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Volumn 44, Issue 36, 2005, Pages 12136-12148

Dissecting the domain structure of Cdc4p, a myosin essential light chain involved in Schizosaccharomyces pombe cytokinesis

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PERTURBATION TECHNIQUES; PLASTICITY; THERMAL EFFECTS;

EID: 24644465033     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050641c     Document Type: Article
Times cited : (4)

References (75)
  • 1
    • 4544268020 scopus 로고    scopus 로고
    • Comparative analysis of cytokinesis in budding yeast, fission yeast and animal cells
    • Balasubramanian, M. K., Bi, E., and Glotzer, M. (2004) Comparative analysis of cytokinesis in budding yeast, fission yeast and animal cells, Curr. Biol. 14, R806-R818.
    • (2004) Curr. Biol. , vol.14
    • Balasubramanian, M.K.1    Bi, E.2    Glotzer, M.3
  • 2
    • 0035433029 scopus 로고    scopus 로고
    • Past and future of the mitotic spindle as an oncology target
    • Wood, K. W., Cornwell, W. D., and Jackson, J. R. (2001) Past and future of the mitotic spindle as an oncology target, Curr. Opin. Pharmacol. 1, 370-377.
    • (2001) Curr. Opin. Pharmacol. , vol.1 , pp. 370-377
    • Wood, K.W.1    Cornwell, W.D.2    Jackson, J.R.3
  • 4
    • 0035144284 scopus 로고    scopus 로고
    • Shedding a little light on light chains
    • Mulvihill, D. P., and Hyams, J. S. (2001) Shedding a little light on light chains, Nat. Cell Biol. 3, E10-E12.
    • (2001) Nat. Cell Biol. , vol.3
    • Mulvihill, D.P.1    Hyams, J.S.2
  • 5
    • 0038353704 scopus 로고    scopus 로고
    • Cytokinesis in fission yeast: A story of rings, rafts and walls
    • Rajagopalan, S., Wachtler, V., and Balasubramanian, M. (2003) Cytokinesis in fission yeast: a story of rings, rafts and walls, Trends Genet. 19, 403-408.
    • (2003) Trends Genet. , vol.19 , pp. 403-408
    • Rajagopalan, S.1    Wachtler, V.2    Balasubramanian, M.3
  • 6
    • 0030973306 scopus 로고    scopus 로고
    • Type II myosin heavy chain encoded by the myo2 gene composes the contractile ring during cytokinesis in Schizosaccharomyces pombe
    • Kitayama, C., Sugimoto, A., and Yamamoto, M. (1997) Type II myosin heavy chain encoded by the myo2 gene composes the contractile ring during cytokinesis in Schizosaccharomyces pombe, J. Cell Biol. 137, 1309-1319.
    • (1997) J. Cell Biol. , vol.137 , pp. 1309-1319
    • Kitayama, C.1    Sugimoto, A.2    Yamamoto, M.3
  • 7
    • 0029125594 scopus 로고
    • Schizosaccharomyces pombe cdc4+ gene encodes a novel EF-hand protein essential for cytokinesis
    • McCollum, D., Balasubramanian, M. K., Pelcher, L. E., Hemmingsen, S. M., and Gould, K. L. (1995) Schizosaccharomyces pombe cdc4+ gene encodes a novel EF-hand protein essential for cytokinesis, J. Cell Biol. 130, 651-660.
    • (1995) J. Cell Biol. , vol.130 , pp. 651-660
    • McCollum, D.1    Balasubramanian, M.K.2    Pelcher, L.E.3    Hemmingsen, S.M.4    Gould, K.L.5
  • 8
    • 0033557757 scopus 로고    scopus 로고
    • Evidence for F-actin-dependent and -independent mechanisms involved in assembly and stability of the medial actomyosin ring in fission yeast
    • Naqvi, N. I., Eng, K., Gould, K. L., and Balasubramanian, M. K. (1999) Evidence for F-actin-dependent and -independent mechanisms involved in assembly and stability of the medial actomyosin ring in fission yeast, EMBO J. 18, 854-862.
