메뉴 건너뛰기




Volumn 31, Issue 4, 2013, Pages 414-425

Binding orientation and specificity of calmodulin to rat olfactory cyclic nucleotide-gated ion channel

Author keywords

Binding mode; Calmodulin; NMR; Protein protein interaction; Recognition; Target binding

Indexed keywords

AMINO ACID; ARGININE; ASPARTIC ACID; CALMODULIN; CHIMERIC PROTEIN; CYCLIC NUCLEOTIDE GATED CHANNEL; GLUTAMINE; GLYCINE; HYDROGEN; ISOLEUCINE; LEUCINE; NITROGEN 15; PALINDROMIC DNA; PHENYLALANINE; PROTEIN M13; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE;

EID: 84879207717     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2012.703069     Document Type: Article
Times cited : (9)

References (54)
  • 2
    • 0037450635 scopus 로고    scopus 로고
    • Structural basis for endothelial nitric oxide synthase binding to calmodulin
    • Aoyagi, M., Arvai, A.S., Tainer, J.A., & Getzoff, E.D. (2003). Structural basis for endothelial nitric oxide synthase binding to calmodulin. EMBO Journal, 22, 766-775.
    • (2003) EMBO Journal , vol.22 , pp. 766-775
    • Aoyagi, M.1    Arvai, A.S.2    Tainer, J.A.3    Getzoff, E.D.4
  • 3
    • 36749024011 scopus 로고    scopus 로고
    • The NMDA receptor NR1 C1 region bound to calmodulin: Structural insights into functional differences between homologous domains
    • Ataman, Z.A., Gakhar, L., Sorensen, B.R., Hell, J.W., & Shea, M.A. (2007). The NMDA receptor NR1 C1 region bound to calmodulin: Structural insights into functional differences between homologous domains. Structure, 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
  • 4
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • Babu, Y.S., Bugg, C.E., & Cook, W.J. (1988). Structure of calmodulin refined at 2.2 A resolution. Journal of Molecular Biology, 204, 191-204.
    • (1988) Journal of Molecular Biology , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 5
    • 3042825009 scopus 로고    scopus 로고
    • Calmodulin permanently associates with rat olfactory CNG channels under native conditions
    • Bradley, J., Bonigk, W., Yau, K.W., & Frings, S. (2004). Calmodulin permanently associates with rat olfactory CNG channels under native conditions. Nature Neuroscience, 7, 705-710.
    • (2004) Nature Neuroscience , vol.7 , pp. 705-710
    • Bradley, J.1    Bonigk, W.2    Yau, K.W.3    Frings, S.4
  • 8
    • 79151482756 scopus 로고    scopus 로고
    • Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5
    • Chagot, B., & Chazin, W.J. (2011). Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5. Journal of Molecular Biology, 406, 106-119.
    • (2011) Journal of Molecular Biology , vol.406 , pp. 106-119
    • Chagot, B.1    Chazin, W.J.2
  • 9
    • 79959988338 scopus 로고    scopus 로고
    • NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin
    • Chen, A.S., Kim, Y.M., Gayen, S., Huang, Q., Raida, M., & Kang, C. (2011). NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin. Biochimica et Biophysica Acta, 1808, 2224-2232.
    • (2011) Biochimica et Biophysica Acta , vol.1808 , pp. 2224-2232
    • Chen, A.S.1    Kim, Y.M.2    Gayen, S.3    Huang, Q.4    Raida, M.5    Kang, C.6
  • 10
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen, R., Li, L., & Weng, Z. (2003). ZDOCK: An initial-stage protein-docking algorithm. Proteins, 52, 80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 11
    • 0028175401 scopus 로고
    • Direct modulation by Ca2+- calmodulin of cyclic nucleotide-activated channel of rat olfactory receptor neurons
    • Chen, T.Y., & Yau, K.W. (1994). Direct modulation by Ca2+- calmodulin of cyclic nucleotide-activated channel of rat olfactory receptor neurons. Nature, 368, 545-548.
