phylogenetics and Evolution , vol.5 , Issue.1 , pp. 50-77
    • Hewett-Emmett, D.1    Tashian, R.E.2
  • 2
    • 0029874435 scopus 로고    scopus 로고
    • A left-handed β-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila
    • C. Kisker, H. Schindelin, B.E. Alber, J.G. Ferry, and D.C. Rees A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila EMBO J. 15 1996 2323 2330 (Pubitemid 26151173)
    • (1996) EMBO Journal , vol.15 , Issue.10 , pp. 2323-2330
    • Kisker, C.1    Schindelin, H.2    Alber, B.E.3    Ferry, J.G.4    Rees, D.C.5
  • 3
    • 74449089655 scopus 로고    scopus 로고
    • The gamma class of carbonic anhydrases
    • J.G. Ferry The gamma class of carbonic anhydrases Biochim. Biophys. Acta 1804 2010 374 381
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 374-381
    • Ferry, J.G.1
  • 6
    • 40449131050 scopus 로고    scopus 로고
    • Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms
    • DOI 10.1038/nature06636, PII NATURE06636
    • Y. Xu, L. Feng, P.D. Jeffrey, Y. Shi, and F.M. Morel Structure and metal exchange in the cadmium carbonic anhydrase of marine diatoms Nature 452 2008 56 61 (Pubitemid 351355092)
    • (2008) Nature , vol.452 , Issue.7183 , pp. 56-61
    • Xu, Y.1    Feng, L.2    Jeffrey, P.D.3    Shi, Y.4    Morel, F.M.M.5
  • 11
    • 0032535186 scopus 로고    scopus 로고
    • Evolutionarily conserved, 'acatalytic' carbonic anhydrase-related protein XI contains a sequence motif present in the neuropeptide sauvagine: The human CA-RP XI gene (CA11) is embedded between the secretor gene cluster and the DBP gene at 19q13.3
    • DOI 10.1006/geno.1998.5585
    • D.A. Lovejoy, D. Hewett-Emmett, C.A. Porter, D. Cepoi, A. Sheffield, W.W. Vale, and R.E. Tashian Evolutionarily conserved, "acatalytic" carbonic anhydrase-related protein XI contains a sequence motif present in the neuropeptide sauvagine: the human CA-RP XI gene (CA11) is embedded between the secretor gene cluster and the DBP gene at 19q13.3 Genomics 54 1998 484 493 (Pubitemid 29036236)
    • (1998) Genomics , vol.54 , Issue.3 , pp. 484-493
    • Lovejoy, D.A.1    Hewett-Emmett, D.2    Porter, C.A.3    Cepoi, D.4    Sheffield, A.5    Vale, W.W.6    Tashian, R.E.7
  • 12
    • 77950390973 scopus 로고    scopus 로고
    • Phylogeny and expression of carbonic anhydrase-related proteins
    • A. Aspatwar, M.E. Tolvanen, and S. Parkkila Phylogeny and expression of carbonic anhydrase-related proteins BMC Mol. Biol. 11 2010 25
    • (2010) BMC Mol. Biol. , vol.11 , pp. 25
    • Aspatwar, A.1    Tolvanen, M.E.2    Parkkila, S.3
  • 13
    • 77249161681 scopus 로고    scopus 로고
    • The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules
    • S. Bouyain, and D.J. Watkins The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules Proc. Natl. Acad. Sci. U.S.A. 107 2010 2443 2448
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 2443-2448
    • Bouyain, S.1    Watkins, D.J.2
  • 14
    • 0026754494 scopus 로고
    • A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases
    • N.X. Krueger, and H. Saito A human transmembrane protein-tyrosine- phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases Proc. Natl. Acad. Sci. U. S. A. 89 1992 7417 7421
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 7417-7421
    • Krueger, N.X.1    Saito, H.2
  • 16
    • 66449105534 scopus 로고    scopus 로고
    • Carbonic anhydrase and acid-base regulation in fish
    • K.M. Gilmour, and S.F. Perry Carbonic anhydrase and acid-base regulation in fish J. Exp. Biol. 212 2009 1647 1661
    • (2009) J. Exp. Biol. , vol.212 , pp. 1647-1661
    • Gilmour, K.M.1    Perry, S.F.2
  • 18
    • 33947414441 scopus 로고    scopus 로고
    • Atomic crystal and molecular dynamics simulation structures of human carbonic anhydrase II: Insights into the proton transfer mechanism
    • DOI 10.1021/bi062066y