    • (1999) EMBO J. , vol.18 , pp. 854-862
    • Naqvi, N.I.1    Eng, K.2    Gould, K.L.3    Balasubramanian, M.K.4
  • 9
    • 0033781602 scopus 로고    scopus 로고
    • Type II myosin regulatory light chain relieves autoinhibition of myosin-heavy-chain function
    • Naqvi, N. I., Wong, K. C., Tang, X., and Balasubramanian, M. K. (2000) Type II myosin regulatory light chain relieves autoinhibition of myosin-heavy-chain function, Nat. Cell Biol. 2, 855-858.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 855-858
    • Naqvi, N.I.1    Wong, K.C.2    Tang, X.3    Balasubramanian, M.K.4
  • 10
    • 0034535299 scopus 로고    scopus 로고
    • The S. pombe rlc1 gene encodes a putative myosin regulatory light chain that binds the type II myosins myo3p and myo2p
    • Le Goff, X., Motegi, F., Salimova, E., Mabuchi, I., and Simanis, V. (2000) The S. pombe rlc1 gene encodes a putative myosin regulatory light chain that binds the type II myosins myo3p and myo2p, J. Cell Sci. 113, 4157-4163.
    • (2000) J. Cell Sci. , vol.113 , pp. 4157-4163
    • Le Goff, X.1    Motegi, F.2    Salimova, E.3    Mabuchi, I.4    Simanis, V.5
  • 11
    • 0035545088 scopus 로고    scopus 로고
    • Interactions of Cdc4p, a myosin light chain, with IQ-domain containing proteins in Schizosaccharomyces pombe
    • D'Souza V, M., Naqvi, N. I., Wang, H., and Balasubramanian, M. K. (2001) Interactions of Cdc4p, a myosin light chain, with IQ-domain containing proteins in Schizosaccharomyces pombe, Cell Struct. Funct. 26, 555-565.
    • (2001) Cell Struct. Funct. , vol.26 , pp. 555-565
    • D'Souza, V.M.1    Naqvi, N.I.2    Wang, H.3    Balasubramanian, M.K.4
  • 12
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu, Y. S., Bugg, C. E., and Cook, W. J. (1988) Structure of calmodulin refined at 2.2 Å resolution, J. Mol. Biol. 204, 191-204.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 13
    • 0026748968 scopus 로고
    • Backbone dynamics of calmodulin studied by N-15 relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • Barbato, G., Ikura, M., Kay, L. E., Pastor, R. W., and Bax, A. (1992) Backbone dynamics of calmodulin studied by N-15 relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible, Biochemistry 31, 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 14
    • 0025866660 scopus 로고
    • Triple-resonance multidimensional NMR study of Calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: Indication of a conformational change in the central helix
    • Ikura, M., Kay, L. E., Krinks, M., and Bax, A. (1991) Triple-resonance multidimensional NMR study of Calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: Indication of a conformational change in the central helix, Biochemistry 30, 5498-5504.
    • (1991) Biochemistry , vol.30 , pp. 5498-5504
    • Ikura, M.1    Kay, L.E.2    Krinks, M.3    Bax, A.4
  • 16
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T., and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin, Nat. Struct. Biol. 2, 758-767.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 17
    • 0023771079 scopus 로고
    • Refined crystal-structure of troponin-C from turkey skeletal-muscle at 2.0-Å resolution
    • Herzberg, O., and James, M. N. G. (1988) Refined crystal-structure of troponin-C from turkey skeletal-muscle at 2.0-Å resolution, J. Mol. Biol. 203, 761-779.
