ライフサイエンスコーパス: troponin C

1 -induced closure of the regulatory domain of troponin C.

2 cium binding affinity of fluorescent cardiac troponin C.

3 o actin as well as increased Ca2+ binding to troponin C.

4 efects by RNA interference of tropomyosin or troponin C.

5 129-166) to the regulatory domain of cardiac troponin C.

6 crossbridge cycling on the Ca2+ affinity of troponin C.

7 n the absence of calcium-bound human cardiac troponin C.

8 tes of calmodulin as well as the EF hands of troponin C.

9 and/or S165 impedes binding of troponin I to troponin C.

10 d calcium affinity at the regulatory site of troponin C.

11 acts with the NH2-terminal domain of cardiac troponin C.

12 lation were carried over to its complex with troponin C.

13 and the mutant complexed with cardiac muscle troponin C.

14 ]free represents the amount of Ca2+ bound to troponin C.

15 re based on the C-terminal domain of Opsanus troponin C.

16 the mutant as in the case of calmodulin and troponin C.

17 d sarcomeres containing fast skeletal muscle troponin C.

18 ractions with negatively charged residues on troponin C.

19 or the proper regulatory function of cardiac troponin C.

20 e linked to the decreased Ca(2+) off-rate of troponin C.

21 etamido-tetramethylrhodamine-labeled cardiac troponin C.

22 tiated when Ca2+ binds to site II of cardiac troponin C.

23 d magnesium binding to F29W chicken skeletal troponin C.

24 f troponin I that is known to bind actin and troponin C, a homolog of CaM.

25 mixtures of up to five proteins (myoglobin, troponin C, actin, bovine serum albumin (BSA), tropomyos

26 ly changes in myosin affinity and troponin I/troponin C affinity.

27 Deletion of the first 11-14 residues of troponin C alters function.

28 ffinity (approximately 3 micromol/L) site on troponin C alters the interactions of proteins in the th

29 of CARP in cardiomyocytes suppresses cardiac troponin C and atrial natriuretic factor transcription.

30 activation is initiated by Ca(2+) binding to troponin C and augmented by strong myosin binding to act

31 with the homologous Ca(2+)-binding proteins troponin C and CaM.

32 2- and COOH-terminal domains in free cardiac troponin C and cardiac troponin C bound cardiac troponin

33 ium-saturated complex formed between cardiac troponin C and cardiac troponin I.

34 apthalenesulfonamide (W7) as an inhibitor of troponin C and compared its effects with that of the myo

35 Computer modeling of troponin C and I variables predicts that the primary def

36 sociation constants of glutamate residues on troponin C and of histidine on skeletal troponin I (His-

37 phobic sites in the N-domain of Ca(2+)-bound troponin C and release of the adjacent TnI-I from actin.

38 Extraction of skeletal troponin C and replacement with functional and mutant ca

39 17357 slows the rate of calcium release from troponin C and sensitizes muscle to calcium.

40 vity and cooperativity of calcium binding to troponin C and the activation and relaxation rates of tr

41 nd increases the rate of Ca(2+) release from troponin C and the rate of relaxation in cardiac muscle.

42 Interactions between troponin C and troponin I play a critical role in the re

43 letion mutants formed a complex with cardiac troponin C and troponin I that exhibited the same concen

44 to facilitate productive interaction between troponin C and troponin I to trigger contraction in skel

45 1-192)) was expressed and reconstituted with troponin C and troponin T to form a mutant troponin.

46 In the absence of Ca2+, the binding of troponin C and troponin T to TnI had very little effect

47 mutated cTnI together with wild-type cardiac troponin C and troponin T.

48 the TnI-1 epitope on TnI in the presence of troponin C and troponin T.

49 TnI is a subunit of the troponin complex (troponin-C and troponin-T being the other two), which, a

50 er with alpha-tropomyosin (Tpma) and cardiac troponins C and I (Tnni3), forms a calcium-sensitive reg

51 lve Ca(2+) binding to and release from cTnC (troponin C) and structural changes in cTnC and other thi

52 (b) the isolated C helix (residues 53-66) of troponin C, and (c) the C helix of the N-terminal region

53 nce from the calcium binding site in cardiac troponin C, and do not affect either the binding pocket

54 s and 30% of hetero-oligomers including Bax, Troponin C, and Early Endosome Antigen 1.

