메뉴 건너뛰기




Volumn 5, Issue 1, 2013, Pages 29-42

Calciomics: Integrative studies of Ca2+-binding proteins and their interactomes in biological systems

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEINS; BIOLOGICAL FUNCTIONS; CALCIUM IONS; CELLULAR ORGANELLES; EARTH'S CRUST; EXPERIMENTAL APPROACHES; HUMAN BODIES; INTRACELLULAR PARASITES; INTRACELLULAR SIGNALS; SYSTEMS LEVELS;

EID: 84871766100     PISSN: 17565901     EISSN: 1756591X     Source Type: Journal    
DOI: 10.1039/c2mt20009k     Document Type: Review
Times cited : (72)

References (94)
  • 1
    • 33751185520 scopus 로고    scopus 로고
    • The evolution of calcium biochemistry
    • R. J. Williams The evolution of calcium biochemistry Biochim. Biophys. Acta 2006 1763 1139 1146
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1139-1146
    • Williams, R.J.1
  • 2
    • 0021753139 scopus 로고
    • The influence of gravity on structure and function of animals
    • M. D. Ross The influence of gravity on structure and function of animals Adv. Space Res. 1984 4 305 314
    • (1984) Adv. Space Res. , vol.4 , pp. 305-314
    • Ross, M.D.1
  • 3
    • 0032246401 scopus 로고    scopus 로고
    • Calcium homeostasis and human evolution
    • W. A. Stini Calcium homeostasis and human evolution Coll. Antropol. 1998 22 411 425
    • (1998) Coll. Antropol. , vol.22 , pp. 411-425
    • Stini, W.A.1
  • 4
    • 34547941644 scopus 로고    scopus 로고
    • Evolution of calcium homeostasis: From birth of the first cell to an omnipresent signalling system
    • R. M. Case D. Eisner A. Gurney O. Jones S. Muallem A. Verkhratsky Evolution of calcium homeostasis: from birth of the first cell to an omnipresent signalling system Cell Calcium 2007 42 345 350
    • (2007) Cell Calcium , vol.42 , pp. 345-350
    • Case, R.M.1    Eisner, D.2    Gurney, A.3    Jones, O.4    Muallem, S.5    Verkhratsky, A.6
  • 5
    • 33846429183 scopus 로고    scopus 로고
    • Clinical lessons from the calcium-sensing receptor
    • E. M. Brown Clinical lessons from the calcium-sensing receptor Nat. Clin. Pract. Endocrinol. Metab. 2007 3 122 133
    • (2007) Nat. Clin. Pract. Endocrinol. Metab. , vol.3 , pp. 122-133
    • Brown, E.M.1
  • 7
    • 0023656068 scopus 로고
    • Maintenance of intracellular calcium in Escherichia coli
    • P. Gangola B. P. Rosen Maintenance of intracellular calcium in Escherichia coli J. Biol. Chem. 1987 262 12570 12574
    • (1987) J. Biol. Chem. , vol.262 , pp. 12570-12574
    • Gangola, P.1    Rosen, B.P.2
  • 8
    • 0023176280 scopus 로고
    • Bacterial calcium transport
    • B. P. Rosen Bacterial calcium transport Biochim. Biophys. Acta 1987 906 101 110
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 101-110
    • Rosen, B.P.1
  • 9
    • 0023256886 scopus 로고
    • A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis
    • N. K. Vyas M. N. Vyas F. A. Quiocho A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis Nature 1987 327 635 638
    • (1987) Nature , vol.327 , pp. 635-638
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 10
    • 0028913030 scopus 로고
    • Free calcium transients in chemotactic and non-chemotactic strains of Escherichia coli determined by using recombinant aequorin
    • N. J. Watkins M. R. Knight A. J. Trewavas A. K. Campbell Free calcium transients in chemotactic and non-chemotactic strains of Escherichia coli determined by using recombinant aequorin Biochem. J. 1995 306 Pt 3 865 869
    • (1995) Biochem. J. , vol.306 , Issue.PART 3 , pp. 865-869
    • Watkins, N.J.1    Knight, M.R.2    Trewavas, A.J.3    Campbell, A.K.4
  • 11
  • 12
    • 0034806053 scopus 로고    scopus 로고
    • A putative prokaryote voltage-gated Ca(2+) channel with only one 6TM motif per subunit