    • (1994) Nature , vol.368 , pp. 545-548
    • Chen, T.Y.1    Yau, K.W.2
  • 12
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin, D., & Means, A.R. (2000). Calmodulin: A prototypical calcium sensor. Trends in Cell Biology, 10, 322-328.
    • (2000) Trends in Cell Biology , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 13
    • 2242474818 scopus 로고    scopus 로고
    • Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: Studies of the kinase activation mechanism
    • Clapperton, J.A., Martin, S.R., Smerdon, S.J., Gamblin, S.J., & Bayley, P.M. (2002). Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: Studies of the kinase activation mechanism. Biochemistry, 41, 14669-14679.
    • (2002) Biochemistry , vol.41 , pp. 14669-14679
    • Clapperton, J.A.1    Martin, S.R.2    Smerdon, S.J.3    Gamblin, S.J.4    Bayley, P.M.5
  • 14
    • 22144464877 scopus 로고    scopus 로고
    • Structure of calmodulin complexed with an olfactory CNG channel fragment and role of the central linker: Residual dipolar couplings to evaluate calmodulin binding modes outside the kinase family
    • Contessa, G.M., Orsale, M., Melino, S., Torre, V., Paci, M., Desideri, A., & Cicero, D.O. (2005). Structure of calmodulin complexed with an olfactory CNG channel fragment and role of the central linker: Residual dipolar couplings to evaluate calmodulin binding modes outside the kinase family. Journal of Biomolecular NMR, 31, 185-199.
    • (2005) Journal of Biomolecular NMR , vol.31 , pp. 185-199
    • Contessa, G.M.1    Orsale, M.2    Melino, S.3    Torre, V.4    Paci, M.5    Desideri, A.6    Cicero, D.O.7
  • 15
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • Drum, C.L., Yan, S.Z., Bard, J., Shen, Y.Q., Lu, D., Soelaiman, S., ...Tang, W.J. (2002). Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature, 415, 396-402.
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.L.1    Yan, S.Z.2    Bard, J.3    Shen, Y.Q.4    Lu, D.5    Soelaiman, S.6    Tang, W.J.7
  • 16
    • 0033592312 scopus 로고    scopus 로고
    • NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump
    • Elshorst, B., Hennig, M., Forsterling, H., Diener, A., Maurer, M., Schulte, P., ...Carafoli, E. (1999). NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump. Biochemistry, 38, 12320-12332.
    • (1999) Biochemistry , vol.38 , pp. 12320-12332
    • Elshorst, B.1    Hennig, M.2    Forsterling, H.3    Diener, A.4    Maurer, M.5    Schulte, P.6    Carafoli, E.7
  • 17
    • 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
    • Feldkamp, M.D., Yu, L., & Shea, M.A. (2011). Structural and energetic determinants of apo calmodulin binding to the IQ motif of the Na(V)1.2 voltage-dependent sodium channel. Structure, 19, 733-747.
    • (2011) Structure , vol.19 , pp. 733-747
    • Feldkamp, M.D.1    Yu, L.2    Shea, M.A.3
  • 18
    • 34447130835 scopus 로고    scopus 로고
    • Structures and metal-ion-binding properties of the Ca2+-binding helix-loophelix EF-hand motifs
    • Gifford, J.L., Walsh, M.P., & Vogel, H.J. (2007). Structures and metal-ion-binding properties of the Ca2+-binding helix-loophelix EF-hand motifs. Biochemical Journal, 405, 199-221.
    • (2007) Biochemical Journal , vol.405 , pp. 199-221
    • Gifford, J.L.1    Walsh, M.P.2    Vogel, H.J.3
  • 20
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich, K.P., & Ikura, M. (2002). Calmodulin in action: Diversity in target recognition and activation mechanisms. Cell, 108, 739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 21
    • 31944434700 scopus 로고    scopus 로고
    • Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality
    • Ikura, M., & Ames, J.B. (2006). Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality. Proceedings of the National Academy of Sciences of the United States of America, 103, 1159-1164.
