메뉴 건너뛰기




Volumn 44, Issue 38, 2005, Pages 12627-12639

Backbone and side chain dynamics of mutant calmodulin-peptide complexes

Author keywords

[No Author keywords available]

Indexed keywords

BONE; CALCIUM; DYNAMIC RESPONSE; MUSCLE; MUTAGENESIS; PERTURBATION TECHNIQUES;

EID: 25444519195     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050832f     Document Type: Article
Times cited : (28)

References (64)
  • 1
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz, M. F. (1970) Stereochemistry of cooperative effects in haemoglobin, Nature 228, 726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 3
    • 0029995804 scopus 로고    scopus 로고
    • Allosteric enzymes as models for chemomechanical energy transducing assemblies
    • Goldsmith, E. J. (1996) Allosteric enzymes as models for chemomechanical energy transducing assemblies, FASEB J. 10, 702-708.
    • (1996) FASEB J. , vol.10 , pp. 702-708
    • Goldsmith, E.J.1
  • 4
    • 0032215090 scopus 로고    scopus 로고
    • Allosteric receptors after 30 years
    • Changeux, J. P., and Edelstein, S. J. (1998) Allosteric receptors after 30 years. Neuron 21, 959-980.
    • (1998) Neuron , vol.21 , pp. 959-980
    • Changeux, J.P.1    Edelstein, S.J.2
  • 6
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Building allosteric switches from simple binding domains
    • Lim, W. A. (2002) The modular logic of signaling proteins: Building allosteric switches from simple binding domains, Curr. Opin. Struct. Biol. 12, 61-68.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 7
    • 0001666112 scopus 로고
    • Entropy changes accompanying association reactions of proteins
    • Steinberg, I. Z., and Scheraga, H. A. (1963) Entropy changes accompanying association reactions of proteins. J. Biol. Chem. 238, 172-181.
    • (1963) J. Biol. Chem. , vol.238 , pp. 172-181
    • Steinberg, I.Z.1    Scheraga, H.A.2
  • 8
    • 0021658956 scopus 로고
    • Allostery without conformational change - A plausible model
    • Cooper, A, and Dryden, D. T. F. (1984) Allostery without conformational change - a plausible model, Eur. Biophys. J. Biophys. Lett. 11, 103-109.
    • (1984) Eur. Biophys. J. Biophys. Lett. , vol.11 , pp. 103-109
    • Cooper, A.1    Dryden, D.T.F.2
  • 9
    • 0023475026 scopus 로고
    • Configurational entropy of native proteins
    • Karplus, M., Ichiye, T., and Pettitt, B. M. (1987) Configurational entropy of native proteins, Biophys. J. 52, 1083-1085.
    • (1987) Biophys. J. , vol.52 , pp. 1083-1085
    • Karplus, M.1    Ichiye, T.2    Pettitt, B.M.3
  • 10
    • 0029794940 scopus 로고    scopus 로고
    • Quantifying biological specificity. The statistical mechanics of molecular recognition
    • Janin, J. (1996) Quantifying biological specificity. The statistical mechanics of molecular recognition, Proteins 25, 438-445.
    • (1996) Proteins , vol.25 , pp. 438-445
    • Janin, J.1
  • 11
    • 0031746754 scopus 로고    scopus 로고
    • Statistical thermodynamic linkage between conformational and binding equilibria
    • Freire, E. (1998) Statistical thermodynamic linkage between conformational and binding equilibria, Adv. Prot. Chem. 51, 255-279.