    • S. R. Durell H. R. Guy A putative prokaryote voltage-gated Ca(2+) channel with only one 6TM motif per subunit Biochem. Biophys. Res. Commun. 2001 281 741 746
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 741-746
    • Durell, S.R.1    Guy, H.R.2
  • 13
    • 0023085099 scopus 로고
    • Endocytobiotic coordination, intracellular calcium signaling, and the origin of endogenous rhythms
    • F. Kippert Endocytobiotic coordination, intracellular calcium signaling, and the origin of endogenous rhythms Ann. N. Y. Acad. Sci. 1987 503 476 495
    • (1987) Ann. N. Y. Acad. Sci. , vol.503 , pp. 476-495
    • Kippert, F.1
  • 14
    • 77950129751 scopus 로고    scopus 로고
    • Integration of Diverse Research Methods to Analyze and Engineer Ca-Binding Proteins: From Prediction to Production
    • M. Kirberger X. Wang K. Zhao S. Tang G. Chen J. J. Yang Integration of Diverse Research Methods to Analyze and Engineer Ca-Binding Proteins: From Prediction to Production Curr. Bioinf. 2010 5 68 80
    • (2010) Curr. Bioinf. , vol.5 , pp. 68-80
    • Kirberger, M.1    Wang, X.2    Zhao, K.3    Tang, S.4    Chen, G.5    Yang, J.J.6
  • 15
    • 0032454584 scopus 로고    scopus 로고
    • Classification and evolution of EF-hand proteins
    • H. Kawasaki S. Nakayama R. H. Kretsinger Classification and evolution of EF-hand proteins Biometals 1998 11 277 295
    • (1998) Biometals , vol.11 , pp. 277-295
    • Kawasaki, H.1    Nakayama, S.2    Kretsinger, R.H.3
  • 16
    • 33750046332 scopus 로고    scopus 로고
    • Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins
    • Y. Zhou W. Yang M. Kirberger H. W. Lee G. Ayalasomayajula J. J. Yang Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins Proteins 2006 65 643 655
    • (2006) Proteins , vol.65 , pp. 643-655
    • Zhou, Y.1    Yang, W.2    Kirberger, M.3    Lee, H.W.4    Ayalasomayajula, G.5    Yang, J.J.6
  • 18
    • 79959603758 scopus 로고    scopus 로고
    • New structural and functional contexts of the Dx[DN]xDG linear motif: Insights into evolution of calcium-binding proteins
    • D. J. Rigden D. D. Woodhead P. W. Wong M. Y. Galperin New structural and functional contexts of the Dx[DN]xDG linear motif: insights into evolution of calcium-binding proteins PLoS One 2011 6 e21507
    • (2011) PLoS One , vol.6 , pp. 21507
    • Rigden, D.J.1    Woodhead, D.D.2    Wong, P.W.3    Galperin, M.Y.4
  • 19
    • 0037432703 scopus 로고    scopus 로고
    • An extracellular calcium-binding domain in bacteria with a distant relationship to EF-hands
    • D. J. Rigden M. J. Jedrzejas M. Y. Galperin An extracellular calcium-binding domain in bacteria with a distant relationship to EF-hands FEMS Microbiol. Lett. 2003 221 103 110
    • (2003) FEMS Microbiol. Lett. , vol.221 , pp. 103-110
    • Rigden, D.J.1    Jedrzejas, M.J.2    Galperin, M.Y.3
  • 20
  • 23
    • 0028181441 scopus 로고
    • Hidden Markov models in computational biology. Applications to protein modeling
    • A. Krogh M. Brown I. S. Mian K. Sjolander D. Haussler Hidden Markov models in computational biology. Applications to protein modeling J. Mol. Biol. 1994 235 1501 1531
    • (1994) J. Mol. Biol. , vol.235 , pp. 1501-1531
    • Krogh, A.1    Brown, M.2    Mian, I.S.3    Sjolander, K.4    Haussler, D.5
  • 25
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: Interactive sequence similarity searching
    • R. D. Finn J. Clements S. R. Eddy HMMER web server: interactive sequence similarity searching Nucleic Acids Res. 2011 39 W29 W37
    • (2011) Nucleic Acids Res. , vol.39
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 26
    • 77953674718 scopus 로고    scopus 로고
    • Bioinformatics in bioinorganic chemistry