    • S.Z. Fisher, C.M. Maupin, M. Budayova-Spano, L. Govindasamy, C. Tu, M. Agbandje-McKenna, D.N. Silverman, G.A. Voth, and R. McKenna Atomic crystal and molecular dynamics simulation structures of human carbonic anhydrase II: insights into the proton transfer mechanism Biochemistry 46 2007 2930 2937 (Pubitemid 46449117)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 2930-2937
    • Fisher, S.Z.1    Maupin, C.M.2    Budayova-Spano, M.3    Govindasamy, L.4    Tu, C.5    Agbandje-McKenna, M.6    Silverman, D.N.7    Voth, G.A.8    McKenna, R.9
  • 19
    • 0032561466 scopus 로고    scopus 로고
    • - exchanger
    • DOI 10.1074/jbc.273.43.28430
    • J.W. Vince, and R.A. Reithmeier Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3-exchanger J. Biol. Chem. 273 1998 28430 28437 (Pubitemid 28496148)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.43 , pp. 28430-28437
    • Vince, J.W.1    Reithmeier, R.A.F.2
  • 20
    • 0037067718 scopus 로고    scopus 로고
    • - exchanger binds carbonic anhydrase IV
    • DOI 10.1074/jbc.M202562200
    • D. Sterling, B.V. Alvarez, and J.R. Casey The extracellular component of a transport metabolon. Extracellular loop 4 of the human AE1 Cl-/HCO3-exchanger binds carbonic anhydrase IV J. Biol. Chem. 277 2002 25239 25246 (Pubitemid 34951831)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25239-25246
    • Sterling, D.1    Alvarez, B.V.2    Casey, J.R.3
  • 22
    • 33847756026 scopus 로고    scopus 로고
    • Evidence against a direct interaction between intracellular carbonic anhydrase II and pure C-terminal domains of SLC4 bicarbonate transporters
    • DOI 10.1074/jbc.M608261200
    • P.M. Piermarini, E.Y. Kim, and W.F. Boron Evidence against a direct interaction between intracellular carbonic anhydrase II and pure C-terminal domains of SLC4 bicarbonate transporters J. Biol. Chem. 282 2007 1409 1421 (Pubitemid 47076561)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.2 , pp. 1409-1421
    • Piermarini, P.M.1    Kim, E.Y.2    Boron, W.F.3
  • 23
    • 0034619277 scopus 로고    scopus 로고
    • Localization of the Cl-/HCO3-anion exchanger binding site to the amino-terminal region of carbonic anhydrase II
    • J.W. Vince, U. Carlsson, and R.A. Reithmeier Localization of the Cl-/HCO3-anion exchanger binding site to the amino-terminal region of carbonic anhydrase II Biochemistry 39 2000 13344 13349
    • (2000) Biochemistry , vol.39 , pp. 13344-13349
    • Vince, J.W.1    Carlsson, U.2    Reithmeier, R.A.3
  • 24
    • 33144457846 scopus 로고    scopus 로고
    • A novel carbonic anhydrase II binding site regulates NHE1 activity
    • DOI 10.1021/bi051132d
    • X. Li, Y. Liu, B.V. Alvarez, J.R. Casey, and L. Fliegel A novel carbonic anhydrase II binding site regulates NHE1 activity Biochemistry 45 2006 2414 2424 (Pubitemid 43271342)
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2414-2424
    • Li, X.1    Liu, Y.2    Alvarez, B.V.3    Casey, J.R.4    Fliegel, L.5
  • 26
    • 0026969367 scopus 로고
    • Purification and characterization of a carbonic anhydrase II inhibitor from porcine plasma
    • DOI 10.1021/bi00164a034
    • E.D. Roush, and C.A. Fierke Purification and characterization of a carbonic anhydrase II inhibitor from porcine plasma Biochemistry 31 1992 12536 12542 (Pubitemid 23163135)
    • (1992) Biochemistry , vol.31 , Issue.49 , pp. 12536-12542
    • Roush, E.D.1    Fierke, C.A.2
  • 27
    • 0030981906 scopus 로고    scopus 로고
    • Cloning, sequencing, and recombinant expression of the porcine inhibitor of carbonic anhydrase: A novel member of the transferrin family
    • DOI 10.1021/bi9627424
    • M.W. Wuebbens, E.D. Roush, C.M. Decastro, and C.A. Fierke Cloning, sequencing, and recombinant expression of the porcine inhibitor of carbonic anhydrase: a novel member of the transferrin family Biochemistry 36 1997 4327 4336 (Pubitemid 27171607)
    • (1997) Biochemistry , vol.36 , Issue.14 , pp. 4327-4336
    • Wuebbens, M.W.1    Roush, E.D.2    Decastro, C.M.3    Fierke, C.A.4
