Crossref
journal-article
Elsevier BV
Cell Calcium (78)
References
78
Referenced
32
{'key': '10.1016/0143-4160(92)90051-S_BIB1', 'series-title': 'Calcium Transport in Contraction and Secretion', 'first-page': '469', 'article-title': 'Hypothesis: calcium modulated proteins contain EF hands', 'author': 'Kretsinger', 'year': '1975'}
/ Calcium Transport in Contraction and Secretion / Hypothesis: calcium modulated proteins contain EF hands by Kretsinger (1975)10.1126/science.6243188
/ Science / Calmodulin plays a pivotal role in cellular regulation by Cheung (1980)10.1021/bi00557a025
/ Biochemistry / Calcium-induced exposure of a hydrophobic surface on calmodulin by La Porte (1980)10.1016/S0021-9258(19)70253-1
/ J. Biol. Chem. / Hydrophobic regions function in calmodulin-enzyme(s) interactions by Tanaka (1980){'key': '10.1016/0143-4160(92)90051-S_BIB5', 'series-title': 'Small-Angle X-ray Scattering', 'first-page': '239', 'article-title': 'Proteins', 'author': 'Pilz', 'year': '1982'}
/ Small-Angle X-ray Scattering / Proteins by Pilz (1982){'key': '10.1016/0143-4160(92)90051-S_BIB6', 'author': 'Feigen', 'year': '1987'}
by Feigen (1987)10.1021/bi00403a011
/ Biochemistry / Comparison of the crystal and solution structures of calmodulin and troponin C by Heidorn (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)10.1021/bi00492a003
/ Biochemistry / Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase by Trewhella (1990){'key': '10.1016/0143-4160(92)90051-S_BIB10', 'first-page': '329', 'article-title': 'Low-resolution structural studies of proteins in solution: calmodulin', 'volume': '6', 'author': 'Heidorn', 'year': '1990', 'journal-title': 'Comm. Mol. Cell. Biophys.'}
/ Comm. Mol. Cell. Biophys. / Low-resolution structural studies of proteins in solution: calmodulin by Heidorn (1990){'key': '10.1016/0143-4160(92)90051-S_BIB11', 'series-title': 'Small-Angle X-ray Scattering', 'first-page': '167', 'article-title': 'Interpretation', 'author': 'Glatter', 'year': '1982'}
/ Small-Angle X-ray Scattering / Interpretation by Glatter (1982)10.1016/0022-2836(75)90131-X
/ J. Mol. Biol. / Comparison of neutron and X-ray scattering of dilute myoglobin solutions by Ibel (1975)10.1021/bi00345a002
/ Biochemistry / Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle scattering by Seaton (1985)10.1107/S0021889887086497
/ J. Appl. Crystallogr. / X-ray scattering from a troponin C solution and its interpretation with a dumbbell-shaped molecule model by Fujisawa (1987)10.1093/oxfordjournals.jbchem.a122672
/ J. Biochem. / Structural change of the troponin C molecule upon Ca2+ binding measured in solution by the X-ray scattering technique by Fujisawa (1989)10.1016/S0021-9258(18)68902-1
/ J. Biol. Chem. / Small-angle scattering investigation of the solution structure of troponin C by Hubbard (1988)10.1021/bi00437a044
/ Biochemistry / pH-dependent conformational changes of wheat germ calmodulin by Wang (1989){'key': '10.1016/0143-4160(92)90051-S_BIB18', 'first-page': '3364', 'article-title': 'Effect of pH on the distance between Met-25 and Cys-98 of troponin C', 'volume': '24', 'author': 'Wang', 'year': '1985', 'journal-title': 'Biochemistry'}
/ Biochemistry / Effect of pH on the distance between Met-25 and Cys-98 of troponin C by Wang (1985)10.1016/S0021-9258(18)47981-1
/ J. Biol. Chem. / pH-dependent structural transition in rabbit skeletal troponin C by Wang (1987)10.1021/bi00235a018
/ Biochemistry / Distance distributions and anisotropy decays of troponin C and its complexes with troponin I by Cheung (1991)10.1016/S0021-9258(18)37733-0
/ J. Biol. Chem. / The central helix of calmodulin functions as a flexible tether by Persechini (1988)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)10.1016/S0021-9258(19)39658-9
/ J. Biol. Chem. / Calmodulin activation of target enzymes: consequences of deletions in the central helix by VanBerkum (1990)10.1016/S0021-9258(19)67653-2
