DOI: 10.1016/s0969-2126(01)00130-7. The evolving model of calmodulin structure,function and activation

The evolving model of calmodulin structure,function and activation

10.1016/s0969-2126(01)00130-7

Crossref journal-article

Elsevier BV

Structure (78)

Bibliography

Finn, B. E., & ForsÃ©n, S. (1995). The evolving model of calmodulin structure,function and activation. Structure, 3(1), 7â11.

Authors 2

Bryan E Finn (first)
Sture Forsén (additional)

References 28 Referenced 71

{'key': '10.1016/S0969-2126(01)00130-7_BIB1', 'first-page': '343', 'article-title': 'Calmodulin', 'volume': '1', 'author': 'Kawasaki', 'year': '1994', 'journal-title': 'Protein Profile'} / Protein Profile / Calmodulin by Kawasaki (1994)
10.1016/0143-4160(92)90050-3 / Cell Calcium / The linker of calmodulin –to helix or not to helix by Kretsinger (1992)
10.1038/315037a0 / Nature / Three-dimensional structure of calmodulin by Babu (1985)
10.1016/0022-2836(88)90608-0 / J. Mol. Biol / Structure of calmodulin refined at 2.2 Å resolution by Babu (1988)
10.1038/313653a0 / Nature / Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution by Herzberg (1985)
10.1126/science.3969570 / Science / Molecular structure of troponin C from chicken skeletal muscle at 3 Å resolution by Sundaralingam (1985)
10.1016/0022-2836(92)90324-D / J. Mol. Biol / Calmodulin structure refined at 1.7 Å resolution by Chattopadhyaya (1992)
10.1016/S0021-9258(18)54647-0 / J. Biol. Chem / Structure of a recombinant calmodulin from Drosophila melanogaster at 2.2-Å resolution by Taylor (1991)
10.1002/pro.5560020316 / Protein Sci / Structure of Paramecium tetraurelia calmodulin at 1.8 Å resolution by Rao (1993)
10.1038/315015a0 / Nature / Hands on the calcium switch by Schutt (1985)
10.1021/bi00345a002 / Biochemistry / Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering by Seaton (1985)
10.1021/bi00403a011 / Biochemistry / Comparison of the crystal and solution structures of calmodulin and troponin C by Heidorn (1988)
10.1016/0143-4160(92)90051-S / Cell Calcium / The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains by Trewhella (1993)
10.1021/bi00102a013 / Biochemistry / Secondary structure and side-chain 1 H and 13 C resonance assignment of calmodulin in solution by heteronuclear multi-dimensional NMR spectroscopy by Ikura (1991)
10.1021/bi00138a005 / Biochemistry / Backbone dynamics of calmodulin studies by 15 N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible by Barbato (1992)
10.1097/00005344-198806125-00002 / J. Cardiovasc. Pharm / Toward a model of the calmodulin–myosin light-chain kinase complex: implications for calmodulin function by Persechini (1988)
10.1021/bi00442a032 / Biochemistry / Changes in the Structure of Calmodulin Induced by a Peptide Based on the Calmodulin-Binding Domain of Myosin Light Chain Kinase by Heidorn (1989)
10.1016/S0021-9258(18)83149-0 / J. Biol. Chem / The effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding by Persechini (1989)
10.1126/science.1585175 / Science / Solution structure of a calmodulin-target peptide complex by multidimensional NMR by Ikura (1992)
10.1016/0143-4160(86)90010-2 / Cell Calcium / Interaction of calmodulin and its fragments with Ca2+–ATPase and myosin light-chain kinase by Szyja (1986)
10.1016/0968-0004(90)90177-D / Trends Biochem. Sci / How calmodulin binds its targets: sequence independent recognition of amphiphilic α–helices by O'Neil (1990)
10.1126/science.1519061 / Science / Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex by Meador (1992)
10.1126/science.8259515 / Science / Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures by Meador (1993)
10.1021/bi00557a025 / Biochemistry / Calcium-induced exposure of a hydrophobic surface on calmodulin by LaPorte (1980)
10.1002/prot.340030102 / Proteins / Two trifluoroperazine-binding sites on calmodulin predicted from comparative molecular modeling with troponin C by Strynadka (1988)
10.1016/0014-5793(87)81182-1 / FEBS Lett / Sequence-specific assignments of downfield-shifted amide proton resonances of calmodulin by Ikura (1987)
10.1016/0014-5793(93)80839-M / FEBS Lett / The structure of apo-calmodulin: a 1 H NMR examination of the carboxy-terminal domain by Finn (1993)
10.1016/0263-7855(88)80054-7 / J. Mol. Graphics / The MIDAS display system by Ferrin (1988)

Dates

Type	When
Created	21 years, 1 month ago (July 23, 2004, 3:10 p.m.)
Deposited	4 years, 2 months ago (June 24, 2021, 10:38 a.m.)
Indexed	2 months, 3 weeks ago (June 10, 2025, 1:48 p.m.)
Issued	30 years, 7 months ago (Jan. 1, 1995)
Published	30 years, 7 months ago (Jan. 1, 1995)
Published Print	30 years, 7 months ago (Jan. 1, 1995)

Funders 0

None

BibTeX

@article{Finn_1995, title={The evolving model of calmodulin structure,function and activation}, volume={3}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/s0969-2126(01)00130-7}, DOI={10.1016/s0969-2126(01)00130-7}, number={1}, journal={Structure}, publisher={Elsevier BV}, author={Finn, Bryan E and Forsén, Sture}, year={1995}, month=jan, pages={7–11} }

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