Ranieri-Raggi M, Montali U, Ronca F, Sabbatini A, BROWN P, Moir A
Biochem J. 1997; 326 ( Pt 3):641-8.
PMID: 9307011
PMC: 1218716.
DOI: 10.1042/bj3260641.
Gusev N, Dobrovolskii A, Severin S
Biochem J. 1980; 189(2):219-26.
PMID: 7458911
PMC: 1161992.
DOI: 10.1042/bj1890219.
Moir A, Solaro R, PERRY S
Biochem J. 1980; 185(2):505-13.
PMID: 7396829
PMC: 1161379.
DOI: 10.1042/bj1850505.
Risnik V, Dobrovolskii A, Gusev N, Severin S
Biochem J. 1980; 191(3):851-4.
PMID: 7283976
PMC: 1162285.
DOI: 10.1042/bj1910851.
Barskaya N, Gusev N
Biochem J. 1982; 207(2):185-92.
PMID: 7159379
PMC: 1153847.
DOI: 10.1042/bj2070185.
Proton-magnetic-resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin.
Grand R, Levine B, PERRY S
Biochem J. 1982; 203(1):61-8.
PMID: 7103951
PMC: 1158193.
DOI: 10.1042/bj2030061.
Studies of the interaction of troponin I with proteins of the I-filament and calmodulin.
Moir A, Ordidge M, Grand R, Trayer I, PERRY S
Biochem J. 1983; 209(2):417-26.
PMID: 6847627
PMC: 1154108.
DOI: 10.1042/bj2090417.
Some properties of cardiac troponin T structure.
Gusev N, Barskaya N, Verin A, Duzhenkova I, Khuchua Z, Zheltova A
Biochem J. 1983; 213(1):123-9.
PMID: 6615417
PMC: 1152098.
DOI: 10.1042/bj2130123.
Preparation of azidocalmodulin: a photoaffinity label for calmodulin-binding proteins.
Andreasen T, Keller C, LaPorte D, EDELMAN A, Storm D
Proc Natl Acad Sci U S A. 1981; 78(5):2782-5.
PMID: 6265911
PMC: 319441.
DOI: 10.1073/pnas.78.5.2782.
The binding of calmodulin to myelin basic protein and histone H2B.
Grand R, PERRY S
Biochem J. 1980; 189(2):227-40.
PMID: 6161607
PMC: 1161993.
DOI: 10.1042/bj1890227.
Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle.
Wang C, Cheung H
Biophys J. 1985; 48(5):727-39.
PMID: 4074834
PMC: 1329398.
DOI: 10.1016/S0006-3495(85)83831-5.
Comparison of the structure of two cardiac troponin T isoforms.
Risnik V, Verin A, Gusev N
Biochem J. 1985; 225(2):549-52.
PMID: 3977845
PMC: 1144623.
DOI: 10.1042/bj2250549.
Distance distributions in proteins recovered by using frequency-domain fluorometry. Applications to troponin I and its complex with troponin C.
Lakowicz J, Gryczynski I, Cheung H, Wang C, Johnson M, Joshi N
Biochemistry. 1988; 27(26):9149-60.
PMID: 3242618
PMC: 6923757.
DOI: 10.1021/bi00426a012.
Distance distributions and anisotropy decays of troponin C and its complex with troponin I.
Cheung H, Wang C, Gryczynski I, Wiczk W, Laczko G, Johnson M
Biochemistry. 1991; 30(21):5238-47.
PMID: 2036391
PMC: 6868476.
DOI: 10.1021/bi00235a018.
The primary structure of troponin T and the interaction with tropomyosin.
Jackson P, Amphlett G, PERRY S
Biochem J. 1975; 151(1):85-97.
PMID: 1212216
PMC: 1172328.
DOI: 10.1042/bj1510085.
The amino acid sequence of troponin I from rabbit skeletal muscle.
Wilkinson J, Grand R
Biochem J. 1975; 149(2):493-6.
PMID: 1180911
PMC: 1165646.
The amino acid sequence of rabbit cardiac troponin I.
Grand R, Wilkinson J
Biochem J. 1976; 159(3):633-41.
PMID: 1008822
PMC: 1164163.
DOI: 10.1042/bj1590633.
Affinity-chromatographic isolation and some properties of troponin C from different muscle types.
Head J, Weeks R, PERRY S
Biochem J. 1977; 161(3):465-71.
PMID: 851428
PMC: 1164530.
DOI: 10.1042/bj1610465.
The phosphorylation sites of troponin T from white skeletal muscle and the effects of interaction with troponin C on their phosphorylation by phosphorylase kinase.
Moir A, Cole H, PERRY S
Biochem J. 1977; 161(2):371-82.
PMID: 849266
PMC: 1164514.
DOI: 10.1042/bj1610371.
The components of troponin from chicken fast skeletal muscle. A comparison of troponin T and troponin I from breast and leg muscle.
Wilkinson J
Biochem J. 1978; 169(1):229-38.
PMID: 629749
PMC: 1184213.
DOI: 10.1042/bj1690229.
