Crossref journal-article
Elsevier BV
Cell Calcium (78)
Bibliography

Trewhella, J. (1992). The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains. Cell Calcium, 13(6–7), 377–390.

Authors 1
  1. J. Trewhella (first)
References 78 Referenced 32
  1. {'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)
  2. 10.1126/science.6243188 / Science / Calmodulin plays a pivotal role in cellular regulation by Cheung (1980)
  3. 10.1021/bi00557a025 / Biochemistry / Calcium-induced exposure of a hydrophobic surface on calmodulin by La Porte (1980)
  4. 10.1016/S0021-9258(19)70253-1 / J. Biol. Chem. / Hydrophobic regions function in calmodulin-enzyme(s) interactions by Tanaka (1980)
  5. {'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)
  6. {'key': '10.1016/0143-4160(92)90051-S_BIB6', 'author': 'Feigen', 'year': '1987'} by Feigen (1987)
  7. 10.1021/bi00403a011 / Biochemistry / Comparison of the crystal and solution structures of calmodulin and troponin C by Heidorn (1988)
  8. 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)
  9. 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)
  10. {'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)
  11. {'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)
  12. 10.1016/0022-2836(75)90131-X / J. Mol. Biol. / Comparison of neutron and X-ray scattering of dilute myoglobin solutions by Ibel (1975)
  13. 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)
  14. 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)
  15. 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)
  16. 10.1016/S0021-9258(18)68902-1 / J. Biol. Chem. / Small-angle scattering investigation of the solution structure of troponin C by Hubbard (1988)
  17. 10.1021/bi00437a044 / Biochemistry / pH-dependent conformational changes of wheat germ calmodulin by Wang (1989)
  18. {'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)
  19. 10.1016/S0021-9258(18)47981-1 / J. Biol. Chem. / pH-dependent structural transition in rabbit skeletal troponin C by Wang (1987)
  20. 10.1021/bi00235a018 / Biochemistry / Distance distributions and anisotropy decays of troponin C and its complexes with troponin I by Cheung (1991)
  21. 10.1016/S0021-9258(18)37733-0 / J. Biol. Chem. / The central helix of calmodulin functions as a flexible tether by Persechini (1988)
  22. 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)
  23. 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)
  24. 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)
  25. 10.1021/bi00243a008 / Biochemistry / Analysis of regulatory and structural defects of troponin C central helix mutants by Drobowolski (1991)
  26. 10.1002/bip.360260409 / Biopolymers / Conformational transitions of calmodulin as studied by vacuum-UV CD by Hennessey (1981)
  27. 10.1042/bj2380485 / Biochem. J. / The effects of Ca2+ and Cd2+ on the secondary and tertiary structure of bovine testis calmodulin by Martin (1986)
  28. 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)
  29. 10.1021/bi00431a038 / Biochemistry / Glycation of calmodulin: chemistry and structural and functional consequences by Kowluru (1989)
  30. 10.1016/S0065-3233(08)60470-2 / Calmodulin. Adv. Prot. Chem. by Klee (1982)
  31. 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)
  32. 10.1016/S0021-9258(17)35835-0 / J. Biol. Chem. / A model for the Ca2+-induced conformational transition of troponin C by Herzberg (1986)
  33. {'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)
  34. 10.1021/bi00429a052 / Biochemistry / Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: effects of Ca2+ and Mg2+ binding by Trewhella (1989)
  35. 10.1016/0006-291X(83)91016-1 / Biochem. Biophys. Res. Commun. / Protein structure by Fourier transform infrared spectroscopy: second derivative spectra by Susi (1983)
  36. 10.1002/bip.360250307 / Biopolymers / Examination of the secondary structure of proteins by deconvolved FTIR spectra by Byler (1986)
  37. 10.1002/bip.1972.360110506 / Biopolymers / The conformation of poly-l-alanine in hexafluoroisopropanol by Parrish (1972)
  38. 10.1038/306281a0 / Nature / Solvent induced distortions and the curvature of α-helices by Blundell (1983)
  39. 10.1016/0022-2836(88)90608-0 / J. Mol. Biol. / Structure of calmodulin refined at 2.2 Å resolution by Babu (1988)
  40. 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)
  41. 10.1021/bi00104a016 / Biochemistry / Fourier transform infrared spectroscopic studies of Ca2+ binding proteins by Jackson (1991)
  42. 10.1021/bi00372a038 / Biochemistry / Amino acid sequence of rabbit skeletal muscle myosin light chain kinase by Takio (1986)
  43. 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)
  44. {'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)
  45. 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)
  46. {'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)
  47. 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)
  48. {'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)
  49. 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)
  50. 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)
  51. 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)
  52. 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)
  53. 10.1021/bi00106a003 / Biochemistry / Structure of smooth muscle myosin light chain kinase calmodulin-binding domain peptide bound to calmodulin by Roth (1991)
  54. 10.1016/S0021-9258(18)67601-X / J. Biol. Chem. / Genetically engineered calmodulins differentially activate target enzymes by Putkey (1986)
  55. 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)
  56. 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)
  57. 10.1002/prot.340070305 / Prot. Struct. Func. Genet. / Model for the interaction of amphiphilic helices with troponin C and calmodulin by Strynadka (1990)
  58. {'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)
  59. 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)
  60. 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)
  61. 10.1021/bi00454a008 / Biochemistry / Interaction of calmodulin with the calmodulin-binding domain of the plasma membrane Ca2+-pump by Voherr (1988)
  62. {'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)
  63. 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)
  64. 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)
  65. 10.1016/S0021-9258(17)35869-6 / J. Biol. Chem. / Analyses of phosphorylase kinase by transmission and scanning transmission electron microscopy by Trempe (1986)
  66. 10.1021/bi00438a004 / Biochemistry / Direct observation of phosphorylase kinase and phosphorylase b by scanning tunnelling microscopy by Edstrom (1989)
  67. 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)
  68. 10.1021/bi00117a019 / Biochemistry / Solution structure of phosphorylase kinase studied using small-angle X-ray and neutron scattering by Henderson (1991)
  69. 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)
  70. Blumenthal DK. Trewhella J. Unpublished observations.
  71. 10.1038/336215a0 / Nature / Structural changes in glycogen phosphorylase induced by phosphorylation by Sprang (1988)
  72. {'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)
  73. 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)
  74. 10.1016/S0021-9258(19)69684-5 / J. Biol. Chem. / Synthetic studies on the inhibitory region of rabbit skeletal troponin I by Talbot (1981)
  75. 10.1016/0014-5793(82)81303-3 / FEBS Lett. / Interaction between troponin I and troponin C by Dalgarno (1982)
  76. 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)
  77. 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)
  78. {'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)
Funders 0

None

@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} }