/ J. Biol. Chem. / Effects of mutations in the central helix of troponin C on its biological activity by Sheng (1991)10.1021/bi00243a008
/ Biochemistry / Analysis of regulatory and structural defects of troponin C central helix mutants by Drobowolski (1991)10.1002/bip.360260409
/ Biopolymers / Conformational transitions of calmodulin as studied by vacuum-UV CD by Hennessey (1981)10.1042/bj2380485
/ Biochem. J. / The effects of Ca2+ and Cd2+ on the secondary and tertiary structure of bovine testis calmodulin by Martin (1986)10.1016/0014-5793(88)80225-4
/ FEBS Lett. / The conformation of calmodulin: a substantial environmentally sensitive helical transition in Ca4-calmodulin with potential mechanistic function by Bayley (1988)10.1021/bi00431a038
/ Biochemistry / Glycation of calmodulin: chemistry and structural and functional consequences by Kowluru (1989)10.1016/S0065-3233(08)60470-2
/ Calmodulin. Adv. Prot. Chem. by Klee (1982)10.1021/bi00102a013
/ Biochemistry / Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy by Ikura (1991)10.1016/S0021-9258(17)35835-0
/ J. Biol. Chem. / A model for the Ca2+-induced conformational transition of troponin C by Herzberg (1986){'key': '10.1016/0143-4160(92)90051-S_BIB33', 'first-page': '17', 'article-title': 'Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modelling with troponin C', 'volume': '3', 'author': 'Strynadka', 'year': '1988', 'journal-title': 'Prot. Struct. Func. Genet.'}
/ Prot. Struct. Func. Genet. / Two trifluoperazine-binding sites on calmodulin predicted from comparative molecular modelling with troponin C by Strynadka (1988)10.1021/bi00429a052
/ Biochemistry / Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: effects of Ca2+ and Mg2+ binding by Trewhella (1989)10.1016/0006-291X(83)91016-1
/ Biochem. Biophys. Res. Commun. / Protein structure by Fourier transform infrared spectroscopy: second derivative spectra by Susi (1983)10.1002/bip.360250307
/ Biopolymers / Examination of the secondary structure of proteins by deconvolved FTIR spectra by Byler (1986)10.1002/bip.1972.360110506
/ Biopolymers / The conformation of poly-l-alanine in hexafluoroisopropanol by Parrish (1972)10.1038/306281a0
/ Nature / Solvent induced distortions and the curvature of α-helices by Blundell (1983)10.1016/0022-2836(88)90608-0
/ J. Mol. Biol. / Structure of calmodulin refined at 2.2 Å resolution by Babu (1988)10.1016/S0021-9258(19)77925-3
/ J. Biol. Chem. / Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-Å resolution by Satyshur (1988)10.1021/bi00104a016
/ Biochemistry / Fourier transform infrared spectroscopic studies of Ca2+ binding proteins by Jackson (1991)10.1021/bi00372a038
/ Biochemistry / Amino acid sequence of rabbit skeletal muscle myosin light chain kinase by Takio (1986)10.1016/S0021-9258(18)45302-1
/ J. Biol. Chem. / Rabbit skeletal muscle myosin light chain kinase: the calmodulin binding domain as a potential active site-directed inhibitory domain by Kennelly (1987){'key': '10.1016/0143-4160(92)90051-S_BIB44', 'first-page': '341', 'article-title': 'Calmodulin-binding domains on target proteins', 'volume': 'Vol. 5', 'author': 'Blumenthal', 'year': '1988'}
/ Calmodulin-binding domains on target proteins by Blumenthal (1988)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){'key': '10.1016/0143-4160(92)90051-S_BIB46', 'first-page': '3187', 'article-title': 'Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase', 'volume': '82', 'author': 'Blumenthal', 'year': '1985'}
/ Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase by Blumenthal (1985)10.1021/bi00348a047
/ Biochemistry / Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formation by Klevit (1985){'key': '10.1016/0143-4160(92)90051-S_BIB48', 'series-title': 'Proceedings of the 5th International Symposium on Calcium Binding Proteins in Health and Disease', 'first-page': '333', 'article-title': '1H NMR studies of calmodulin-peptide interactions', 'author': 'Klevit', 'year': '1987'}