  • 29
    • 34547567977 scopus 로고    scopus 로고
    • Selecton 2007: Advanced models for detecting positive and purifying selection using a Bayesian inference approach
    • A. Stern, A. Doron-Faigenboim, E. Erez, E. Martz, E. Bacharach, and T. Pupko Selecton 2007: advanced models for detecting positive and purifying selection using a Bayesian inference approach Nucleic Acids Res. 35 2007 W506 W511
    • (2007) Nucleic Acids Res. , vol.35
    • Stern, A.1    Doron-Faigenboim, A.2    Erez, E.3    Martz, E.4    Bacharach, E.5    Pupko, T.6
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J. Thompson, D. Higgins, and T. Gibson 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 1994 4673 4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0002511466 scopus 로고    scopus 로고
    • GeneDoc: Analysis and visualization of genetic variation
    • K. Nicholas, H.J. Nicholas, and D.I. Deerfield GeneDoc: analysis and visualization of genetic variation EMBNEW NEWS 4 1997 14
    • (1997) EMBNEW NEWS , vol.4 , pp. 14
    • Nicholas, K.1    Nicholas, H.J.2    Deerfield, D.I.3
  • 33
    • 0031240609 scopus 로고    scopus 로고
    • A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Engelbrecht, S. Brunak, and G. von Heijne A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Int. J. Neural Syst. 8 1997 581 599
    • (1997) Int. J. Neural Syst. , vol.8 , pp. 581-599
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 35
    • 33747847779 scopus 로고    scopus 로고
    • PAL2NAL: Robust conversion of protein sequence alignments into the corresponding codon alignments
    • M. Suyama, D. Torrents, and P. Bork PAL2NAL: robust conversion of protein sequence alignments into the corresponding codon alignments Nucleic Acids Res. 34 2006 W609 W612
    • (2006) Nucleic Acids Res. , vol.34
    • Suyama, M.1    Torrents, D.2    Bork, P.3
  • 36
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • DOI 10.1093/bioinformatics/bti263
    • F. Abascal, R. Zardoya, and D. Posada ProtTest: selection of best-fit models of protein evolution Bioinformatics 21 2005 2104 2105 (Pubitemid 40668057)
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 37
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • K. Tamura, J. Dudley, M. Nei, and S. Kumar MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0 Mol. Biol. Evol. 24 2007 1596 1599 (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 38
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • D.T. Jones, W.R. Taylor, and J.M. Thornton 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
  • 39
    • 0037197254 scopus 로고    scopus 로고
    • Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature
    • DOI 10.1002/jcc.10061
    • O.V. Tsodikov, M.T. Record Jr., and Y.V. Sergeev Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature J. Comput. Chem. 23 2002 600 609 (Pubitemid 34312083)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.6 , pp. 600-609
    • Tsodikov, O.V.1    Thomas Record Jr., M.2    Sergeev, Y.V.3
  • 40
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 41
    • 13044272912 scopus 로고    scopus 로고
    • Automated analysis of interatomic contacts in proteins
    • DOI 10.1093/bioinformatics/15.4.327
    • V. Sobolev, A. Sorokine, J. Prilusky, E.E. Abola, and M. Edelman Automated analysis of interatomic contacts in proteins Bioinformatics 15 1999 327 332 (Pubitemid 29213759)
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 327-332
    • Sobolev, V.1    Sorokine, A.2    Prilusky, J.3    Abola, E.E.4    Edelman, M.5
  • 43
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 58149495978 scopus 로고    scopus 로고
    • Hypoxia-inducible carbonic anhydrase IX expression is insufficient to alleviate intracellular metabolic acidosis in the muscle of zebrafish, Danio rerio