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , pp. 1159-1164
    • Ikura, M.1    Ames, J.B.2
  • 22
    • 0026536335 scopus 로고
    • Solution structure of a calmodulintarget peptide complex by multidimensional NMR
    • Ikura, M., Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C. B., & Bax, A. (1992). Solution structure of a calmodulintarget peptide complex by multidimensional NMR. Science, 256, 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 23
    • 50649109020 scopus 로고    scopus 로고
    • Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: A unique apocalmodulin-binding mode and the possible role of the Cterminal type-2 CH-domain in smooth muscle relaxation
    • Ishida, H., Borman, M.A., Ostrander, J., Vogel, H.J., & MacDonald, J.A. (2008). Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: A unique apocalmodulin-binding mode and the possible role of the Cterminal type-2 CH-domain in smooth muscle relaxation. Journal of Biological Chemistry, 283, 20569-20578.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 20569-20578
    • Ishida, H.1    Borman, M.A.2    Ostrander, J.3    Vogel, H.J.4    Macdonald, J.A.5
  • 24
    • 70350488894 scopus 로고    scopus 로고
    • Structural studies of soybean calmodulin isoform 4 bound to the calmodulin- binding domain of tobacco mitogen-activated protein kinase phosphatase-1 provide insights into a sequential target binding mode
    • Ishida, H., Rainaldi, M., & Vogel, H.J. (2009). Structural studies of soybean calmodulin isoform 4 bound to the calmodulin- binding domain of tobacco mitogen-activated protein kinase phosphatase-1 provide insights into a sequential target binding mode. Journal of Biological Chemistry, 284, 28292-28305.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 28292-28305
    • Ishida, H.1    Rainaldi, M.2    Vogel, H.J.3
  • 25
    • 33646409891 scopus 로고    scopus 로고
    • Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding
    • Ishida, H., & Vogel, H.J. (2006). Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding. Protein and Peptide Letters, 13, 455-465.
    • (2006) Protein and Peptide Letters , vol.13 , pp. 455-465
    • Ishida, H.1    Vogel, H.J.2
  • 26
    • 78649648346 scopus 로고    scopus 로고
    • The solution structure of a plant calmodulin and the CaM-binding domain of the vacuolar calcium-ATPase BCA1 reveals a new binding and activation mechanism
    • Ishida, H., & Vogel, H.J. (2010). The solution structure of a plant calmodulin and the CaM-binding domain of the vacuolar calcium-ATPase BCA1 reveals a new binding and activation mechanism. Journal of Biological Chemistry, 285, 38502-38510.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 38502-38510
    • Ishida, H.1    Vogel, H.J.2
  • 27
    • 79953173950 scopus 로고    scopus 로고
    • Conformation of the calmodulin-binding domain of metabotropic glutamate receptor subtype 7 and its interaction with calmodulin
    • Isozumi, N., Iida, Y., Nakatomi, A., Nemoto, N., Yazawa, M., & Ohki, S. (2011). Conformation of the calmodulin-binding domain of metabotropic glutamate receptor subtype 7 and its interaction with calmodulin. Journal of Biochemistry, 149, 463-474.
    • (2011) Journal of Biochemistry , vol.149 , pp. 463-474
    • Isozumi, N.1    Iida, Y.2    Nakatomi, A.3    Nemoto, N.4    Yazawa, M.5    Ohki, S.6
  • 29
    • 34248190722 scopus 로고    scopus 로고
    • Cyclic nucleotide- gated channels in plants
    • Kaplan, B., Sherman, T., & Fromm, H. (2007). Cyclic nucleotide- gated channels in plants. FEBS Letters, 581, 2237-2246.