55 such as Nkx2.5, GATA4, Tbx5, dHAND, cardiac troponin C, and SM22-alpha.

56 e clone with the highest level of binding to troponin C, and the N-terminal region of troponin I isof

57 o be crosslinked products Tm*146-TnI, Tm*146-troponin C, and Tm*146-TnT using fluorescence-labeled Tn

58 isoforms of actin, tropomyosin, troponin I, troponin C, and troponin T is not affected by aging or h

59 ) dissociation from the regulatory domain of troponin C ( approximately 2.5-fold).

60 to determine incorporation of mutant cardiac troponin C ( approximately 21%) into the KI-TnC-A8V(+/-)

61 ) dissociation from the regulatory domain of troponin C ( approximately 8.1-fold), which was complete

62 e motion of the N- and C-terminal domains of troponin C are independent.

63 the regulatory N-terminal domain of skeletal troponin-C are a combination of intrinsic and induced pr

64 resonance yielded dissociation constants for troponin C as low as 0.43 microM for pT5; in contrast, d

65 rs that could minimize this concern utilizes troponin C as the Ca(2+) sensor.

66 ation of troponin I reduced its affinity for troponin C, as measured by isothermal titration microcal

67 f the endogenous Cys-84, labeling of cardiac troponin C at a novel engineered Cys-53 with 2-(4'-iodoa

68 behavior of two mutants of chicken skeletal troponin C bearing a single tryptophan residue at positi

69 Cardiac troponin C belongs to the EF-hand superfamily of calcium

70 mains in free cardiac troponin C and cardiac troponin C bound cardiac troponin I-(1-80)DD tumble inde

71 ansverse relaxation rates for intact cardiac troponin C bound to either cardiac troponin I(1-80)/trop

72 egulatory domain of Ca(2+)-saturated cardiac troponin C bound to the isolated N-domain of cardiac tro

73 esidues 81-128 do not interact strongly with troponin C but likely serve to modulate the interaction

74 d S23 troponin I showed reduced affinity for troponin C but the effect was diminished with respect to

75 ific N terminus can modulate the function of troponin C by altering the conformational equilibrium of

76 calcium affinity of the N-domain of cardiac troponin C by facilitating the movement of helices B and

77 iants identified in the TNNC1 (gene encoding troponin C) can evoke cardiac remodeling in vivo.

78 RNA interference of tropomyosin or troponin C caused sterility by inhibiting ovarian contra

79 Here, we utilized seven tight binding CaM-troponin C chimeras, which variably activate nNOS NO syn

80 he highest-ranked up-regulated gene, cardiac troponin C, codes for a neuronal calcium-binding protein

81 Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinas

82 of 2 m urea to the intact cardiac troponin I-troponin C complex significantly increased linker flexib

83 Between pCa 8-5.4 and at troponin C concentrations of 8-28 muM, the slow relaxati

84 ly 70% of the N-terminal regulatory sites of troponin C consistent with their rapid Ca2+ on-rate (8.7

85 Troponin C contains a 14-residue alpha-helix at the amin

86 nin I provides a deeper understanding of how troponin C controls signal transduction.

87 rtrophic cardiomyopathy mutations in cardiac troponin C (cTnC) (A8V, C84Y, E134D, and D145E) were rep

88 lta2-11) interact with the N lobe of cardiac troponin C (cTnC) and that phosphorylation at Ser(23/24)

89 I(1-32) interacts with the N-lobe of cardiac troponin C (cTnC) and thus is positioned to modulate myo

90 Mutations in TNNC1-encoded cardiac troponin C (cTnC) are a relatively rare cause of HCM.

91 novel mutations (G159D and L29Q) in cardiac troponin C (CTnC) associate their phenotypic outcomes wi

92 ich a double mutation (E59D/D75Y) in cardiac troponin C (CTnC) associated with dilated cardiomyopathy

93 myopathy-associated mutant D145E, in cardiac troponin C (cTnC) C-domain, causes generalised instabili

94 The solution structure of cardiac troponin C (cTnC) challenges existing structure/function

95 omplex with the C-terminal domain of cardiac troponin C (cTnC) comprising residues 81-161.