    • A.J. Esbaugh, S.F. Perry, and K.M. Gilmour Hypoxia-inducible carbonic anhydrase IX expression is insufficient to alleviate intracellular metabolic acidosis in the muscle of zebrafish, Danio rerio Am. J. Physiol. Regul. Integr. Comp. Physiol. 296 2009 R150 R160
    • (2009) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.296
    • Esbaugh, A.J.1    Perry, S.F.2    Gilmour, K.M.3
  • 47
    • 0031040821 scopus 로고    scopus 로고
    • Carbonic anhydrase IX, MN/CA IX: Analysis of stomach complementary DNA sequence and expression in human and rat alimentary tracts
    • DOI 10.1053/gast.1997.v112.pm9024293
    • S. Pastorekova, S. Parkkila, A.K. Parkkila, R. Opavsky, V. Zelnik, J. Saarnio, and J. Pastorek Carbonic anhydrase IX, MN/CA IX: analysis of stomach complementary DNA sequence and expression in human and rat alimentary tracts Gastroenterology 112 1997 398 408 (Pubitemid 27078826)
    • (1997) Gastroenterology , vol.112 , Issue.2 , pp. 398-408
    • Pastorekova, S.1    Parkkila, S.2    Parkkila, A.-K.3    Opavsky, R.4    Zelnik, V.5    Saarnio, J.6    Pastorek, J.7
  • 48
    • 33749563056 scopus 로고    scopus 로고
    • Protein evolution is faster outside the cell
    • DOI 10.1093/molbev/msl081
    • K. Julenius, and A.G. Pedersen Protein evolution is faster outside the cell Mol. Biol. Evol. 23 2006 2039 2048 (Pubitemid 44536813)
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.11 , pp. 2039-2048
    • Julenius, K.1    Pedersen, A.G.2
  • 50
    • 0037067035 scopus 로고    scopus 로고
    • Developmental expression of carbonic anhydrase-related proteins VIII, X, and XI in the human brain
    • DOI 10.1016/S0306-4522(02)00066-0, PII S0306452202000660
    • K. Taniuchi, I. Nishimori, T. Takeuchi, K. Fujikawa-Adachi, Y. Ohtsuki, and S. Onishi Developmental expression of carbonic anhydrase-related proteins VIII, X, and XI in the human brain Neuroscience 112 2002 93 99 (Pubitemid 34603500)
    • (2002) Neuroscience , vol.112 , Issue.1 , pp. 93-99
    • Taniuchi, K.1    Nishimori, I.2    Takeuchi, T.3    Fujikawa-Adachi, K.4    Ohtsuki, Y.5    Onishi, S.6
  • 51
    • 0025195942 scopus 로고
    • Binding of substrate CO2 to the active site of human carbonic anhydrase II: A molecular dynamics study
    • J.Y. Liang, and W.N. Lipscomb Binding of substrate CO2 to the active site of human carbonic anhydrase II: a molecular dynamics study Proc. Natl. Acad. Sci. U.S.A. 87 1990 3675 3679
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3675-3679
    • Liang, J.Y.1    Lipscomb, W.N.2
  • 52
    • 0027418070 scopus 로고
    • Importance of the conserved active-site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II
    • DOI 10.1111/j.1432-1033.1993.tb17614.x
    • Z. Liang, Y. Xue, G. Behravan, B.H. Jonsson, and S. Lindskog Importance of the conserved active-site residues Tyr7, Glu106 and Thr199 for the catalytic function of human carbonic anhydrase II Eur. J. Biochem. 211 1993 821 827 (Pubitemid 23050058)
    • (1993) European Journal of Biochemistry , vol.211 , Issue.3 , pp. 821-827
    • Liang, Z.1    Xue, Y.2    Behravan, G.3    Jonsson, B.-H.4    Lindskog, S.5
  • 53
    • 0033802752 scopus 로고    scopus 로고
    • Enhancement of catalytic efficiency by the combination of site-specific mutations in a carbonic anhydrase-related protein
    • B. Elleby, B. Sjoblom, C. Tu, D.N. Silverman, and S. Lindskog Enhancement of catalytic efficiency by the combination of site-specific mutations in a carbonic anhydrase-related protein Eur. J. Biochem. 267 2000 5908 5915
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5908-5915
    • Elleby, B.1    Sjoblom, B.2    Tu, C.3    Silverman, D.N.4    Lindskog, S.5
  • 54
    • 0030566855 scopus 로고    scopus 로고
    • Two point mutations convert a catalytically inactive carbonic anhydrase-related protein (CARP) to an active enzyme
    • DOI 10.1016/S0014-5793(96)01263-X, PII S001457939601263X
    • B. Sjoblom, B. Elleby, K. Wallgren, B.H. Jonsson, and S. Lindskog Two point mutations convert a catalytically inactive carbonic anhydrase-related protein (CARP) to an active enzyme FEBS Lett. 398 1996 322 325 (Pubitemid 26414334)