    • (1998) Adv. Prot. Chem. , vol.51 , pp. 255-279
    • Freire, E.1
  • 12
    • 0034710950 scopus 로고    scopus 로고
    • Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble
    • Pan, H., Lee, J. C., and Hilser, V. J. (2000) Binding sites in Escherichia coli dihydrofolate reductase communicate by modulating the conformational ensemble, Proc. Natl. Acad. Sci. U.S.A. 97, 12020-12025.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12020-12025
    • Pan, H.1    Lee, J.C.2    Hilser, V.J.3
  • 13
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand, A. J. (2001) Dynamic activation of protein function: A view emerging from NMR spectroscopy, Nat. Struct. Biol. 8, 926-931.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 15
    • 0030601792 scopus 로고    scopus 로고
    • Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding
    • Yang, D. W., and Kay, L. E. (1996) Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding, J. Mol. Biol. 263, 369-382.
    • (1996) J. Mol. Biol. , vol.263 , pp. 369-382
    • Yang, D.W.1    Kay, L.E.2
  • 16
    • 0030473440 scopus 로고    scopus 로고
    • Insights into the local residual entropy of proteins provided by NMR relaxation
    • Li, Z., Raychaudhuri, S., and Wand, A. J. (1996) Insights into the local residual entropy of proteins provided by NMR relaxation, Protein Sci. 5, 2647-50.
    • (1996) Protein Sci. , vol.5 , pp. 2647-2650
    • Li, Z.1    Raychaudhuri, S.2    Wand, A.J.3
  • 17
    • 0035901519 scopus 로고    scopus 로고
    • An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in cdc42hs
    • Loh, A. P., Pawley, N., Nicholson, L. K., and Oswald, R. E. (2001) An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in cdc42hs, Biochemistry 40, 4590-4600.
    • (2001) Biochemistry , vol.40 , pp. 4590-4600
    • Loh, A.P.1    Pawley, N.2    Nicholson, L.K.3    Oswald, R.E.4
  • 18
    • 0033988897 scopus 로고    scopus 로고
    • Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex
    • Lee, A. L., Kinnear, S. A., and Wand, A. J. (2000) Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex, Nat. Struct. Biol. 7, 72-77.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 21
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin - 2.4-angstrom structure of a calmodulin-peptide complex
    • Meador, W. E., Means, A. R., and Quiocho, F. A. (1992) Target enzyme recognition by calmodulin - 2.4-angstrom 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
  • 22
    • 0033616783 scopus 로고    scopus 로고
    • Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties
    • Mirzoeva, S., Weigand, S., Lukas, T. J., Shuvalova, L., Anderson. W. F., and Watterson, D. M. (1999) Analysis of the functional coupling between calmodulin's calcium binding and peptide recognition properties, Biochemistry 38, 3936-3947.
    • (1999) Biochemistry , vol.38 , pp. 3936-3947
    • Mirzoeva, S.1    Weigand, S.2    Lukas, T.J.3    Shuvalova, L.4    Anderson, W.F.5    Watterson, D.M.6
  • 23
    • 0029058666 scopus 로고
    • Structural analysis of a novel interaction by calmodulin - High-affinity binding of a peptide in the absence of calcium
    • Urbauer, J. L., Short, J. H., Dow, L. K., and Wand, A. J. (1995) Structural analysis of a novel interaction by calmodulin - high-affinity binding of a peptide in the absence of calcium, Biochemistry 34, 8099-8109.
    • (1995) Biochemistry , vol.34 , pp. 8099-8109
    • Urbauer, J.L.1    Short, J.H.2    Dow, L.K.3    Wand, A.J.4
  • 24
    • 0037176906 scopus 로고    scopus 로고
    • Dissection of the pathway of molecular recognition by calmodulin
    • Kranz, J. K., Flynn, P. F., Fuentes, E. J., and Wand, A. J. (2002) Dissection of the pathway of molecular recognition by calmodulin, Biochemistry 41, 2599-2608.
    • (2002) Biochemistry , vol.41 , pp. 2599-2608
    • Kranz, J.K.1    Flynn, P.F.2    Fuentes, E.J.3    Wand, A.J.4
  • 26
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and Kay, L. E. (1994) Gradient-enhanced triple-resonance 3-dimensional NMR experiments with improved sensitivity, J. Magn. Reson. Ser. B 103, 203-216.