    • I. Bertini G. Cavallaro Bioinformatics in bioinorganic chemistry Metallomics 2010 2 39 51
    • (2010) Metallomics , vol.2 , pp. 39-51
    • Bertini, I.1    Cavallaro, G.2
  • 28
    • 0037093639 scopus 로고    scopus 로고
    • Structural analysis, identification, and design of calcium-binding sites in proteins
    • W. Yang H. W. Lee H. Hellinga J. J. Yang Structural analysis, identification, and design of calcium-binding sites in proteins Proteins 2002 47 344 356
    • (2002) Proteins , vol.47 , pp. 344-356
    • Yang, W.1    Lee, H.W.2    Hellinga, H.3    Yang, J.J.4
  • 29
    • 0034856791 scopus 로고    scopus 로고
    • Structural characteristics of protein binding sites for calcium and lanthanide ions
    • E. Pidcock G. R. Moore Structural characteristics of protein binding sites for calcium and lanthanide ions J. Biol. Inorg. Chem. 2001 6 479 489
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 479-489
    • Pidcock, E.1    Moore, G.R.2
  • 33
    • 33947407691 scopus 로고    scopus 로고
    • Prediction of the functional class of metal-binding proteins from sequence derived physicochemical properties by support vector machine approach
    • H. H. Lin L. Y. Han H. L. Zhang C. J. Zheng B. Xie Z. W. Cao Y. Z. Chen Prediction of the functional class of metal-binding proteins from sequence derived physicochemical properties by support vector machine approach BMC Bioinf. 2006 7 Suppl 5 S13
    • (2006) BMC Bioinf. , vol.7 , Issue.SUPPL. 5 , pp. 13
    • Lin, H.H.1    Han, L.Y.2    Zhang, H.L.3    Zheng, C.J.4    Xie, B.5    Cao, Z.W.6    Chen, Y.Z.7
  • 34
    • 57249116902 scopus 로고    scopus 로고
    • Predicting small ligand binding sites in proteins using backbone structure
    • A. J. Bordner Predicting small ligand binding sites in proteins using backbone structure Bioinformatics 2008 24 2865 2871
    • (2008) Bioinformatics , vol.24 , pp. 2865-2871
    • Bordner, A.J.1
  • 35
    • 79551476059 scopus 로고    scopus 로고
    • FINDSITE-metal: Integrating evolutionary information and machine learning for structure-based metal-binding site prediction at the proteome level
    • M. Brylinski J. Skolnick FINDSITE-metal: integrating evolutionary information and machine learning for structure-based metal-binding site prediction at the proteome level Proteins 2011 79 735 751
    • (2011) Proteins , vol.79 , pp. 735-751
    • Brylinski, M.1    Skolnick, J.2
  • 36
    • 33744803962 scopus 로고    scopus 로고
    • Predicting calcium-binding sites in proteins-a graph theory and geometry approach
    • H. Deng G. Chen W. Yang J. J. Yang Predicting calcium-binding sites in proteins-a graph theory and geometry approach Proteins 2006 64 34 42
    • (2006) Proteins , vol.64 , pp. 34-42
    • Deng, H.1    Chen, G.2    Yang, W.3    Yang, J.J.4
  • 37
    • 66149162969 scopus 로고    scopus 로고
    • 2+-binding sites with different coordination numbers in proteins with atomic resolution
    • 2+-binding sites with different coordination numbers in proteins with atomic resolution Proteins 2009 75 787 798
    • (2009) Proteins , vol.75 , pp. 787-798
    • Wang, X.1    Kirberger, M.2    Qiu, F.3    Chen, G.4    Yang, J.J.5
  • 39
    • 0042622410 scopus 로고    scopus 로고
    • WebFEATURE: An interactive web tool for identifying and visualizing functional sites on macromolecular structures
    • M. P. Liang D. R. Banatao T. E. Klein D. L. Brutlag R. B. Altman WebFEATURE: An interactive web tool for identifying and visualizing functional sites on macromolecular structures Nucleic Acids Res. 2003 31 3324 3327
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3324-3327
    • Liang, M.P.1    Banatao, D.R.2    Klein, T.E.3    Brutlag, D.L.4    Altman, R.B.5
  • 40
    • 40549094379 scopus 로고    scopus 로고