    • (2007) FEBS Letters , vol.581 , pp. 2237-2246
    • Kaplan, B.1    Sherman, T.2    Fromm, H.3
  • 30
    • 0037053380 scopus 로고    scopus 로고
    • A direct test of the reductionist approach to structural studies of calmodulin activity: Relevance of peptide models of target proteins
    • Kranz, J.K., Lee, E.K., Nairn, A.C., & Wand, A.J. (2002). A direct test of the reductionist approach to structural studies of calmodulin activity: Relevance of peptide models of target proteins. Journal of Biological Chemistry, 277, 16351-16354.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 16351-16354
    • Kranz, J.K.1    Lee, E.K.2    Nairn, A.C.3    Wand, A.J.4
  • 31
    • 0035823139 scopus 로고    scopus 로고
    • Targetinduced conformational adaptation of calmodulin revealed by the crystal structure of a complex with nematode Ca2+/ calmodulin-dependent kinase kinase peptide
    • Kurokawa, H., Osawa, M., Kurihara, H., Katayama, N., Tokumitsu, H., Swindells, M.B., ...Ikura, M. (2001). Targetinduced conformational adaptation of calmodulin revealed by the crystal structure of a complex with nematode Ca2+/ calmodulin-dependent kinase kinase peptide. Journal of Molecular Biology, 312, 59-68.
    • (2001) Journal of Molecular Biology , vol.312 , pp. 59-68
    • Kurokawa, H.1    Osawa, M.2    Kurihara, H.3    Katayama, N.4    Tokumitsu, H.5    Swindells, M.B.6    Ikura, M.7
  • 32
    • 0242299200 scopus 로고    scopus 로고
    • RDOCK: Refinement of rigid-body protein docking predictions
    • Li, L., Chen, R., & Weng, Z. (2003). RDOCK: Refinement of rigid-body protein docking predictions. Proteins, 53, 693-707.
    • (2003) Proteins , vol.53 , pp. 693-707
    • Li, L.1    Chen, R.2    Weng, Z.3
  • 33
    • 0028600648 scopus 로고
    • Calcium-calmodulin modulation of the olfactory cyclic nucleotide-gated cation channel
    • Liu, M., Chen, T.Y., Ahamed, B., Li, J., & Yau, K.W. (1994). Calcium-calmodulin modulation of the olfactory cyclic nucleotide-gated cation channel. Science, 266, 1348-1354.
    • (1994) Science , vol.266 , pp. 1348-1354
    • Liu, M.1    Chen, T.Y.2    Ahamed, B.3    Li, J.4    Yau, K.W.5
  • 34
    • 2642524483 scopus 로고    scopus 로고
    • A physical reference state unifies the structure-derived potential of mean force for protein folding and binding
    • Liu, S., Zhang, C., Zhou, H., & Zhou, Y. (2004). A physical reference state unifies the structure-derived potential of mean force for protein folding and binding. Proteins, 56, 93-101.
    • (2004) Proteins , vol.56 , pp. 93-101
    • Liu, S.1    Zhang, C.2    Zhou, H.3    Zhou, Y.4
  • 35
    • 33749246223 scopus 로고    scopus 로고
    • Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode
    • Maximciuc, A.A., Putkey, J.A., Shamoo, Y., & Mackenzie, K. R. (2006). Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode. Structure, 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
  • 36
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin- peptide complex
    • Meador, W.E., Means, A.R., & Quiocho, F.A. (1992). Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin- peptide complex. Science, 257, 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 37
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador, W.E., Means, A.R., & Quiocho, F.A. (1993). Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science, 262, 1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 38
  • 40
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads, A.R., & Friedberg, F. (1997). Sequence motifs for calmodulin recognition. Faseb Journal, 11, 331-340.
    • (1997) Faseb Journal , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 41
    • 0035953757 scopus 로고    scopus 로고
    • Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin
    • Schumacher, M.A., Rivard, A.F., Bachinger, H.P., & Adelman, J.P. (2001). Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin. Nature, 410, 1120-1124.
    • (2001) Nature , vol.410 , pp. 1120-1124
    • Schumacher, M.A.1    Rivard, A.F.2    Bachinger, H.P.3    Adelman, J.P.4
  • 42
    • 0000434191 scopus 로고    scopus 로고
    • Interactions between domains of apo calmodulin alter calcium binding and stability
    • Sorensen, B.R., & Shea, M.A. (1998). Interactions between domains of apo calmodulin alter calcium binding and stability. Biochemistry, 37, 4244-4253.