    • (1994) J. Magn. Reson. Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 27
    • 84890928276 scopus 로고
    • An efficient triple resonance experiment using C-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically enriched proteins
    • Montelione, G. T., Lyons, B. A., Emerson, S. D., and Tashiro, M. (1992) An efficient triple resonance experiment using C-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically enriched proteins. J. Am. Chem. Soc. 114, 10974-10975.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10974-10975
    • Montelione, G.T.1    Lyons, B.A.2    Emerson, S.D.3    Tashiro, M.4
  • 29
    • 0028544153 scopus 로고
    • Resonance assignment of methionine methyl groups and chi(3) angular information from long-range proton-carbon and carbon-carbon J-correlation in a calmodulin peptide complex
    • Bax, A., Delaglio, F., Grzesiek, S., and Vuister, G. W. (1994) Resonance assignment of methionine methyl groups and chi(3) angular information from long-range proton-carbon and carbon-carbon J-correlation in a calmodulin peptide complex, J. Biomol. NMR 4, 787-797.
    • (1994) J. Biomol. NMR , vol.4 , pp. 787-797
    • Bax, A.1    Delaglio, F.2    Grzesiek, S.3    Vuister, G.W.4
  • 30
    • 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
  • 31
  • 33
    • 0029176895 scopus 로고
    • Measurement of H-2 T-1 and T-1ρ relaxation-times in uniformly C-13-labeled and fractionally H-2-labeled proteins in solution
    • Muhandiram, D. R., Yamazaki, T., Sykes, B. D., and Kay, L. E. (1995) Measurement of H-2 T-1 and T-1ρ relaxation-times in uniformly C-13-labeled and fractionally H-2-labeled proteins in solution, J. Am. Chem. Soc. 117, 11536-11544.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11536-11544
    • Muhandiram, D.R.1    Yamazaki, T.2    Sykes, B.D.3    Kay, L.E.4
  • 34
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and Szabo, A. (1982) Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity, J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 35
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari, G., and Szabo, A. (1982) Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104, 4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 36
    • 0033579152 scopus 로고    scopus 로고
    • Measurement of methyl H-2 quadrupolar couplings in oriented proteins. How uniform is the quadrupolar coupling constant?
    • Mittermaier, A., and Kay, L. E, (1999) Measurement of methyl H-2 quadrupolar couplings in oriented proteins. How uniform is the quadrupolar coupling constant? J. Am. Chem. Soc. 121, 10608-10613.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10608-10613
    • Mittermaier, A.1    Kay, L.E.2
  • 38
    • 0030740124 scopus 로고    scopus 로고
    • Structure/calcium affinity relationships of site III of calmodulin: Testing the acid pair hypothesis using calmodulin mutants
    • Wu, X. C., and Reid, R. E. (1997) Structure/calcium affinity relationships of site III of calmodulin: Testing the acid pair hypothesis using calmodulin mutants, Biochemistry 36, 8649-8656.
    • (1997) Biochemistry , vol.36 , pp. 8649-8656
    • Wu, X.C.1    Reid, R.E.2
  • 39
    • 0030989059 scopus 로고    scopus 로고
    • Conservative D133E mutation of calmodulin site IV drastically alters calcium binding and phosphodiesterase regulation
    • Wu, X. C., and Reid, R. E. (1997) Conservative D133E mutation of calmodulin site IV drastically alters calcium binding and phosphodiesterase regulation, Biochemistry 36, 3608-3616.