    • Combining molecular dynamics and machine learning to improve protein function recognition
    • D. S. Glazer R. J. Radmer R. B. Altman Combining molecular dynamics and machine learning to improve protein function recognition Pac. Symp. Biocomput. 2008 332 343
    • (2008) Pac. Symp. Biocomput. , pp. 332-343
    • Glazer, D.S.1    Radmer, R.J.2    Altman, R.B.3
  • 41
    • 77952728548 scopus 로고    scopus 로고
    • Analysis and prediction of calcium-binding pockets from apo-protein structures exhibiting calcium-induced localized conformational changes
    • X. Wang K. Zhao M. Kirberger H. Wong G. Chen J. J. Yang Analysis and prediction of calcium-binding pockets from apo-protein structures exhibiting calcium-induced localized conformational changes Protein Sci. 2010 19 1180 1190
    • (2010) Protein Sci. , vol.19 , pp. 1180-1190
    • Wang, X.1    Zhao, K.2    Kirberger, M.3    Wong, H.4    Chen, G.5    Yang, J.J.6
  • 42
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • K. P. Hoeflich M. Ikura Calmodulin in action: diversity in target recognition and activation mechanisms Cell (Cambridge, Mass.) 2002 108 739 742
    • (2002) Cell (Cambridge, Mass.) , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 44
  • 45
    • 36749024011 scopus 로고    scopus 로고
    • The NMDA receptor NR1 C1 region bound to calmodulin: Structural insights into functional differences between homologous domains
    • Z. A. Ataman L. Gakhar B. R. Sorensen J. W. Hell M. A. Shea The NMDA receptor NR1 C1 region bound to calmodulin: structural insights into functional differences between homologous domains Structure 2007 15 1603 1617
    • (2007) Structure , vol.15 , pp. 1603-1617
    • Ataman, Z.A.1    Gakhar, L.2    Sorensen, B.R.3    Hell, J.W.4    Shea, M.A.5
  • 46
    • 33749246223 scopus 로고    scopus 로고
    • Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode
    • A. A. Maximciuc J. A. Putkey Y. Shamoo K. R. Mackenzie Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode Structure 2006 14 1547 1556
    • (2006) Structure , vol.14 , pp. 1547-1556
    • Maximciuc, A.A.1    Putkey, J.A.2    Shamoo, Y.3    MacKenzie, K.R.4
  • 47
    • 79955816232 scopus 로고    scopus 로고
    • Structural and energetic determinants of apo calmodulin binding to the IQ motif of the Na(V)1.2 voltage-dependent sodium channel
    • M. D. Feldkamp L. Yu M. A. Shea Structural and energetic determinants of apo calmodulin binding to the IQ motif of the Na(V)1.2 voltage-dependent sodium channel Structure 2011 19 733 747
    • (2011) Structure , vol.19 , pp. 733-747
    • Feldkamp, M.D.1    Yu, L.2    Shea, M.A.3
  • 48
    • 79151482756 scopus 로고    scopus 로고
    • Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5
    • B. Chagot W. J. Chazin Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5 J. Mol. Biol. 2011 406 106 119
    • (2011) J. Mol. Biol. , vol.406 , pp. 106-119
    • Chagot, B.1    Chazin, W.J.2
  • 55
    • 78649756849 scopus 로고    scopus 로고
    • Site-specific modification of calmodulin Ca(2)(+) affinity tunes the skeletal muscle ryanodine receptor activation profile
    • J. Jiang Y. Zhou J. Zou Y. Chen P. Patel J. J. Yang E. M. Balog Site-specific modification of calmodulin Ca(2)(+) affinity tunes the skeletal muscle ryanodine receptor activation profile Biochem. J. 2010 432 89 99
    • (2010) Biochem. J. , vol.432 , pp. 89-99
    • Jiang, J.1    Zhou, Y.2    Zou, J.3    Chen, Y.4    Patel, P.5    Yang, J.J.6    Balog, E.M.7
  • 56
    • 0021379023 scopus 로고
    • Detection of calcium binding proteins by 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • K. Maruyama T. Mikawa S. Ebashi Detection of calcium binding proteins by 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis J. Biochem. 1984 95 511 519