    • (1998) Biochemistry , vol.37 , pp. 4244-4253
    • Sorensen, B.R.1    Shea, M.A.2
  • 43
    • 0038820000 scopus 로고    scopus 로고
    • Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels
    • Trudeau, M.C., & Zagotta, W.N. (2003). Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels. Journal of Biological Chemistry, 278, 18705-18708.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 18705-18708
    • Trudeau, M.C.1    Zagotta, W.N.2
  • 44
    • 79953893804 scopus 로고    scopus 로고
    • Distinct binding properties distinguish LQ-type calmodulin-binding domains in cyclic nucleotidegated channels
    • Ungerer, N., Mucke, N., Broecker, J., Keller, S., Frings, S., & Mohrlen, F. (2011). Distinct binding properties distinguish LQ-type calmodulin-binding domains in cyclic nucleotidegated channels. Biochemistry, 50, 3221-3228.
    • (2011) Biochemistry , vol.50 , pp. 3221-3228
    • Ungerer, N.1    Mucke, N.2    Broecker, J.3    Keller, S.4    Frings, S.5    Mohrlen, F.6
  • 45
    • 0030863675 scopus 로고    scopus 로고
    • Interdomain interactions underlying activation of cyclic nucleotide-gated channels
    • Varnum, M.D., & Zagotta, W.N. (1997). Interdomain interactions underlying activation of cyclic nucleotide-gated channels. Science, 278, 110-113.
    • (1997) Science , vol.278 , pp. 110-113
    • Varnum, M.D.1    Zagotta, W.N.2
  • 46
    • 0031574184 scopus 로고    scopus 로고
    • Motions of calmodulin characterized using both Bragg and diffuse Xray scattering
    • Wall, M.E., Clarage, J.B., & Phillips, G.N. (1997). Motions of calmodulin characterized using both Bragg and diffuse Xray scattering. Structure, 5, 1599-1612.
    • (1997) Structure , vol.5 , pp. 1599-1612
    • Wall, M.E.1    Clarage, J.B.2    Phillips, G.N.3
  • 47
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., & Wallace, B.A. (2004). DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Research, 32, W668-W673.
    • (2004) Nucleic Acids Research , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 48
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L., & Wallace, B.A. (2008). Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases. Biopolymers, 89, 392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 49
    • 0034257929 scopus 로고    scopus 로고
    • The 1.0 A crystal structure of Ca2+-bound calmodulin: An analysis of disorder and implications for functionally relevant plasticity
    • Wilson, M.A., & Brunger, A.T. (2000). The 1.0 A crystal structure of Ca2+-bound calmodulin: An analysis of disorder and implications for functionally relevant plasticity. Journal of Molecular Biology, 301, 1237-1256.
    • (2000) Journal of Molecular Biology , vol.301 , pp. 1237-1256
    • Wilson, M.A.1    Brunger, A.T.2
  • 51
    • 0037337760 scopus 로고    scopus 로고
    • Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin
    • Yamauchi, E., Nakatsu, T., Matsubara, M., Kato, H., & Taniguchi, H. (2003). Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin. Natural Structural Biology, 10, 226-231.
    • (2003) Natural Structural Biology , vol.10 , pp. 226-231
    • Yamauchi, E.1    Nakatsu, T.2    Matsubara, M.3    Kato, H.4    Taniguchi, H.5
  • 53
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T., & Ikura, M. (1995). Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Natural Structural Biology, 2, 758-767.
    • (1995) Natural Structural Biology , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 54
    • 0042336988 scopus 로고    scopus 로고
    • Disruption of an intersubunit interaction underlies Ca2+-calmodulin modulation of cyclic nucleotide-gated channels
    • Zheng, J., Varnum, M.D., & Zagotta, W.N. (2003). Disruption of an intersubunit interaction underlies Ca2+-calmodulin modulation of cyclic nucleotide-gated channels. Journal of Neuroscience, 23, 8167-8175.
    • (2003) Journal of Neuroscience , vol.23 , pp. 8167-8175
    • Zheng, J.1    Varnum, M.D.2    Zagotta, W.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.