    • (1988) J. Mol. Biol. , vol.203 , pp. 761-779
    • Herzberg, O.1    James, M.N.G.2
  • 18
    • 0023947009 scopus 로고
    • Refined structure of chicken skeletal-muscle troponin-C in the 2-calcium state at 2-Å resolution
    • Satyshur, K. A., Rao, S. T., Pyzalska, D., Drendel, W., Greaser, M., and Sundaralingam, M. (1988) Refined structure of chicken skeletal-muscle troponin-C in the 2-calcium state at 2-Å resolution, J. Biol. Chem. 263, 1628-1647.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1628-1647
    • Satyshur, K.A.1    Rao, S.T.2    Pyzalska, D.3    Drendel, W.4    Greaser, M.5    Sundaralingam, M.6
  • 19
    • 0029088936 scopus 로고
    • Structures of the troponin-C regulatory domains in the apo and calcium-saturated states
    • Gagne, S. M., Tsuda, S., Li, M. X., Smillie, L. B., and Sykes, B. D. (1995) Structures of the troponin-C regulatory domains in the apo and calcium-saturated states, Nat. Struct. Biol. 2, 784-789.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 784-789
    • Gagne, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 20
    • 0028891899 scopus 로고
    • NMR solution structure of calcium-saturated skeletal muscle troponin C
    • Slupsky, C. M., and Sykes, B. D. (1995) NMR solution structure of calcium-saturated skeletal muscle troponin C, Biochemistry 34, 15953-15964.
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2
  • 23
    • 0035937171 scopus 로고    scopus 로고
    • Structure of Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe
    • Slupsky, C. M., Desautels, M., Huebert, T., Zhao, R., Hemmingsen, S. M., and McIntosh, L. P. (2001) Structure of Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe, J. Biol. Chem. 276, 5943-5951.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5943-5951
    • Slupsky, C.M.1    Desautels, M.2    Huebert, T.3    Zhao, R.4    Hemmingsen, S.M.5    McIntosh, L.P.6
  • 24
    • 0039799573 scopus 로고    scopus 로고
    • Regulation of contraction by calcium binding myosins
    • Szent-Gyorgyi, A. G. (1996) Regulation of contraction by calcium binding myosins, Biophys. Chem. 59, 357-363.
    • (1996) Biophys. Chem. , vol.59 , pp. 357-363
    • Szent-Gyorgyi, A.G.1
  • 25
    • 0141887125 scopus 로고    scopus 로고
    • Fine-tuning the myosin motor: The role of the essential light chain in striated muscle myosin
    • Timson, D. J. (2003) Fine-tuning the myosin motor: the role of the essential light chain in striated muscle myosin, Biochimie 85, 639-645.
    • (2003) Biochimie , vol.85 , pp. 639-645
    • Timson, D.J.1
  • 26
    • 0028800173 scopus 로고
    • Vps27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper, R. C., Cooper, A. A., Yang, H., and Stevens, T. H. (1995) Vps27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae, J. Cell Biol. 131, 603-617.
    • (1995) J. Cell Biol. , vol.131 , pp. 603-617
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.H.4
  • 27
    • 0141625302 scopus 로고    scopus 로고
    • Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation
    • Swanson, K. A., Kang, R. S., Stamenova, S. D., Hicke, L., and Radhakrishnan, I. (2003) Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation, EMBO J. 22, 4597-4606.
    • (2003) EMBO J. , vol.22 , pp. 4597-4606
    • Swanson, K.A.1    Kang, R.S.2    Stamenova, S.D.3    Hicke, L.4    Radhakrishnan, I.5
  • 28
    • 0035937151 scopus 로고    scopus 로고
    • Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe, interacts with a phosphatidylinositol 4-kinase
    • Desautels, M., Den Haese, J. P., Slupsky, C. M., McIntosh, L. P., and Hemmingsen, S. M. (2001) Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe, interacts with a phosphatidylinositol 4-kinase, J. Biol. Chem. 276, 5932-5942.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5932-5942
    • Desautels, M.1    Den Haese, J.P.2    Slupsky, C.M.3    McIntosh, L.P.4    Hemmingsen, S.M.5
  • 29
    • 0242362741 scopus 로고    scopus 로고
    • Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis
    • Wu, J. Q., Kuhn, J. R., Kovar, D. R., and Pollard, T. D. (2003) Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis, Dev. Cell 5, 723-734.
