메뉴 건너뛰기




Volumn 43, Issue 40, 2004, Pages 12937-12944

Single-molecule dynamics reveal an altered conformation for the autoinhibitory domain of plasma membrane Ca2+-ATPase bound to oxidatively modified calmodulin

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; ENZYMES; FLUORESCENCE; OXIDATION; POLARIZATION;

EID: 4944253793     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048806p     Document Type: Article
Times cited : (23)

References (60)
  • 2
    • 0028506122 scopus 로고
    • Calmodulin: A versatile calcium mediator protein
    • Vogel, H. J. (1994) Calmodulin: a Versatile Calcium Mediator Protein, Biochem. Cell Biol. 72, 357-376.
    • (1994) Biochem. Cell Biol. , vol.72 , pp. 357-376
    • Vogel, H.J.1
  • 4
    • 0028180432 scopus 로고
    • 2+-binding and structural dynamics in the functions of calmodulin
    • 2+-Binding and Structural Dynamics in the Functions of Calmodulin, Annu. Rev. Physiol. 56, 213-236.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 213-236
    • Weinstein, H.1    Mehler, E.L.2
  • 5
    • 0029149085 scopus 로고
    • Molecular and structural basis of target recognition by calmodulin
    • Crivici, A., and Ikura, M. (1995) Molecular and Structural Basis of Target Recognition by Calmodulin, Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 85-116
    • Crivici, A.1    Ikura, M.2
  • 6
    • 0030980830 scopus 로고    scopus 로고
    • Plasma membrane calcium pump: Structure, function and relationships
    • Carafoli, E. (1997) Plasma Membrane Calcium Pump: Structure, Function and Relationships, Basic Res. Cardiol. 92, 59-61.
    • (1997) Basic Res. Cardiol. , vol.92 , pp. 59-61
    • Carafoli, E.1
  • 8
    • 0027979136 scopus 로고
    • 2+ pump. 28 Residues suffice to bind calmodulin but more are needed for full auto-inhibition of the activity
    • 2+ Pump. 28 Residues Suffice to Bind Calmodulin but More are Needed for Full Auto-Inhibition of the Activity, J. Biol. Chem. 269, 1687-1691.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1687-1691
    • Verma, A.K.1    Enyedi, A.2    Filoteo, A.G.3    Penniston, J.T.4
  • 10
    • 17144472061 scopus 로고    scopus 로고
    • Intramolecular interactions of the regulatory region with the catalytic core in the plasma membrane calcium pump
    • Padanyi, R., Paszty, K., Penheiter, A. R., Filoteo, A. G., Penniston, J. T., and Enyedi, A. (2003) Intramolecular interactions of the regulatory region with the catalytic core in the plasma membrane calcium pump, J. Biol. Chem. 278, 35798-35804.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35798-35804
    • Padanyi, R.1    Paszty, K.2    Penheiter, A.R.3    Filoteo, A.G.4    Penniston, J.T.5    Enyedi, A.6
  • 11
    • 0034185616 scopus 로고    scopus 로고
    • Protein oxidation and age-dependent alterations in calcium homeostasis
    • Squier, T. C., and Bigelow, D. J. (2000) Protein Oxidation and Age-Dependent Alterations in Calcium Homeostasis, Front. Biosci. 5, d504-d526.
    • (2000) Front. Biosci. , vol.5
    • Squier, T.C.1    Bigelow, D.J.2
  • 12
    • 0032581012 scopus 로고    scopus 로고
    • Progressive decline in the ability of calmodulin isolated from aged brain to activate the plasma membrane Ca-ATPase
    • Gao, J., Yao, Y., Williams, T. D., and Squier, T. C. (1998) Progressive Decline in the Ability of Calmodulin Isolated from Aged Brain To Activate the Plasma Membrane Ca-ATPase, Biochemistry 37, 9536-9548.
    • (1998) Biochemistry , vol.37 , pp. 9536-9548
    • Gao, J.1    Yao, Y.2    Williams, T.D.3    Squier, T.C.4
  • 13
    • 0029969392 scopus 로고    scopus 로고
    • Oxidative modification of a carboxyl-terminal methionine in calmodulin by hydrogen peroxide inhibits calmodulin-dependent activation of the plasma membrane Ca-ATPase
    • Yao, Y., Yin, D., Jas, G. S., Kuczera, K., Williams, T. D., Schöneich, C., and Squier, T. C. (1996) Oxidative Modification of a Carboxyl-Terminal Methionine in Calmodulin By Hydrogen Peroxide Inhibits Calmodulin-Dependent Activation of the Plasma Membrane Ca-ATPase, Biochemistry 35, 2767-2787.