/ Proceedings of the 5th International Symposium on Calcium Binding Proteins in Health and Disease / 1H NMR studies of calmodulin-peptide interactions by Klevit (1987)10.1021/bi00392a046
/ Biochemistry / Properties of a monoclonal antibody directed to the calmodulin-binding domain of rabbit skeletal muscle myosin light chain kinase by Nunnally (1987)10.1021/bi00236a024
/ Biochemistry / Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light chain kinase: indication of a conformational change in the central helix by Ikura (1991)10.1021/bi00435a057
/ Biochemistry / Structural characterization of the interactions between calmodulin and skeletal muscle myosin light chain kinase: effect of peptide (576–594)G binding on the Ca2+-binding domain by Seeholzer (1989)10.1016/0003-9861(90)90003-H
/ Arch. Biochem. Biophys. / The interaction of calmodulin with the C-terminal M5 peptide of myosin light chain kinase by Garone (1990)10.1021/bi00106a003
/ Biochemistry / Structure of smooth muscle myosin light chain kinase calmodulin-binding domain peptide bound to calmodulin by Roth (1991)10.1016/S0021-9258(18)67601-X
/ J. Biol. Chem. / Genetically engineered calmodulins differentially activate target enzymes by Putkey (1986)10.1097/00005344-198800125-00002
/ J. Cardiovasc. Pharmacol. / Toward a model of the calmodulin-myosin light chain kinase complex: implications for calmodulin function by Persechini (1988)10.1002/prot.340060311
/ Prot. Struct. Func. Genet. / The interaction of calmodulin with fluorescent and photoreactive modelpeptides: evidence for a short interdomain separation by O'Neil (1989)10.1002/prot.340070305
/ Prot. Struct. Func. Genet. / Model for the interaction of amphiphilic helices with troponin C and calmodulin by Strynadka (1990){'key': '10.1016/0143-4160(92)90051-S_BIB58', 'first-page': '6944', 'article-title': 'Melittin binding causes a large calcium-dependent conformational change in calmodulin', 'volume': '86', 'author': 'Kataoka', 'year': '1989'}
/ Melittin binding causes a large calcium-dependent conformational change in calmodulin by Kataoka (1989)10.1016/S0021-9258(19)47170-6
/ J. Biol. Chem. / Calcium-induced shape change of calmodulin with mastoparan studied by solution X-ray scattering by Yoshino (1989)10.1021/bi00239a024
/ Biochemistry / Small-angle X-ray scattering study of calmodulin bound to two peptides corresponding to parts of the calmodulin-binding domain of the plasma membrane Ca2+-pump by Kataoka (1991)10.1021/bi00454a008
/ Biochemistry / Interaction of calmodulin with the calmodulin-binding domain of the plasma membrane Ca2+-pump by Voherr (1988){'key': '10.1016/0143-4160(92)90051-S_BIB62', 'first-page': '395', 'article-title': 'Phosphorylase kinase', 'volume': 'Vol 17', 'author': 'Picket-Gies', 'year': '1986'}
/ Phosphorylase kinase by Picket-Gies (1986)10.1111/j.1432-1033.1980.tb04971.x
/ Eur. J. Biochem. / Phosphorylase kinase from rabbit skeletal muscle: identification of the calmodulin-binding subunits by Picton (1980)10.1016/B978-0-12-152814-0.50008-3
/ Curr. Top. Cell. Regul. / The role of cyclic-AMP-dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle by Cohen (1978)10.1016/S0021-9258(17)35869-6
/ J. Biol. Chem. / Analyses of phosphorylase kinase by transmission and scanning transmission electron microscopy by Trempe (1986)10.1021/bi00438a004
/ Biochemistry / Direct observation of phosphorylase kinase and phosphorylase b by scanning tunnelling microscopy by Edstrom (1989)10.1016/S0006-3495(90)82489-9
/ Biophys. J. / Direct visualization of phosphorylase-phosphorylase kinase complexes by scanning tunnelling and atomic force microscopy by Edstrom (1990)10.1021/bi00117a019
/ Biochemistry / Solution structure of phosphorylase kinase studied using small-angle X-ray and neutron scattering by Henderson (1991)10.1016/S0021-9258(18)71472-5
/ J. Biol. Chem. / The γ-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin by Dasgupta (1989)- Blumenthal DK. Trewhella J. Unpublished observations.