    • (1997) Biochemistry , vol.36 , pp. 3608-3616
    • Wu, X.C.1    Reid, R.E.2
  • 40
    • 0025854636 scopus 로고
    • Restoration of the calcium-binding activity of mutant calmodulins toward normal by the presence of a calmodulin binding structure
    • Haiech, J., Kilhoffer, M. C., Lukas, T. J., Craig, T. A., Roberts, D. M., and Watterson, D. M. (1991) Restoration of the calcium-binding activity of mutant calmodulins toward normal by the presence of a calmodulin binding structure, J. Biol. Chem. 266, 3427-3431.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3427-3431
    • Haiech, J.1    Kilhoffer, M.C.2    Lukas, T.J.3    Craig, T.A.4    Roberts, D.M.5    Watterson, D.M.6
  • 44
    • 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
  • 45
    • 0028176721 scopus 로고
    • The effect of Met -Leu mutations on calmodulins ability to activate cyclic-nucleotide phosphodiesterase
    • Zhang, M. J., Li, M., Wang, J. H., and Vogel, H. J. (1994) The effect of Met -Leu mutations on calmodulins ability to activate cyclic-nucleotide phosphodiesterase, J. Biol. Chem. 269, 15546-15552.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15546-15552
    • Zhang, M.J.1    Li, M.2    Wang, J.H.3    Vogel, H.J.4
  • 46
    • 0029803672 scopus 로고    scopus 로고
    • Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases
    • Chin, D., and Means, A. R. (1996) Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases, J. Biol. Chem. 271, 30465-30471.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30465-30471
    • Chin, D.1    Means, A.R.2
  • 47
    • 0030036355 scopus 로고    scopus 로고
    • The fourth EF-hand of calmodulin and its helix-loop-helix components: Impact on calcium binding and enzyme activation
    • George, S. E., Su, Z. H., Fan, D. J., Wang, S. T., and Johnson, J. D. (1996) The fourth EF-hand of calmodulin and its helix-loop-helix components: Impact on calcium binding and enzyme activation, Biochemistry 35, 8307-8313.
    • (1996) Biochemistry , vol.35 , pp. 8307-8313
    • George, S.E.1    Su, Z.H.2    Fan, D.J.3    Wang, S.T.4    Johnson, J.D.5
  • 48
    • 0022549779 scopus 로고
    • Calmodulin binding domains: Characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase
    • Lukas, T. J., Burgess, W. H., Prendergast, F. G., Lau, W., and Watterson, D. M. (1986) Calmodulin binding domains: Characterization of a phosphorylation and calmodulin binding site from myosin light chain kinase, Biochemistry 25, 1458-1464.
    • (1986) Biochemistry , vol.25 , pp. 1458-1464
    • Lukas, T.J.1    Burgess, W.H.2    Prendergast, F.G.3    Lau, W.4    Watterson, D.M.5
  • 49
    • 0023664006 scopus 로고
    • The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence
    • Kemp, B. E., Pearson, R. B., Guerriero, V., Jr., Bagchi, I. C., and Means, A. R. (1987) The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence, J. Biol. Chem. 262, 2542-2548.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2542-2548
    • Kemp, B.E.1    Pearson, R.B.2    Guerriero Jr., V.3    Bagchi, I.C.4    Means, A.R.5
  • 51
    • 0021931438 scopus 로고
    • Chemical synthesis and expression of a calmodulin gene designed for site-specific mutagenesis
    • Roberts, D. M., Crea, R., Malecha, M., Alvaradourbina, G., Chiarello, R. H., and Watterson, D. M. (1985) Chemical synthesis and expression of a calmodulin gene designed for site-specific mutagenesis, Biochemistry 24, 5090-5098.