    • (1996) Biochemistry , vol.35 , pp. 2767-2787
    • Yao, Y.1    Yin, D.2    Jas, G.S.3    Kuczera, K.4    Williams, T.D.5    Schöneich, C.6    Squier, T.C.7
  • 14
    • 0035066857 scopus 로고    scopus 로고
    • Oxidatively modified calmodulin binds to the plasma membrane Ca-ATPase in a nonproductive and conformationally disordered complex
    • Gao, J., Yao, Y., and Squier, T. C. (2001) Oxidatively Modified Calmodulin Binds to the Plasma Membrane Ca-ATPase in a Nonproductive and Conformationally Disordered Complex, Biophys. J. 80, 1791-1801.
    • (2001) Biophys. J. , vol.80 , pp. 1791-1801
    • Gao, J.1    Yao, Y.2    Squier, T.C.3
  • 15
    • 0033524399 scopus 로고    scopus 로고
    • Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase
    • Sun, H., Gao, J., Ferrington, D. A., Biesiada, H., Williams, T. D., and Squier, T. C. (1999) Repair of Oxidized Calmodulin by Methionine Sulfoxide Reductase Restores Ability to Activate the Plasma Membrane Ca-ATPase, Biochemistry 38, 105-112.
    • (1999) Biochemistry , vol.38 , pp. 105-112
    • Sun, H.1    Gao, J.2    Ferrington, D.A.3    Biesiada, H.4    Williams, T.D.5    Squier, T.C.6
  • 16
    • 0001468698 scopus 로고    scopus 로고
    • Optical studies of single molecules at room temperature
    • Xie, X. S., and Trautman, J. K. (1998) Optical Studies of Single Molecules at Room Temperature, Annu. Rev. Phys. Chem. 49, 441-480.
    • (1998) Annu. Rev. Phys. Chem. , vol.49 , pp. 441-480
    • Xie, X.S.1    Trautman, J.K.2
  • 17
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • Lu, H. P., Xun, L., and Xie, X. S. (1998) Single-Molecule Enzymatic Dynamics, Science 282, 1877-1882.
    • (1998) Science , vol.282 , pp. 1877-1882
    • Lu, H.P.1    Xun, L.2    Xie, X.S.3
  • 18
    • 0033548657 scopus 로고    scopus 로고
    • Illuminating single molecules in condensed matter
    • Moerner, W. E., and Orrit, M. (1999) Illuminating Single Molecules in Condensed Matter, Science 283, 1670-1676.
    • (1999) Science , vol.283 , pp. 1670-1676
    • Moerner, W.E.1    Orrit, M.2
  • 19
    • 0033548686 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single Biomolecules
    • Weiss, S. (1999) Fluorescence Spectroscopy of Single Biomolecules, Science 283, 1676-1683.
    • (1999) Science , vol.283 , pp. 1676-1683
    • Weiss, S.1
  • 20
    • 0033813064 scopus 로고    scopus 로고
    • Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy
    • Weiss, S. (2000) Measuring Conformational Dynamics of Biomolecules by Single Molecule Fluorescence Spectroscopy, Nat. Struct. Biol. 7, 724-729.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 724-729
    • Weiss, S.1
  • 21
    • 0028137085 scopus 로고
    • Probing single molecule dynamics
    • Xie, X. S., and Dunn, R. C. (1994) Probing Single Molecule Dynamics, Science 265, 361-364.
    • (1994) Science , vol.265 , pp. 361-364
    • Xie, X.S.1    Dunn, R.C.2
  • 22
    • 0001185990 scopus 로고    scopus 로고
    • Polarization spectroscopy of single fluorescent molecules
    • Ha, T., Laurence, T. A., Chemla, D. S., and Weiss, S. (1999) Polarization Spectroscopy of Single Fluorescent Molecules, J. Phys. Chem. B 103, 6839-6850.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 6839-6850
    • Ha, T.1    Laurence, T.A.2    Chemla, D.S.3    Weiss, S.4
  • 25
    • 0034995132 scopus 로고    scopus 로고
    • ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy
    • Sosa, H., Peterman, E. J., Moerner, W. E., and Goldstein, L. S. (2001) ADP-Induced Rocking of the Kinesin Motor Domain Revealed by Single-molecule Fluorescence Polarization Microscopy, Nat. Struct. Biol. 8, 540-544.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 540-544
    • Sosa, H.1    Peterman, E.J.2    Moerner, W.E.3    Goldstein, L.S.4
  • 26
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization
    • Forkey, J. N., Quinlan, M. E., Shaw, M. A., Corrie, J. E., and Goldman, Y. E. (2003) Three-dimensional Structural Dynamics of Myosin V by Single-molecule Fluorescence Polarization, Nature 422, 399-404.