    • (1984) J. Biochem. , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 57
    • 0020643575 scopus 로고
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye Stains-all
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye "Stains-all" J. Biol. Chem. 1983 258 11267 11273
    • (1983) J. Biol. Chem. , vol.258 , pp. 11267-11273
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3
  • 58
    • 0027289150 scopus 로고
    • Studies on the interaction of the dye, stains-all, with individual calcium-binding domains of calmodulin
    • Y. Sharma A. Gopalakrishna D. Balasubramanian T. Fairwell G. Krishna Studies on the interaction of the dye, stains-all, with individual calcium-binding domains of calmodulin FEBS Lett. 1993 326 59 64
    • (1993) FEBS Lett. , vol.326 , pp. 59-64
    • Sharma, Y.1    Gopalakrishna, A.2    Balasubramanian, D.3    Fairwell, T.4    Krishna, G.5
  • 59
    • 34247229637 scopus 로고    scopus 로고
    • Molecular properties of a novel, hydrophilic cation-binding protein associated with the plasma membrane
    • Y. Ide N. Nagasaki R. Tomioka M. Suito T. Kamiya M. Maeshima Molecular properties of a novel, hydrophilic cation-binding protein associated with the plasma membrane J. Exp. Bot. 2007 58 1173 1183
    • (2007) J. Exp. Bot. , vol.58 , pp. 1173-1183
    • Ide, Y.1    Nagasaki, N.2    Tomioka, R.3    Suito, M.4    Kamiya, T.5    Maeshima, M.6
  • 61
    • 0027415086 scopus 로고
    • Identification and purification of a calcium-binding protein in hepatic nuclear membranes
    • J. S. Gilchrist G. N. Pierce Identification and purification of a calcium-binding protein in hepatic nuclear membranes J. Biol. Chem. 1993 268 4291 4299
    • (1993) J. Biol. Chem. , vol.268 , pp. 4291-4299
    • Gilchrist, J.S.1    Pierce, G.N.2
  • 62
    • 0025834610 scopus 로고
    • Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum
    • R. E. Milner S. Baksh C. Shemanko M. R. Carpenter L. Smillie J. E. Vance M. Opas M. Michalak Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum J. Biol. Chem. 1991 266 7155 7165
    • (1991) J. Biol. Chem. , vol.266 , pp. 7155-7165
    • Milner, R.E.1    Baksh, S.2    Shemanko, C.3    Carpenter, M.R.4    Smillie, L.5    Vance, J.E.6    Opas, M.7    Michalak, M.8
  • 63
    • 0035914434 scopus 로고    scopus 로고
    • Calcium binding properties of gamma-crystallin: Calcium ion binds at the Greek key beta gamma-crystallin fold
    • B. Rajini P. Shridas C. S. Sundari D. Muralidhar S. Chandani F. Thomas Y. Sharma Calcium binding properties of gamma-crystallin: calcium ion binds at the Greek key beta gamma-crystallin fold J. Biol. Chem. 2001 276 38464 38471
    • (2001) J. Biol. Chem. , vol.276 , pp. 38464-38471
    • Rajini, B.1    Shridas, P.2    Sundari, C.S.3    Muralidhar, D.4    Chandani, S.5    Thomas, F.6    Sharma, Y.7
  • 64
    • 0022687239 scopus 로고
    • Molecular characterization of synaptophysin, a major calcium-binding protein of the synaptic vesicle membrane
    • H. Rehm B. Wiedenmann H. Betz Molecular characterization of synaptophysin, a major calcium-binding protein of the synaptic vesicle membrane EMBO J. 1986 5 535 541
    • (1986) EMBO J. , vol.5 , pp. 535-541
    • Rehm, H.1    Wiedenmann, B.2    Betz, H.3
  • 65
    • 34250689929 scopus 로고    scopus 로고
    • Azido ruthenium: A new photoreactive probe for calcium-binding proteins
    • A. Israelson N. Zilberberg V. Shoshan-Barmatz Azido ruthenium: a new photoreactive probe for calcium-binding proteins Nat. Protoc. 2006 1 111 117
    • (2006) Nat. Protoc. , vol.1 , pp. 111-117
    • Israelson, A.1    Zilberberg, N.2    Shoshan-Barmatz, V.3
  • 68
    • 0037512359 scopus 로고    scopus 로고