    • (1996) FEBS Letters , vol.398 , Issue.2-3 , pp. 322-325
    • Sjoblom, B.1    Elleby, B.2    Wallgren, K.3    Jonsson, B.-H.4    Lindskog, S.5
  • 55
    • 0035826614 scopus 로고    scopus 로고
    • Thermodynamics of metal ion binding. 1. Metal ion binding by wild-type carbonic anhydrase
    • DOI 10.1021/bi001731e
    • C.A. DiTusa, T. Christensen, K.A. McCall, C.A. Fierke, and E.J. Toone Thermodynamics of metal ion binding. 1. Metal ion binding by wild-type carbonic anhydrase Biochemistry 40 2001 5338 5344 (Pubitemid 32458233)
    • (2001) Biochemistry , vol.40 , Issue.18 , pp. 5338-5344
    • DiTusa, C.A.1    Christensen, T.2    McCall, K.A.3    Fierke, C.A.4    Toone, E.J.5
  • 56
    • 0028935889 scopus 로고
    • Structural basis of inhibitor affinity to variants of human carbonic anhydrase II
    • S.K. Nair, J.F. Krebs, D.W. Christianson, and C.A. Fierke Structural basis of inhibitor affinity to variants of human carbonic anhydrase II Biochemistry 34 1995 3981 3989
    • (1995) Biochemistry , vol.34 , pp. 3981-3989
    • Nair, S.K.1    Krebs, J.F.2    Christianson, D.W.3    Fierke, C.A.4
  • 57
    • 77955423402 scopus 로고    scopus 로고
    • Mutation of Phe91 to Asn in human carbonic anhydrase i unexpectedly enhanced both catalytic activity and affinity for sulfonamide inhibitors
    • F. Kockar, A. Maresca, M. Aydin, S. Isik, S. Turkoglu, S. Sinan, O. Arslan, O.O. Guler, Y. Turan, and C.T. Supuran Mutation of Phe91 to Asn in human carbonic anhydrase I unexpectedly enhanced both catalytic activity and affinity for sulfonamide inhibitors Bioorg. Med. Chem. 18 2010 5498 5503
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 5498-5503
    • Kockar, F.1    Maresca, A.2    Aydin, M.3    Isik, S.4    Turkoglu, S.5    Sinan, S.6    Arslan, O.7    Guler, O.O.8    Turan, Y.9    Supuran, C.T.10
  • 58
    • 0026047767 scopus 로고
    • Altering the mouth of a hydrophobic pocket: Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121
    • S.K. Nair, T.L. Calderone, D.W. Christianson, and C.A. Fierke Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121 J. Biol. Chem. 266 1991 17320 17325 (Pubitemid 21907942)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.26 , pp. 17320-17325
    • Nair, S.K.1    Calderone, T.L.2    Christianson, D.W.3    Fierke, C.A.4
  • 62
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • W.P. Russ, and D.M. Engelman The GxxxG motif: a framework for transmembrane helix-helix association J. Mol. Biol. 296 2000 911 919
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 63
    • 0036373261 scopus 로고    scopus 로고
    • Localization of a protein inhibitor of carbonic anhydrase in pig tissues
    • DOI 10.1046/j.1365-201X.2002.01010.x
    • Y. Ridderstrale, C.A. Fierke, E.D. Roush, and P.J. Wistrand Localization of a protein inhibitor of carbonic anhydrase in pig tissues Acta Physiol. Scand. 176 2002 27 31 (Pubitemid 34989205)
    • (2002) Acta Physiologica Scandinavica , vol.176 , Issue.1 , pp. 27-31
    • Ridderstrale, Y.1    Fierke, C.A.2    Roush, E.D.3    Wistrand, P.J.4
  • 65
    • 0347766006 scopus 로고    scopus 로고
    • Elevated rates of protein secretion, evolution, and disease among tissue-specific genes
    • DOI 10.1101/gr.1924004
    • E.E. Winter, L. Goodstadt, and C.P. Ponting Elevated rates of protein secretion, evolution, and disease among tissue-specific genes Genome Res. 14 2004 54 61 (Pubitemid 38088525)
    • (2004) Genome Research , vol.14 , Issue.1 , pp. 54-61
    • Winter, E.E.1    Goodstadt, L.2    Ponting, C.P.3
  • 68
    • 33846458646 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. DNA cloning, characterization, and inhibition studies of the human secretory isoform VI, a new target for sulfonamide and sulfamate inhibitors
    • DOI 10.1021/jm0612057