10.1038/336215a0
/ Nature / Structural changes in glycogen phosphorylase induced by phosphorylation by Sprang (1988){'key': '10.1016/0143-4160(92)90051-S_BIB72', 'article-title': 'Troponin C shows conformational flexibility when complexed with various peptides: differences and similarities with calmodulin', 'author': 'Blechner', 'year': '1992', 'journal-title': 'Biochemistry'}
/ Biochemistry / Troponin C shows conformational flexibility when complexed with various peptides: differences and similarities with calmodulin by Blechner (1992)10.1042/bj1530375
/ Biochem. J. / The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit by Syska (1976)10.1016/S0021-9258(19)69684-5
/ J. Biol. Chem. / Synthetic studies on the inhibitory region of rabbit skeletal troponin I by Talbot (1981)10.1016/0014-5793(82)81303-3
/ FEBS Lett. / Interaction between troponin I and troponin C by Dalgarno (1982)10.1021/bi00286a024
/ Biochemistry / Calcium-dependent inhibitory region of troponin: a proton nuclear magnetic resonance study on the interaction between troponin C and the synthetic peptide Nα-acetyl[FPhe106]TnI-(104–115)amide by Cachia (1983)10.1016/S0021-9258(18)92763-8
/ J. Biol. Chem. / Cross-linding of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I by Kobyashi (1991){'key': '10.1016/0143-4160(92)90051-S_BIB78', 'first-page': '7258', 'article-title': 'Functional and structural similarities between the inhibitory region of troponin I coded by exon VII and the calmodulin-regulatory region of the catalytic subunit of phosphorylase kinase', 'volume': '87', 'author': 'Paudel', 'year': '1990'}
/ Functional and structural similarities between the inhibitory region of troponin I coded by exon VII and the calmodulin-regulatory region of the catalytic subunit of phosphorylase kinase by Paudel (1990)
Dates
Type | When |
---|---|
Created | 21 years, 4 months ago (April 17, 2004, 2:47 p.m.) |
Deposited | 4 years, 2 months ago (June 15, 2021, 5:30 p.m.) |
Indexed | 1 year, 7 months ago (Jan. 27, 2024, 4:55 a.m.) |
Issued | 33 years, 2 months ago (June 1, 1992) |
Published | 33 years, 2 months ago (June 1, 1992) |
Published Print | 33 years, 2 months ago (June 1, 1992) |
@article{Trewhella_1992, title={The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains}, volume={13}, ISSN={0143-4160}, url={http://dx.doi.org/10.1016/0143-4160(92)90051-s}, DOI={10.1016/0143-4160(92)90051-s}, number={6–7}, journal={Cell Calcium}, publisher={Elsevier BV}, author={Trewhella, J.}, year={1992}, month=jun, pages={377–390} }