    • Liquid chromatography-inductively coupled plasma mass spectrometry
    • M. Montes-Bayon K. DeNicola J. A. Caruso Liquid chromatography- inductively coupled plasma mass spectrometry J. Chromatogr., A 2003 1000 457 476
    • (2003) J. Chromatogr., A , vol.1000 , pp. 457-476
    • Montes-Bayon, M.1    Denicola, K.2    Caruso, J.A.3
  • 69
    • 15744393917 scopus 로고    scopus 로고
    • Probing site-specific calmodulin calcium and lanthanide affinity by grafting
    • Y. Ye H. W. Lee W. Yang S. Shealy J. J. Yang Probing site-specific calmodulin calcium and lanthanide affinity by grafting J. Am. Chem. Soc. 2005 127 3743 3750
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 3743-3750
    • Ye, Y.1    Lee, H.W.2    Yang, W.3    Shealy, S.4    Yang, J.J.5
  • 70
    • 0042203560 scopus 로고    scopus 로고
    • Obtaining site-specific calcium-binding affinities of calmodulin
    • J. J. Yang A. Gawthrop Y. Ye Obtaining site-specific calcium-binding affinities of calmodulin Protein Pept. Lett. 2003 10 331 345
    • (2003) Protein Pept. Lett. , vol.10 , pp. 331-345
    • Yang, J.J.1    Gawthrop, A.2    Ye, Y.3
  • 71
    • 0042767564 scopus 로고    scopus 로고
    • A grafting approach to obtain site-specific metal-binding properties of EF-hand proteins
    • Y. Ye S. Shealy H. W. Lee I. Torshin R. Harrison J. J. Yang A grafting approach to obtain site-specific metal-binding properties of EF-hand proteins Protein Eng. 2003 16 429 434
    • (2003) Protein Eng. , vol.16 , pp. 429-434
    • Ye, Y.1    Shealy, S.2    Lee, H.W.3    Torshin, I.4    Harrison, R.5    Yang, J.J.6
  • 73
    • 0027525244 scopus 로고
    • Luminescence spectroscopy
    • W. D. Horrocks, Jr. Luminescence spectroscopy Methods Enzymol. 1993 226 495 538
    • (1993) Methods Enzymol. , vol.226 , pp. 495-538
    • Horrocks Jr., W.D.1
  • 75
    • 76449084891 scopus 로고    scopus 로고
    • Calciomics: Prediction and analysis of EF-hand calcium binding proteins by protein engineering
    • C. Yanyi X. Shenghui Z. Yubin Y. J. Jie Calciomics: prediction and analysis of EF-hand calcium binding proteins by protein engineering Sci. China: Chem. 2010 53 52 60
    • (2010) Sci. China: Chem. , vol.53 , pp. 52-60
    • Yanyi, C.1    Shenghui, X.2    Yubin, Z.3    Jie, Y.J.4
  • 76
    • 77958514966 scopus 로고    scopus 로고
    • Elucidation of a novel extracellular calcium-binding site on metabotropic glutamate receptor 1alpha (mGluR1) that controls receptor activation
    • Y. Jiang Y. Huang H. C. Wong Y. Zhou X. Wang J. Yang R. A. Hall E. M. Brown J. J. Yang Elucidation of a novel extracellular calcium-binding site on metabotropic glutamate receptor 1alpha (mGluR1) that controls receptor activation J. Biol. Chem. 2010 285 33463 33474
    • (2010) J. Biol. Chem. , vol.285 , pp. 33463-33474
    • Jiang, Y.1    Huang, Y.2    Wong, H.C.3    Zhou, Y.4    Wang, X.5    Yang, J.6    Hall, R.A.7    Brown, E.M.8    Yang, J.J.9
  • 78
    • 0037399919 scopus 로고    scopus 로고
    • CaMBOT: Profiling and characterizing calmodulin-binding proteins
    • D. H. O'Day CaMBOT: profiling and characterizing calmodulin-binding proteins Cell. Signalling 2003 15 347 354
    • (2003) Cell. Signalling , vol.15 , pp. 347-354
    • O'Day, D.H.1
  • 83
    • 80054735073 scopus 로고    scopus 로고
    • Probing calmodulin protein-protein interactions using high-content protein arrays
    • D. J. O'Connell M. Bauer S. Linse D. J. Cahill Probing calmodulin protein-protein interactions using high-content protein arrays Methods Mol. Biol. 2011 785 289 303
    • (2011) Methods Mol. Biol. , vol.785 , pp. 289-303
    • O'Connell, D.J.1    Bauer, M.2    Linse, S.3    Cahill, D.J.4
  • 84
    • 77950377028 scopus 로고    scopus 로고