    • (2003) Nature , vol.422 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.4    Goldman, Y.E.5
  • 27
    • 0141683490 scopus 로고    scopus 로고
    • Maximum likelihood approach to single-molecule polarization modulation analysis
    • Osborn, K. D., Singh, M. K., Urbauer, R. J. B., and Johnson, C. K. (2003) Maximum Likelihood Approach to Single-Molecule Polarization Modulation Analysis, ChemPhysChem. 4, 1005-1011.
    • (2003) ChemPhysChem , vol.4 , pp. 1005-1011
    • Osborn, K.D.1    Singh, M.K.2    Urbauer, R.J.B.3    Johnson, C.K.4
  • 29
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato, A. (1988) Computer Programs For Calculating Total From Specified Free Or Free From Specified Total Ionic Concentrations In Aqueous Solutions Containing Multiple Metals And Ligands, Methods Enzymol. 157, 378-417.
    • (1988) Methods Enzymol. , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 30
    • 1642497604 scopus 로고    scopus 로고
    • Fluorescence labeling, purification and immobilization of a double cysteine mutant calmodulin fusion protein for single-molecule experiments
    • Allen, M. W., Urbauer, R. J. B., Zaidi, A., Williams, T. D., Urbauer, J. L., and Johnson, C. K. (2004) Fluorescence Labeling, Purification and Immobilization of a Double Cysteine Mutant Calmodulin Fusion Protein for Single-Molecule Experiments, Anal. Biochem. 325, 273-284.
    • (2004) Anal. Biochem. , vol.325 , pp. 273-284
    • Allen, M.W.1    Urbauer, R.J.B.2    Zaidi, A.3    Williams, T.D.4    Urbauer, J.L.5    Johnson, C.K.6
  • 31
    • 0037465704 scopus 로고    scopus 로고
    • Oxidation of Met144 and Met145 in calmodulin blocks calmodulin dependent activation of the plasma membrane Ca-ATPase
    • Bartlett, R. K., Bieber Urbauer, R. J., Anbanandam, A., Smallwood, H. S., Urbauer, J. L., and Squier, T. C. (2003) Oxidation of Met144 and Met145 in Calmodulin Blocks Calmodulin Dependent Activation of the Plasma Membrane Ca-ATPase, Biochemistry 42, 3231-3238.
    • (2003) Biochemistry , vol.42 , pp. 3231-3238
    • Bartlett, R.K.1    Bieber Urbauer, R.J.2    Anbanandam, A.3    Smallwood, H.S.4    Urbauer, J.L.5    Squier, T.C.6
  • 32
    • 0019876575 scopus 로고
    • 2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids
    • 2+)-ATPase of the Erythrocyte Membrane. Reconstitution and Effect of Calmodulin and Phospholipids, J. Biol. Chem. 256, 395-401.
    • (1981) J. Biol. Chem. , vol.256 , pp. 395-401
    • Niggli, V.1    Adunyah, E.S.2    Penniston, J.T.3    Carafoli, E.4
  • 33
    • 0018654140 scopus 로고
    • 2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column
    • 2+)-ATPase from Human Erythrocyte Membranes Using a Calmodulin Affinity Column, J. Biol. Chem. 254, 9955-9958.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9955-9958
    • Niggli, V.1    Penniston, J.T.2    Carafoli, E.3
  • 34
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P. A., Alverez, L. J., Reinsch, P. S., and Candia, O. (1979) An Improved Assay for Nanomole Amounts of Inorganic Phosphate, Anal. Biochem. 100, 95-97.