    • (2003) Dev. Cell , vol.5 , pp. 723-734
    • Wu, J.Q.1    Kuhn, J.R.2    Kovar, D.R.3    Pollard, T.D.4
  • 30
    • 0037415748 scopus 로고    scopus 로고
    • Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications
    • Terrak, M., Wu, G., Stafford, W. F., Lu, R. C., and Dominguez, R. (2003) Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications, EMBO J. 22, 362-371.
    • (2003) EMBO J. , vol.22 , pp. 362-371
    • Terrak, M.1    Wu, G.2    Stafford, W.F.3    Lu, R.C.4    Dominguez, R.5
  • 32
    • 0017637023 scopus 로고
    • Cleavage at aspartyl-prolyl bonds
    • Landon (1977) Cleavage at aspartyl-prolyl bonds, Methods Enzymol. 47, 145-149.
    • (1977) Methods Enzymol. , vol.47 , pp. 145-149
    • Landon1
  • 33
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro, M. M., and Bolen, D. W. (1992) A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range, Biochemistry 31, 4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 34
    • 0029946423 scopus 로고    scopus 로고
    • Relationship between stability and function for isolated domains of troponin C
    • Fredricksen, R. S., and Swenson, C. A. (1996) Relationship between stability and function for isolated domains of troponin C, Biochemistry 35, 14012-14026.
    • (1996) Biochemistry , vol.35 , pp. 14012-14026
    • Fredricksen, R.S.1    Swenson, C.A.2
  • 35
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 36
    • 0004757060 scopus 로고    scopus 로고
    • University of California, San Francisco
    • Goddard, T. D., and Kneller, D. G. (2004) SPARKY, University of California, San Francisco.
    • (2004) SPARKY
    • Goddard, T.D.1    Kneller, D.G.2
  • 38
    • 0006159639 scopus 로고    scopus 로고
    • Columbia University, New York
    • Palmer, A. G. (1998) Curvefit, Columbia University, New York.
    • (1998) Curvefit
    • Palmer, A.G.1
  • 39
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset, P., Hus, J. C., Blackledge, M., and Marion, D. (2000) Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data, J. Biomol. NMR 16, 23-28.
    • (2000) J. Biomol. NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.C.2    Blackledge, M.3    Marion, D.4
  • 40
    • 0027169975 scopus 로고
    • Isotope effects in peptide group hydrogen exchange
    • Connelly, G. P., Bai, Y., Jeng, M. F., and Englander, S. W. (1993) Isotope effects in peptide group hydrogen exchange, Proteins 17, 87-92.
    • (1993) Proteins , vol.17 , pp. 87-92
    • Connelly, G.P.1    Bai, Y.2    Jeng, M.F.3    Englander, S.W.4
  • 41
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Primary structure effects on peptide group hydrogen exchange, Proteins 17, 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 42
    • 0033515440 scopus 로고    scopus 로고
    • The cellulose-binding domains from Cellulomonas fimi beta-1,4-glucanase CenC bind nitroxide spin-labeled cellooligosaccharides in multiple orientations
    • Johnson, P. E., Brun, E., MacKenzie, L. F., Withers, S. G., and McIntosh, L. P. (1999) The cellulose-binding domains from Cellulomonas fimi beta-1,4-glucanase CenC bind nitroxide spin-labeled cellooligosaccharides in multiple orientations, J. Mol. Biol. 287, 609-625.