96 containing WT cardiac troponin T/I + cardiac troponin C (cTnC) D65A (a site II inactive cTnC mutant).

97 ecific enhancer-promoter of the slow/cardiac troponin C (cTnC) gene contains five protein binding reg

98 Troponin C (cTnC) interaction with cTnI (C-I interaction

99 Cardiac troponin C (cTnC) is the Ca(2+)-binding component of the

100 Cardiac troponin C (cTnC) is the calcium-dependent switch for co

101 Cardiac troponin C (cTnC) is the regulatory protein that initiat

102 ree subunits, using a monocysteine mutant of troponin C (cTnC) labeled with the fluorescent probe 2-[

103 e changes include the opening of the cardiac troponin C (cTnC) N-domain, the change of secondary stru

104 tory N-terminal domain in Ca2+-bound cardiac troponin C (cTnC) presents a much different binding surf

105 he N-terminal regulatory lobe of the cardiac troponin C (cTnC) subunit in the troponin complex.

106 residue N-terminal region that binds cardiac troponin C (cTnC) to increase the calcium sensitivity of

107 ng site in the cardiac-specific slow/cardiac troponin C (cTnC) transcriptional enhancer and overexpre

108 tetramethylrhodamine (5'ATR)-labeled cardiac troponin C (cTnC) was measured to monitor cTnC structure

109 function is initiated by binding of Ca2+ to troponin C (cTnC) which induces a series of structural c

110 ation is initiated by Ca2+ dissociation from troponin C (cTnC), followed by multiple structural chang

111 The Ca(2+) sensor of the sarcomere, cardiac troponin C (cTnC), plays an important role in regulating

112 TNNC1, which encodes cardiac troponin C (cTnC), remains elusive as a dilated cardiomy

113 e N-domain regulatory site of cardiac muscle troponin C (cTnC).

114 evosimendan, are reported to bind to cardiac troponin C (cTnC).

115 Coincident S-nitrosylation of cardiac troponin C decreases myocardial sensitivity to Ca(2+).

116 the Ca2+ affinity of the regulatory protein troponin C decreases when sarcomere length is reduced.

117 on that alternately binds to either actin or troponin C, depending on the intracellular concentration

118 hat were troponin C-replete, Ca2+ binding to troponin C did not differ at short (approximately 1.97 m

119 Chimeras that were singly substituted with troponin C domains 4, 3, 2, or 1 were increasingly unabl

120 parvalbumin, (b) fast off-rate of Ca2+ from troponin C due to an alteration in troponin, and (c) fas

121 ntration-dependent conformational changes in troponin C during systole leading to sensitization of th

122 ds that is a member of the CTER (calmodulin, troponin C, essential and regulatory myosin light chains

123 2+ sensitivity via Ca2+-dependent binding to troponin C, exerts positive inotropic and lusitropic eff

124 Fluorescence emission from cardiac troponin C(F20W/N51C)(AEDANS) complexed to cardiac tropo

125 The regulatory N-domains of cardiac troponin C(F27W) and its mutants were also able to bind

126 affinity of the regulatory domain of cardiac troponin C(F27W) approximately 2.1-15.2-fold.

127 To sensitize the N-domain of cardiac troponin C(F27W) to calcium, we individually substituted

128 and dissociation of the N-domain of cardiac troponin C(F27W).

129 on 27 with Trp, making a fluorescent cardiac troponin C(F27W).

130 on: (a) the calcium binding and dynamics of troponin C(F29W) complexed with the regulatory fragment

131 >10-fold lower affinity of calcium-saturated troponin C(F29W) for troponin I(96-148), causing a drast

132 lly affect the affinity of calcium-saturated troponin C(F29W) for troponin I(96-148).

133 duction in force recovery, even though these troponin C(F29W) mutants still bound to the thin filamen

134 48) complexes than from that of the isolated troponin C(F29W) mutants.

135 in the regulatory domain of the fluorescent troponin C(F29W) with polar Gln to examine the effects o

136 I for measuring the calcium dynamics of the troponin C(F29W)-troponin I complexes.

137 predicted from the calcium affinities of the troponin C(F29W)-troponin I(96-148) complexes than from

138 The calcium affinities of the troponin C(F29W)-troponin I(96-148) complexes varied app

139 After extracting troponin C, fibers did not generate tension following th

140 in D is due to a decrease in the affinity of troponin C for Ca2+.

