The evolving model of calmodulin structure, function and activation.
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B. Finn | S. Forsén | S Forsén | B E Finn
[1] C. Bugg,et al. Structure of calmodulin refined at 2.2 A resolution. , 1988, Journal of molecular biology.
[2] B. Finn,et al. The structure of apo‐calmodulin , 1993, FEBS letters.
[3] Charles E. Bugg,et al. Three-dimensional structure of calmodulin , 1985, Nature.
[4] F A Quiocho,et al. Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. , 1992, Science.
[5] D. Blumenthal,et al. The effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding. , 1989, The Journal of biological chemistry.
[6] K. Ling,et al. Structure of Paramecium tetraurelia calmodulin at 1.8 Å resolution , 1993, Protein science : a publication of the Protein Society.
[7] F A Quiocho,et al. Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. , 1993, Science.
[8] William F. DeGrado,et al. How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices , 1990 .
[9] J S Sack,et al. Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution. , 1992, The Journal of biological chemistry.
[10] A. Gronenborn,et al. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. , 1994, Science.
[11] M Ikura,et al. Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. , 1992, Biochemistry.
[12] F M Richards,et al. Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering. , 1985, Biochemistry.
[13] Mitsuhiko Ikura,et al. Sequence‐specific assignments of downfield‐shifted amide proton resonances of calmodulin Use of two‐dimensional NMR analysis of its tryptic fragments , 1987 .
[14] R. Kretsinger. The linker of calmodulin--to helix or not to helix. , 1992, Cell calcium.
[15] J. Trewhella,et al. Comparison of the crystal and solution structures of calmodulin and troponin C. , 1988, Biochemistry.
[16] D. Blumenthal,et al. Changes in the structure of calmodulin induced by a peptide based on the calmodulin-binding domain of myosin light chain kinase. , 1989, Biochemistry.
[17] L. Kay,et al. Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. , 1991, Biochemistry.
[18] M. Sundaralingam,et al. Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution. , 1985, Science.
[19] C. Schutt. Protein structure: Hands on the calcium switch , 1985, Nature.
[20] J. Trewhella. The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains. , 1992, Cell calcium.
[21] A. Wrzosek,et al. Interaction of calmodulin and its fragments with Ca2+-ATPase and myosin light chain kinase. , 1986, Cell calcium.
[22] Conrad C. Huang,et al. The MIDAS display system , 1988 .
[23] D. Storm,et al. Calcium-induced exposure of a hydrophobic surface on calmodulin. , 1980, Biochemistry.
[24] M. James,et al. Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution , 1985, Nature.
[25] M. James,et al. Two trifluoperazine‐binding sites on calmodulin predicted from comparative molecular modeling with troponin‐C , 1988, Proteins.
[26] F A Quiocho,et al. Calmodulin structure refined at 1.7 A resolution. , 1992, Journal of molecular biology.