    • (1999) J. Mol. Biol. , vol.287 , pp. 609-625
    • Johnson, P.E.1    Brun, E.2    MacKenzie, L.F.3    Withers, S.G.4    McIntosh, L.P.5
  • 43
    • 0020855355 scopus 로고
    • Hydrogen-exchange and structural dynamics of proteins and nucleic-acids
    • Englander, S. W., and Kallenbach, N. R. (1983) Hydrogen-exchange and structural dynamics of proteins and nucleic-acids, Q. Rev. Biophys. 16, 521-655.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 44
    • 0346159350 scopus 로고    scopus 로고
    • Motional model analyses of protein and peptide dynamics using C-13 and N-15 NMR relaxation
    • Daragan, V. A., and Mayo, K. H. (1997) Motional model analyses of protein and peptide dynamics using C-13 and N-15 NMR relaxation, Prog. Nucl. Magn. Reson, Spectrosc. 31, 63-105.
    • (1997) Prog. Nucl. Magn. Reson. Spectrosc. , vol.31 , pp. 63-105
    • Daragan, V.A.1    Mayo, K.H.2
  • 45
    • 0037028988 scopus 로고    scopus 로고
    • An effective method for the discrimination of motional anisotropy and chemical exchange
    • Kneller, J. M., Lu, M., and Bracken, C. (2002) An effective method for the discrimination of motional anisotropy and chemical exchange, J. Am. Chem. Soc. 124, 1852-1853.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1852-1853
    • Kneller, J.M.1    Lu, M.2    Bracken, C.3
  • 46
    • 0000406389 scopus 로고    scopus 로고
    • Amino terminal Cu(II)- and Ni(II)-binding (ATCUN) motif of proteins and peptides: Metal binding, DNA cleavage, and other properties
    • Harford, C., and Sarkar, B. (1997) Amino terminal Cu(II)- and Ni(II)-binding (ATCUN) motif of proteins and peptides: Metal binding, DNA cleavage, and other properties, Acc. Chem. Res. 30, 123-130.
    • (1997) Acc. Chem. Res. , vol.30 , pp. 123-130
    • Harford, C.1    Sarkar, B.2
  • 47
    • 0035840960 scopus 로고    scopus 로고
    • Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy
    • Donaldson, L. W., Skrynnikov, N. R., Choy, W. Y., Muhandiram, D. R., Sarkar, B., Forman-Kay, J. D., and Kay, L. E. (2001) Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy, J. Am. Chem. Soc. 123, 9843-9847.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9843-9847
    • Donaldson, L.W.1    Skrynnikov, N.R.2    Choy, W.Y.3    Muhandiram, D.R.4    Sarkar, B.5    Forman-Kay, J.D.6    Kay, L.E.7
  • 48
    • 7244226219 scopus 로고    scopus 로고
    • UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II
    • Lord, M., and Pollard, T. D. (2004) UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II, J. Cell Biol. 167, 315-325.
    • (2004) J. Cell Biol. , vol.167 , pp. 315-325
    • Lord, M.1    Pollard, T.D.2
  • 50
    • 0034681952 scopus 로고    scopus 로고
    • The whole is not the simple sum of its parts in Calmodulin from S. cerevisiae
    • Lee, S. Y., and Klevit, R. E. (2000) The whole is not the simple sum of its parts in Calmodulin from S. cerevisiae, Biochemistry 39, 4225-4230.
    • (2000) Biochemistry , vol.39 , pp. 4225-4230
    • Lee, S.Y.1    Klevit, R.E.2
  • 51
    • 0021761383 scopus 로고
    • High field proton NMR studies of tryptic fragments of calmodulin: A comparison with the native protein
    • Aulabaugh, A., Niemczura, W. P., and Gibbons, W. A. (1984) High field proton NMR studies of tryptic fragments of calmodulin: a comparison with the native protein, Biochem. Biophys. Res. Commun. 118, 225-232.