141 affinity of the regulatory domain of cardiac troponin C for cardiac troponin I(129-166) and provides

142 y 8-fold decrease in the affinity of cardiac troponin C for the regulatory region of cardiac troponin

143 s minimally affected the affinity of cardiac troponin C for the regulatory region of cardiac troponin

144 d, along with functional differences between troponin C from Drosophila and vertebrates.

145 egulatory N-terminal domain of fast skeletal troponin C (fsTnC), and a substantial exposure of a hydr

146 of the N-helix are generally sufficient for troponin C function.

147 By examining the Troponin C gene family of Drosophila melanogaster, which

148 inity of hypertrophic cardiomyopathy-cardiac troponin C (HCM-cTnC) mutants.

149 ng with human cardiac troponin I (HCTnI) and troponin C (HCTnC), and the Ca(2+) dependent isometric f

150 onstituted with human cardiac troponin I and troponin C (HCTnI.TnC) complex showed a decrease in the

151 es and slower Ca(2+) dissociation rates from troponin C in all the systems studied.

152 two-stage mechanism for Ca(2+) regulation by troponin C in cardiac muscle.

153 characteristics of human recombinant cardiac troponin C in in vitro conditions.

154 examine length dependence of Ca2+ binding to troponin C in skeletal muscle, we developed a protocol t

155 The role of the C-domain sites of cardiac troponin C in the modulation of the calcium signal remai

156 trated that pT5 formed a stable complex with troponin C in the presence of calcium.

157 minants of calcium binding and exchange with troponin C in the presence of troponin I provides a deep

158 The distinct structural changes of troponin C in the thin filaments and myosin regulatory l

159 We used fluorescent probes on troponin C in the thin filaments and on myosin regulator

160 ry light chain in the thick filaments and on troponin C in the thin filaments.

161 We thus conclude that troponin C in thin filaments detects structural changes

162 n of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or

163 res of functional cardiac and mutant cardiac troponin C insensitive to calcium and permanently inacti

164 a 1:1 molar ratio of the troponin I peptide, troponin C is approximately spherical.

165 The pK(a) of Glu-19 is decreased when troponin C is bound to skeletal troponin I and the pK(a)

166 raction of mutant troponin I with Drosophila troponin C is discussed, along with functional differenc

167 echanism by which the regulatory function of troponin C is effected.

168 m-saturated troponin I peptide-bound states, troponin C is elongated, having an axial ratio of 4-5.

169 the kinetics of Ca(2+) exchange with cardiac troponin C is essential to elucidating the Ca(2+)-depend

170 se of its large muscle fibers, there are two troponin-C isoforms, called F1 and F2, that have distinc

171 g that the rate of dissociation of Ca2+ from troponin C (k(off)) is similar in the 2 species.

172 on due to the slower off-rate of Ca(2+) from troponin C leading to longer force and [Ca(2+)] transien

173 ex allergens (Ani s 1-6, 8, 9, 11 and 12 and troponin C-like protein) showed that the patient serum s

174 ur allergens (Ani s 1, Ani s 2, Ani s 12 and troponin C-like protein), possibly infested in the raw s

175 i s 1 and Ani s 12 and weakly to Ani s 2 and troponin C-like protein.

176 Here we show a large decrease in cardiac troponin C linker flexibility, corresponding to residues

177 troponin I peptide-induced length changes in troponin C may play a role in the mechanism by which the

178 regulatory N-terminal domain of full-length troponin C mutants from skeletal muscle.

179 The design of calcium-sensitizing cardiac troponin C mutants presented in this work enhances the u

180 enerated a series of chicken skeletal muscle troponin C mutants to study the conformation of the regu

181 Systems with troponin C, myosin light chain, or calmodulin as the Ca(

182 including cardiac alpha-myosin heavy chain, troponin C, myosin light chain-2v, Nkx-2.5/Csx, dHAND, e

183 filament activation, the N-domain of cardiac troponin C (N-cTnC) binds to Ca(2+) and interacts with t

184 reproduce reported effects of nonfunctional troponin C on myofilament force generation.

185 d mutations A8V, E134D, and D145E in cardiac troponin C on the properties of the C-domain sites.