    • (1979) Anal. Biochem. , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alverez, L.J.2    Reinsch, P.S.3    Candia, O.4
  • 35
    • 0028970124 scopus 로고
    • Stabilities of the fluorescent SH-reagent eosin-5-maleimide and its adducts with sulhydryl compounds
    • Majima, E., Gogo, S., Hori, H., Shinohara, Y., Hong, Y.-M., and Terada, H. (1995) Stabilities of the Fluorescent SH-Reagent Eosin-5-Maleimide and its Adducts with Sulhydryl Compounds, Biochim. Biophys. Acta 1243, 336-342.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 336-342
    • Majima, E.1    Gogo, S.2    Hori, H.3    Shinohara, Y.4    Hong, Y.-M.5    Terada, H.6
  • 38
    • 0030764548 scopus 로고    scopus 로고
    • Oxidant injury in Pc12 cells - A possible model of calcium "dysregulation" in aging: II. Interactions with membrane lipids
    • Denisova, N. A., Strain, J. G., and Joseph, J. A. (1997) Oxidant Injury in Pc12 Cells-A Possible Model of Calcium "Dysregulation" in Aging: II. Interactions with Membrane Lipids, J. Neurochem. 69, 1259-1266.
    • (1997) J. Neurochem. , vol.69 , pp. 1259-1266
    • Denisova, N.A.1    Strain, J.G.2    Joseph, J.A.3
  • 39
    • 0033562894 scopus 로고    scopus 로고
    • Regulation of ryanodine receptors by reactive nitrogen species
    • Eu, J. P., Xu, L., Stamler, J. S., and Meissner, G. (1999) Regulation of Ryanodine Receptors by Reactive Nitrogen Species, Biochem. Pharmacol. 57, 1079-1084.
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 1079-1084
    • Eu, J.P.1    Xu, L.2    Stamler, J.S.3    Meissner, G.4
  • 41
    • 0028305218 scopus 로고
    • Activation of myosin light chain kinase and nitric oxide synthase activities by calmodulin fragments
    • Persechini, A., McMillan, K., and Leakey, P. (1994) Activation of Myosin Light Chain Kinase and Nitric Oxide Synthase Activities by Calmodulin Fragments, J. Biol. Chem. 269, 16148-16154.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16148-16154
    • Persechini, A.1    McMillan, K.2    Leakey, P.3
  • 43
    • 0030008340 scopus 로고    scopus 로고
    • Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences
    • Bayley, P. M., Findlay, W. A., and Martin, S. R. (1996) Target Recognition by Calmodulin: Dissecting the Kinetics and Affinity of Interaction Using Short Peptide Sequences, Protein Sci. 5, 1215-1228.
    • (1996) Protein Sci. , vol.5 , pp. 1215-1228
    • Bayley, P.M.1    Findlay, W.A.2    Martin, S.R.3
  • 44
    • 0031893953 scopus 로고    scopus 로고
    • Specificity and symmetry in the interaction of calmodulin domains with the skeletal muscle myosin light chain kinase target sequence
    • Barth, A., Martin, S. R., and Bayley, P. M. (1998) Specificity and Symmetry in the Interaction of Calmodulin Domains with the Skeletal Muscle Myosin Light Chain Kinase Target Sequence, J. Biol. Chem. 273, 2174-2183.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2174-2183
    • Barth, A.1    Martin, S.R.2    Bayley, P.M.3
  • 45
    • 0034695601 scopus 로고    scopus 로고
    • Ordered and cooperative binding of opposing globular domains of calmodulin to the plasma membrane Ca-ATPase
    • Sun, H., and Squier, T. C. (2000) Ordered and Cooperative Binding of Opposing Globular Domains of Calmodulin to the Plasma Membrane Ca-ATPase, J. Biol. Chem. 275, 1731-1738.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1731-1738
    • Sun, H.1    Squier, T.C.2
  • 46
    • 0029809047 scopus 로고    scopus 로고
    • Dynamic structure of the calmodulin-binding domain of the plasma membrane Ca-ATPase in native erythrocyte ghost membranes
    • Yao, Y., Gao, J., and Squier, T. C. (1996) Dynamic Structure of the Calmodulin-Binding Domain of the Plasma Membrane Ca-ATPase in Native Erythrocyte Ghost Membranes, Biochemistry 35, 12015-12028.
    • (1996) Biochemistry , vol.35 , pp. 12015-12028
    • Yao, Y.1    Gao, J.2    Squier, T.C.3
  • 47
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal Structure of the Calcium Pump of Sarcoplasmic Reticulum at 2.6 Å Resolution, Nature 405, 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 48
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C., and Nomura, H. (2002) Structural Changes in the Calcium Pump Accompanying the Dissociation of Calcium, Nature 418, 605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 50
    • 0023226103 scopus 로고
    • Fluorescence properties of calmodulin-binding peptides reflect alpha-helical periodicity
    • O'Neil, K. T., Wolfe, H. R., Erickson-Viitanen, S., and DeGrado, W. E. (1987) Fluorescence Properties of Calmodulin-Binding Peptides Reflect Alpha-Helical Periodicity, Science 236, 1454-1457.