    • (1984) Biochem. Biophys. Res. Commun. , vol.118 , pp. 225-232
    • Aulabaugh, A.1    Niemczura, W.P.2    Gibbons, W.A.3
  • 53
    • 0037184479 scopus 로고    scopus 로고
    • The ATCUN domain as a probe of intermolecular interactions: Application to calmodulin-peptide complexes
    • Mal, T. K., Ikura, M., and Kay, L. E. (2002) The ATCUN domain as a probe of intermolecular interactions: application to calmodulin-peptide complexes, J. Am. Chem. Soc. 124, 14002-14003.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14002-14003
    • Mal, T.K.1    Ikura, M.2    Kay, L.E.3
  • 54
    • 0024300799 scopus 로고
    • Nuclear magnetic resonance study on rabbit skeletal troponin C: Calcium-induced conformational change
    • Tsuda, S., Hasegawa, Y., Yoshida, M., Yagi, K., and Hikichi, K. (1988) Nuclear magnetic resonance study on rabbit skeletal troponin C: calcium-induced conformational change, Biochemistry 27, 4120-4126,
    • (1988) Biochemistry , vol.27 , pp. 4120-4126
    • Tsuda, S.1    Hasegawa, Y.2    Yoshida, M.3    Yagi, K.4    Hikichi, K.5
  • 55
    • 0024293557 scopus 로고
    • 1H nuclear magnetic resonance study of pike pI 5.0 parvalbumin (Esox lucius). Sequential resonance assignments and folding of the polypeptide chain
    • 1H nuclear magnetic resonance study of pike pI 5.0 parvalbumin (Esox lucius). Sequential resonance assignments and folding of the polypeptide chain, J. Mol. Biol. 204, 995-1017.
    • (1988) J. Mol. Biol. , vol.204 , pp. 995-1017
    • Padilla, A.1    Cave, A.2    Parello, J.3
  • 57
    • 0024473841 scopus 로고
    • 1H NMR studies of porcine calbindin D9k in solution: Sequential resonance assignment, secondary structure, and global fold
    • 1H NMR studies of porcine calbindin D9k in solution: sequential resonance assignment, secondary structure, and global fold, Biochemistry 28, 5946-5954.
    • (1989) Biochemistry , vol.28 , pp. 5946-5954
    • Drakenberg, T.1    Hofmann, T.2    Chazin, W.J.3
  • 58
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka, N. C., and James, M. N. (1989) Crystal structures of the helix-loop-helix calcium-binding proteins, Annu. Rev. Biochem. 58, 951-998.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-998
    • Strynadka, N.C.1    James, M.N.2
  • 59
    • 0029990420 scopus 로고    scopus 로고
    • Spectroscopic characterization of a high-affinity calmodulin-target peptide hybrid molecule
    • Martin, S. R., Bayley, P. M., Brown, S. E., Porumb, T., Zhang, M. J., and Ikura, M. (1996) Spectroscopic characterization of a high-affinity calmodulin-target peptide hybrid molecule, Biochemistry 35, 3508-3517.
    • (1996) Biochemistry , vol.35 , pp. 3508-3517
    • Martin, S.R.1    Bayley, P.M.2    Brown, S.E.3    Porumb, T.4    Zhang, M.J.5    Ikura, M.6
  • 60
    • 0037441514 scopus 로고    scopus 로고
    • Basic interdomain boundary residues in calmodulin decrease calcium affinity of sites I and II by stabilizing helix-helix interactions
    • Faga, L. A., Sorensen, B. R., VanScyoc, W. S., and Shea, M. A. (2003) Basic interdomain boundary residues in calmodulin decrease calcium affinity of sites I and II by stabilizing helix-helix interactions, Proteins 50, 381-391.
    • (2003) Proteins , vol.50 , pp. 381-391
    • Faga, L.A.1    Sorensen, B.R.2    Vanscyoc, W.S.3    Shea, M.A.4
  • 61
    • 0035965145 scopus 로고    scopus 로고
    • Prediction of functionally important residues based solely on the computed energetics of protein structure
    • Elcock, A. H. (2001) Prediction of functionally important residues based solely on the computed energetics of protein structure, J. Mol. Biol. 312, 885-896.
