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1 ortant for the proper regulatory function of cardiac troponin C.
2 ' iodoacetamido-tetramethylrhodamine-labeled cardiac troponin C.
3 n is initiated when Ca2+ binds to site II of cardiac troponin C.
4 the calcium binding affinity of fluorescent cardiac troponin C.
5 tivity in the absence of calcium-bound human cardiac troponin C.
6 ponin I(129-166) to the regulatory domain of cardiac troponin C.
7 I interacts with the NH2-terminal domain of cardiac troponin C.
8 ression of CARP in cardiomyocytes suppresses cardiac troponin C and atrial natriuretic factor transcr
9 , the NH2- and COOH-terminal domains in free cardiac troponin C and cardiac troponin C bound cardiac
11 minal deletion mutants formed a complex with cardiac troponin C and troponin I that exhibited the sam
13 , together with alpha-tropomyosin (Tpma) and cardiac troponins C and I (Tnni3), forms a calcium-sensi
14 nt distance from the calcium binding site in cardiac troponin C, and do not affect either the binding
16 as used to determine incorporation of mutant cardiac troponin C ( approximately 21%) into the KI-TnC-
17 beling of the endogenous Cys-84, labeling of cardiac troponin C at a novel engineered Cys-53 with 2-(
19 minal domains in free cardiac troponin C and cardiac troponin C bound cardiac troponin I-(1-80)DD tum
20 (15)N transverse relaxation rates for intact cardiac troponin C bound to either cardiac troponin I(1-
21 in the regulatory domain of Ca(2+)-saturated cardiac troponin C bound to the isolated N-domain of car
22 ease the calcium affinity of the N-domain of cardiac troponin C by facilitating the movement of helic
23 um binding to the single, regulatory site of cardiac troponin C by measuring the rates of calcium-med
26 new hypertrophic cardiomyopathy mutations in cardiac troponin C (cTnC) (A8V, C84Y, E134D, and D145E)
27 cTnI(Delta2-11) interact with the N lobe of cardiac troponin C (cTnC) and that phosphorylation at Se
29 tion, TnI(1-32) interacts with the N-lobe of cardiac troponin C (cTnC) and thus is positioned to modu
32 ms by which a double mutation (E59D/D75Y) in cardiac troponin C (CTnC) associated with dilated cardio
33 c cardiomyopathy-associated mutant D145E, in cardiac troponin C (cTnC) C-domain, causes generalised i
35 binary complex with the C-terminal domain of cardiac troponin C (cTnC) comprising residues 81-161.
36 and cTn containing WT cardiac troponin T/I + cardiac troponin C (cTnC) D65A (a site II inactive cTnC
37 uscle-specific enhancer-promoter of the slow/cardiac troponin C (cTnC) gene contains five protein bin
41 These changes include the opening of the cardiac troponin C (cTnC) N-domain, the change of second
42 e regulatory N-terminal domain in Ca2+-bound cardiac troponin C (cTnC) presents a much different bind
43 2+) to the N-terminal regulatory lobe of the cardiac troponin C (cTnC) subunit in the troponin comple
44 ique 31-residue N-terminal region that binds cardiac troponin C (cTnC) to increase the calcium sensit
45 r 85 in the N-terminal hydrophobic region of cardiac troponin C (cTnC) to provide specific sites for
46 in binding site in the cardiac-specific slow/cardiac troponin C (cTnC) transcriptional enhancer and o
48 m of 5'-tetramethylrhodamine (5'ATR)-labeled cardiac troponin C (cTnC) was measured to monitor cTnC s
57 calcium affinity of the regulatory domain of cardiac troponin C(F27W) approximately 2.1-15.2-fold.
61 binding affinity of the regulatory domain of cardiac troponin C for cardiac troponin I(129-166) and p
62 oximately 8-fold decrease in the affinity of cardiac troponin C for the regulatory region of cardiac
63 mutations minimally affected the affinity of cardiac troponin C for the regulatory region of cardiac
68 th mixtures of functional cardiac and mutant cardiac troponin C insensitive to calcium and permanentl
69 eins on the kinetics of Ca(2+) exchange with cardiac troponin C is essential to elucidating the Ca(2+
72 ac thin-filament activation, the N-domain of cardiac troponin C (N-cTnC) binds to Ca(2+) and interact
73 hy-linked mutations A8V, E134D, and D145E in cardiac troponin C on the properties of the C-domain sit
74 omplex correlate with partial opening of the cardiac troponin C regulatory domain previously demonstr
78 ation, in general, and for phospholamban and cardiac troponin C S-nitrosylation, in particular, in be
79 e proton/nitrogen chemical shift analysis of cardiac troponin C showed that, in the presence of cTnI-
80 dge binding cooperatively induced changes in cardiac troponin C structure, as measured by dichroism o
81 ndling proteins, including phospholamban and cardiac troponin C, thereby playing an essential and pre
86 tions due to troponin I(129-166) binding the cardiac troponin C/troponin I(1-80) complex correlate wi
87 ) for cardiac troponin I(129-166) binding to cardiac troponin C/troponin I(1-80) was 43.3 +/- 3.2 mic
88 eronuclear magnetic resonance studies of the cardiac troponin C/troponin I(1-80)/troponin I(129-166)
89 t both the NH2- and COOH-terminal domains of cardiac troponin C tumble with similar correlation times
90 entify conformational and dynamic changes in cardiac troponin C upon binding a phosphomimetic troponi
92 latory N-terminal domain (N-domain) of human cardiac troponin C, we substituted Phe at position 27 wi
93 mational changes in the regulatory domain of cardiac troponin C were monitored in complexes with trop
94 C and replacement with functional and mutant cardiac troponin C were used to evaluate the relationshi
95 n the regulatory domain of calcium-saturated cardiac troponin C when bound to the NH2-terminal domain
96 ponin I (corresponding to residues 34-71) to cardiac troponin C with the D145E mutation was not able
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