    • I. Nishimori, T. Minakuchi, S. Onishi, D. Vullo, A. Scozzafava, and C.T. Supuran Carbonic anhydrase inhibitors. DNA cloning, characterization, and inhibition studies of the human secretory isoform VI, a new target for sulfonamide and sulfamate inhibitors J. Med. Chem. 50 2007 381 388 (Pubitemid 46147718)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.2 , pp. 381-388
    • Nishimori, I.1    Minakuchi, T.2    Onishi, S.3    Vullo, D.4    Scozzafava, A.5    Supuran, C.T.6
  • 69
    • 0033127895 scopus 로고    scopus 로고
    • Salivary carbonic anhydrase isoenzyme VI is located in the human enamel pellicle
    • J. Leinonen, J. Kivela, S. Parkkila, A.K. Parkkila, and H. Rajaniemi Salivary carbonic anhydrase isoenzyme VI is located in the human enamel pellicle Caries Res. 33 1999 185 190
    • (1999) Caries Res. , vol.33 , pp. 185-190
    • Leinonen, J.1    Kivela, J.2    Parkkila, S.3    Parkkila, A.K.4    Rajaniemi, H.5
  • 70
    • 0033125261 scopus 로고    scopus 로고
    • A low concentration of carbonic anhydrase isoenzyme VI in whole saliva is associated with caries prevalence
    • J. Kivela, S. Parkkila, A.K. Parkkila, and H. Rajaniemi A low concentration of carbonic anhydrase isoenzyme VI in whole saliva is associated with caries prevalence Caries Res. 33 1999 178 184
    • (1999) Caries Res. , vol.33 , pp. 178-184
    • Kivela, J.1    Parkkila, S.2    Parkkila, A.K.3    Rajaniemi, H.4
  • 71
    • 33746058994 scopus 로고    scopus 로고
    • The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway
    • DOI 10.1101/gad.1411206
    • H.J. Chen, C.M. Lin, C.S. Lin, R. Perez-Olle, C.L. Leung, and R.K. Liem The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway Genes Dev. 20 2006 1933 1945 (Pubitemid 44079330)
    • (2006) Genes and Development , vol.20 , Issue.14 , pp. 1933-1945
    • Chen, H.-J.1    Lin, C.-M.2    Lin, C.-S.3    Perez-Olle, R.4    Leung, C.L.5    Liem, R.K.H.6
  • 73
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • DOI 10.1016/S0022-2836(02)01223-8
    • Y. Ofran, and B. Rost Analysing six types of protein-protein interfaces J. Mol. Biol. 325 2003 377 387 (Pubitemid 36062695)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.2 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 74
    • 70349330141 scopus 로고    scopus 로고
    • Evolutionary conservation in multiple faces of protein interaction
    • Y.S. Choi, J.S. Yang, Y. Choi, S.H. Ryu, and S. Kim Evolutionary conservation in multiple faces of protein interaction Proteins 77 2009 14 25
    • (2009) Proteins , vol.77 , pp. 14-25
    • Choi, Y.S.1    Yang, J.S.2    Choi, Y.3    Ryu, S.H.4    Kim, S.5
  • 75
    • 79954538172 scopus 로고    scopus 로고
    • Ferritin structure from Mycobacterium tuberculosis: Comparative study with homologues identifies extended c-terminus involved in ferroxidase activity
    • G. Khare, V. Gupta, P. Nangpal, R.K. Gupta, N.K. Sauter, and A.K. Tyagi Ferritin structure from Mycobacterium tuberculosis: comparative study with homologues identifies extended c-terminus involved in ferroxidase activity PLoS One 6 2011 e18570
    • (2011) PLoS One , vol.6 , pp. 18570
    • Khare, G.1    Gupta, V.2    Nangpal, P.3    Gupta, R.K.4    Sauter, N.K.5    Tyagi, A.K.6
  • 76
    • 77953265216 scopus 로고    scopus 로고
    • Mapping of interaction sites of the Schizosaccharomyces pombe protein Translin with nucleic acids and proteins: A combined molecular genetics and bioinformatics study
    • E. Eliahoo, R. Ben Yosef, L. Perez-Cano, J. Fernandez-Recio, F. Glaser, and H. Manor Mapping of interaction sites of the Schizosaccharomyces pombe protein Translin with nucleic acids and proteins: a combined molecular genetics and bioinformatics study Nucleic Acids Res. 38 2010 2975 2989
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2975-2989
    • Eliahoo, E.1    Ben Yosef, R.2    Perez-Cano, L.3    Fernandez-Recio, J.4    Glaser, F.5    Manor, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.