    • (2001) J. Mol. Biol. , vol.312 , pp. 885-896
    • Elcock, A.H.1
  • 62
    • 0344603844 scopus 로고    scopus 로고
    • The hydrogen exchange core and protein folding
    • Li, R. H., and Woodward, C. (1999) The hydrogen exchange core and protein folding, Protein Sci. 8, 1571-1590.
    • (1999) Protein Sci. , vol.8 , pp. 1571-1590
    • Li, R.H.1    Woodward, C.2
  • 63
    • 1542289841 scopus 로고    scopus 로고
    • Native state hydrogen-exchange analysis of protein folding and protein motional domains
    • Woodward, C., Carulla, N., and Barany, G. (2004) Native state hydrogen-exchange analysis of protein folding and protein motional domains, Methods Enzymol. 380, 379-400.
    • (2004) Methods Enzymol. , vol.380 , pp. 379-400
    • Woodward, C.1    Carulla, N.2    Barany, G.3
  • 64
    • 0033837859 scopus 로고    scopus 로고
    • Ligand binding and thermodynamic stability of a multidomain protein, calmodulin
    • Masino, L., Martin, S. R., and Bayley, P. M. (2000) Ligand binding and thermodynamic stability of a multidomain protein, calmodulin, Protein Sci. 9, 1519-1529.
    • (2000) Protein Sci. , vol.9 , pp. 1519-1529
    • Masino, L.1    Martin, S.R.2    Bayley, P.M.3
  • 65
    • 0034719155 scopus 로고    scopus 로고
    • Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy: Evidence for interaction between the two globular domains
    • Fefeu, S., Biekofsky, R. R., McCormick, J. E., Martin, S. R., Bayley, P. M., and Feeney, J. (2000) Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy: evidence for interaction between the two globular domains, Biochemistry 39, 15920-15931.
    • (2000) Biochemistry , vol.39 , pp. 15920-15931
    • Fefeu, S.1    Biekofsky, R.R.2    McCormick, J.E.3    Martin, S.R.4    Bayley, P.M.5    Feeney, J.6
  • 68
    • 0032454584 scopus 로고    scopus 로고
    • Classification and evolution of EF-hand proteins
    • Kawasaki, H., Nakayama, S., and Kretsinger, R. H. (1998) Classification and evolution of EF-hand proteins, Biometals 11, 277-295.
    • (1998) Biometals , vol.11 , pp. 277-295
    • Kawasaki, H.1    Nakayama, S.2    Kretsinger, R.H.3
  • 69
    • 0026771336 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. 2. Domains of several subfamilies have diverse evolutionary histories
    • Nakayama, S., Moncrief, N. D., and Kretsinger, R. H. (1992) Evolution of EF-hand calcium-modulated proteins. 2. Domains of several subfamilies have diverse evolutionary histories, J. Mol. Evol. 34, 416-448.
    • (1992) J. Mol. Evol. , vol.34 , pp. 416-448
    • Nakayama, S.1    Moncrief, N.D.2    Kretsinger, R.H.3
  • 70
    • 0025311949 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. 1. Relationships based on amino-acid-sequences
    • Moncrief, N. D., Kretsinger, R. H., and Goodman, M. (1990) Evolution of EF-hand calcium-modulated proteins. 1. Relationships based on amino-acid-sequences, J. Mol. Evol. 30, 522-562.
    • (1990) J. Mol. Evol. , vol.30 , pp. 522-562
    • Moncrief, N.D.1    Kretsinger, R.H.2    Goodman, M.3
  • 71
    • 0037318056 scopus 로고    scopus 로고
    • Novel aspects of calmodulin target recognition and activation
    • Vetter, S. W., and Leclerc, E. (2003) Novel aspects of calmodulin target recognition and activation, Eur. J. Biochem. 270, 404-414.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 404-414
    • Vetter, S.W.1    Leclerc, E.2
  • 74
  • 75
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy, Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


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