    • (1987) Science , vol.236 , pp. 1454-1457
    • O'Neil, K.T.1    Wolfe, H.R.2    Erickson-Viitanen, S.3    DeGrado, W.E.4
  • 51
    • 0025840594 scopus 로고
    • Structure of the smooth muscle myosin light-chain kinase calmodulin-binding domain peptide bound to calmodulin
    • Roth, S. M., Schneider, D. M., Strobel, L. A., VanBerkum, M. F. A., Means, A. R., and Wand, A. J. (1991) Structure of the Smooth Muscle Myosin Light-Chain Kinase Calmodulin-Binding Domain Peptide Bound to Calmodulin, Biochemistry 30, 10078-10084.
    • (1991) Biochemistry , vol.30 , pp. 10078-10084
    • Roth, S.M.1    Schneider, D.M.2    Strobel, L.A.3    VanBerkum, M.F.A.4    Means, A.R.5    Wand, A.J.6
  • 52
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B., and Bax, A. (1992) Solution Structure of a Calmodulin-Target 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
  • 53
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • Meador, W. E., Means, A. R., and Quiocho, F. A. (1992) Target Enzyme Recognition by Calmodulin: 2.4 Å 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
  • 54
    • 0028273407 scopus 로고
    • The calmodulin-binding domain of caldesmon binds to calmodulin in an α-helical conformation
    • Zhang, M., and Vogel, H. J. (1994) The Calmodulin-Binding Domain of Caldesmon Binds to Calmodulin in an α-Helical Conformation, Biochemistry 33, 1163-1171.
    • (1994) Biochemistry , vol.33 , pp. 1163-1171
    • Zhang, M.1    Vogel, H.J.2
  • 55
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic alpha-helices
    • O'Neil, K. T., and DeGrado, W. F. (1990) How Calmodulin Binds its Targets: Sequence Independent Recognition of Amphiphilic Alpha-Helices, Trends Biochem. Sci. 15, 59-64.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 56
    • 0018959292 scopus 로고
    • Calcium-induced exposure of a hydrophobic surface on calmodulin
    • LaPorte, D. C., Wierman, B. M., and Storm, D. R. (1980) Calcium-Induced Exposure of a Hydrophobic Surface on Calmodulin, Biochemistry 19, 3814-3819.
    • (1980) Biochemistry , vol.19 , pp. 3814-3819
    • LaPorte, D.C.1    Wierman, B.M.2    Storm, D.R.3
  • 58
    • 0032055830 scopus 로고    scopus 로고
    • Activation of calcineurin and smooth muscle myosin light chain kinase by met-to-leu mutants of calmodulin
    • Edwards, R. A., Walsh, M. P., Sutherland, C., and Vogel, H. J. (1998) Activation of Calcineurin and Smooth Muscle Myosin Light Chain Kinase by Met-to-Leu Mutants of Calmodulin, Biochem. J. 331, 149-152.
    • (1998) Biochem. J. , vol.331 , pp. 149-152
    • Edwards, R.A.1    Walsh, M.P.2    Sutherland, C.3    Vogel, H.J.4
  • 59
    • 0036681457 scopus 로고    scopus 로고
    • Free-energy simulations of the oxidation of C-terminal methionines in calmodulin
    • Jas, G. S., and Kuczera, K. (2002) Free-Energy Simulations of the Oxidation of C-Terminal Methionines in Calmodulin, Proteins: Struct., Funct., Genet. 48, 257-268.
    • (2002) Proteins: Struct., Funct., Genet. , vol.48 , pp. 257-268
    • Jas, G.S.1    Kuczera, K.2
  • 60
    • 0033550067 scopus 로고    scopus 로고
    • Nonessential role for methionines in the productive association between calmodulin and the plasma membrane Ca-ATPase
    • Yin, D., Sun, H., Weaver, R. F., and Squier, T. C. (1999) Nonessential Role for Methionines in the Productive Association Between Calmodulin and the Plasma Membrane Ca-ATPase, Biochemistry 38, 13654-13660.
    • (1999) Biochemistry , vol.38 , pp. 13654-13660
    • Yin, D.1    Sun, H.2    Weaver, R.F.3    Squier, T.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.