    • Molecular basis of calcium signaling in lymphocytes: STIM and ORAI
    • P. G. Hogan R. S. Lewis A. Rao Molecular basis of calcium signaling in lymphocytes: STIM and ORAI Annu. Rev. Immunol. 2010 28 491 533
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 491-533
    • Hogan, P.G.1    Lewis, R.S.2    Rao, A.3
  • 86
    • 10044239342 scopus 로고    scopus 로고
    • The EF-Handome: Combining comparative genomic study using FamDBtool, a new bioinformatics tool, and the network of expertise of the European Calcium Society
    • J. Haiech S. B. Moulhaye M. C. Kilhoffer The EF-Handome: combining comparative genomic study using FamDBtool, a new bioinformatics tool, and the network of expertise of the European Calcium Society Biochim. Biophys. Acta 2004 1742 179 183
    • (2004) Biochim. Biophys. Acta , vol.1742 , pp. 179-183
    • Haiech, J.1    Moulhaye, S.B.2    Kilhoffer, M.C.3
  • 87
    • 77956341043 scopus 로고    scopus 로고
    • A protein sequence meta-functional signature for calcium binding residue prediction
    • J. A. Horst R. Samudrala A protein sequence meta-functional signature for calcium binding residue prediction Pattern Recognit. Lett. 2010 31 2103 2112
    • (2010) Pattern Recognit. Lett. , vol.31 , pp. 2103-2112
    • Horst, J.A.1    Samudrala, R.2
  • 88
    • 84861144301 scopus 로고    scopus 로고
    • MetalloPred: A tool for hierarchical prediction of metal ion binding proteins using cluster of neural networks and sequence derived features
    • K. N. Pradeep R. Piyush K. Pooja MetalloPred: A tool for hierarchical prediction of metal ion binding proteins using cluster of neural networks and sequence derived features J. Biophys. Chem. 2011 2 112 123
    • (2011) J. Biophys. Chem. , vol.2 , pp. 112-123
    • Pradeep, K.N.1    Piyush, R.2    Pooja, K.3
  • 89
    • 79955892164 scopus 로고    scopus 로고
    • FunFOLD: An improved automated method for the prediction of ligand binding residues using 3D models of proteins
    • D. B. Roche S. J. Tetchner L. J. McGuffin FunFOLD: an improved automated method for the prediction of ligand binding residues using 3D models of proteins BMC Bioinf. 2011 12 160
    • (2011) BMC Bioinf. , vol.12 , pp. 160
    • Roche, D.B.1    Tetchner, S.J.2    McGuffin, L.J.3
  • 90
    • 69249150494 scopus 로고    scopus 로고
    • MetaPocket: A meta approach to improve protein ligand binding site prediction
    • B. Huang MetaPocket: a meta approach to improve protein ligand binding site prediction Omics 2009 13 325 330
    • (2009) Omics , vol.13 , pp. 325-330
    • Huang, B.1
  • 92
    • 33646192301 scopus 로고    scopus 로고
    • Structural bioinformatics prediction of membrane-binding proteins
    • N. Bhardwaj R. V. Stahelin R. E. Langlois W. Cho H. Lu Structural bioinformatics prediction of membrane-binding proteins J. Mol. Biol. 2006 359 486 495
    • (2006) J. Mol. Biol. , vol.359 , pp. 486-495
    • Bhardwaj, N.1    Stahelin, R.V.2    Langlois, R.E.3    Cho, W.4    Lu, H.5
  • 93
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • B. I. Dahiyat S. L. Mayo De novo protein design: fully automated sequence selection Science 1997 278 82 87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 94
    • 0026335211 scopus 로고
    • Construction of new ligand binding sites in proteins of known structure. I. Computer-aided modeling of sites with pre-defined geometry
    • H. W. Hellinga F. M. Richards Construction of new ligand binding sites in proteins of known structure. I. Computer-aided modeling of sites with pre-defined geometry J. Mol. Biol. 1991 222 763 785
    • (1991) J. Mol. Biol. , vol.222 , pp. 763-785
    • Hellinga, H.W.1    Richards, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.