    • (1985) Biochemistry , vol.24 , pp. 5090-5098
    • Roberts, D.M.1    Crea, R.2    Malecha, M.3    Alvaradourbina, G.4    Chiarello, R.H.5    Watterson, D.M.6
  • 52
  • 53
    • 0034868445 scopus 로고    scopus 로고
    • NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding
    • Stone, M. J. (2001) NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding, Acc. Chem. Res. 34, 379-388.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 379-388
    • Stone, M.J.1
  • 55
    • 0034765285 scopus 로고    scopus 로고
    • Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity
    • Stevens, S. Y., Sanker, S., Kent, C., and Zuiderweg, E. R. P. (2001) Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity, Nat. Struct. Biol. 8, 947-952.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 947-952
    • Stevens, S.Y.1    Sanker, S.2    Kent, C.3    Zuiderweg, E.R.P.4
  • 56
    • 0029905210 scopus 로고    scopus 로고
    • Dynamical mapping of E-coli thioredoxin via C-13 NMR relaxation analysis
    • LeMaster, D. M., and Kushlan, D. M. (1996) Dynamical mapping of E-coli thioredoxin via C-13 NMR relaxation analysis, J. Am. Chem. Soc. 118, 9255-9264.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9255-9264
    • LeMaster, D.M.1    Kushlan, D.M.2
  • 57
    • 0029921643 scopus 로고    scopus 로고
    • Internal dynamics of human ubiquitin revealed by C-13-relaxation studies of randomly fractionally labeled protein
    • Wand, A. J., Urbauer, J. L., McEvoy, R. P., and Bieber, R. J. (1996) Internal dynamics of human ubiquitin revealed by C-13-relaxation studies of randomly fractionally labeled protein, Biochemistry 35, 6116-6125.
    • (1996) Biochemistry , vol.35 , pp. 6116-6125
    • Wand, A.J.1    Urbauer, J.L.2    McEvoy, R.P.3    Bieber, R.J.4
  • 58
  • 59
    • 0030042698 scopus 로고    scopus 로고
    • Correlation between dynamics and high affinity binding in an SH2 domain interaction
    • Kay, L. E., Muhandiram, D. R., Farrow, N. A., Aubin, Y., and Forman-Kay, J. D. (1996) Correlation between dynamics and high affinity binding in an SH2 domain interaction. Biochemistry 35, 361-368.
    • (1996) Biochemistry , vol.35 , pp. 361-368
    • Kay, L.E.1    Muhandiram, D.R.2    Farrow, N.A.3    Aubin, Y.4    Forman-Kay, J.D.5
  • 60
    • 0347753736 scopus 로고    scopus 로고
    • Ligand-dependent dynamics and intramolecular signaling in a PDZ domain
    • Fuentes, E. J., Der, C. J., and Lee, A. L. (2004) Ligand-dependent dynamics and intramolecular signaling in a PDZ domain, J. Mol. Biol. 335, 1105-1115.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1105-1115
    • Fuentes, E.J.1    Der, C.J.2    Lee, A.L.3
  • 61
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless, S. W., and Ranganathan, R. (1999) Evolutionarily conserved pathways of energetic connectivity in protein families, Science 286, 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 62
    • 0038630482 scopus 로고    scopus 로고
    • The effects of mutations on motions of side-chains in protein L studied by H-2 NMR dynamics and scalar couplings
    • Millet, O., Mittermaier, A., Baker, D., and Kay, L. E. (2003) The effects of mutations on motions of side-chains in protein L studied by H-2 NMR dynamics and scalar couplings, J. Mol. Biol. 329, 551-563.
    • (2003) J. Mol. Biol. , vol.329 , pp. 551-563
    • Millet, O.1    Mittermaier, A.2    Baker, D.3    Kay, L.E.4
  • 63
    • 4744347909 scopus 로고    scopus 로고
    • Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c
    • Clarkson, M. W., and Lee, A. L. (2004) Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c, Biochemistry 43, 12448-12458.
    • (2004) Biochemistry , vol.43 , pp. 12448-12458
    • Clarkson, M.W.1    Lee, A.L.2
  • 64
    • 0027483204 scopus 로고
    • Features of calmodulin that are important in the activation of the catalytic subunit of phosphorylase-kinase
    • Farrar, Y. J. K., Lukas, T. J., Craig, T. A., Watterson, D. M., and Carlson, G. M. (1993) Features of calmodulin that are important in the activation of the catalytic subunit of phosphorylase-kinase, J. Biol. Chem. 268, 4120-4125.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4120-4125
    • Farrar, Y.J.K.1    Lukas, T.J.2    Craig, T.A.3    Watterson, D.M.4    Carlson, G.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.