186 onin [composed of TnI, troponin T (TnT), and troponin C] or with actin and TnI.

187 orrelate with partial opening of the cardiac troponin C regulatory domain previously demonstrated by

188 tion of troponin I(129-166) with the cardiac troponin C regulatory domain.

189 amino-terminus of troponin I and the cardiac troponin C regulatory domain.

190 s with and induces an opening of the cardiac troponin C regulatory domain.

191 le of inducing conformational changes in the troponin C regulatory domain.

192 In fibers that were troponin C-replete, Ca2+ binding to troponin C did not d

193 n general, and for phospholamban and cardiac troponin C S-nitrosylation, in particular, in betaAR-dep

194 er, mutation of both residues to Cys reduces troponin C's affinity for the troponin complex on the th

195 both residues 48 and 82 on opposite sides of troponin-C's (TnC's) N-terminal regulatory hydrophobic c

196 The troponin C-selected peptides yield a consensus binding s

197 /nitrogen chemical shift analysis of cardiac troponin C showed that, in the presence of cTnI-AllP and

198 of the N-terminal region (residues 1-90) of troponin C (sNTnC).

199 ns of two of the phage clone sequences bound troponin C specifically, and were specifically competed

200 of troponin I were synthesized shown to bind troponin C specifically.

201 ified 10 distinct novel sequences which bind troponin C specifically.

202 We studied how enhanced skeletal troponin C (sTnC) Ca2+-binding affinity affects cooperat

203 Changes in skeletal troponin C (sTnC) structure during thin filament activat

204 Native skeletal troponin C (sTnC) was replaced with sTnC mutants having

205 rminal lobe of cTnC, unlike that of skeletal troponin C (sTnC), contains only one functional EF-hand

206 after the first Ca(2+) ion binds to skeletal troponin C (sTnC), whereas the slower change requires Ca

207 The transition of the troponin C structure from a closed conformation to an op

208 ing cooperatively induced changes in cardiac troponin C structure, as measured by dichroism of 5' iod

209 a comparison of CaM41/75 with other CaM and troponin C structures a detailed two-step mechanism of t

210 Calbindin D28K, a member of the troponin-C superfamily of calcium-binding proteins, cont

211 lacement with mixtures of cardiac and mutant troponin C, the rate of force generation was independent

212 In the x-ray structures of troponin C there is a salt bridge between Arg 11 in the

213 roteins, including phospholamban and cardiac troponin C, thereby playing an essential and previously

214 , we found that skeletal troponin I bound to troponin C tighter at pH 6.1 than at pH 7.5.

215 Skeletal muscle troponin C (TnC) adopts an extended conformation when cr

216 rce, the rate of dissociation of Ca(2+) from troponin C (TnC) and decreased crossbridge detachment ra

217 relative contributions of Ca(2+) binding to troponin C (TnC) and myosin binding to actin in activati

218 The calcium-dependent interactions between troponin C (TnC) and other thin and thick filament prote

219 binding interaction between rabbit skeletal troponin C (TnC) and rabbit skeletal troponin I (TnI) re

220 amounts of Ca2+ on the in situ structures of troponin C (TnC) and troponin I (TnI) in whole troponin

221 o-fluorophore-based sensor, carrying Opsanus troponin C (TnC) as the Ca(2+)-binding moiety, has two b

222 Troponin C (TnC) belongs to the superfamily of EF-hand (

223 TnI consisting of residues 1-64 (I1-64) with troponin C (TnC) by isothermal titration microcalorimetr

224 n ATPase activity, and Ca(2+) binding to the troponin C (TnC) component reverses the inhibition.

225 model for teleost fish, have two paralogous troponin C (TnC) genes that are expressed in the heart d

226 The C terminal of cardiac troponin C (TnC) has two Ca2+-Mg2+ sites which exhibit a

227 idge detachment and Ca(2+) dissociation from troponin C (TnC) have been hypothesized to rate-limit my

228 ne the orientation of the C-terminal lobe of troponin C (TnC) in skeletal muscle cells as a step towa

229 troponin I (TnI) is thought to interact with troponin C (TnC) in the presence of Ca(2+) and with acti

230 44A and R81A) of rabbit fast skeletal muscle troponin C (TnC) in which the charged residues were repl

231 uction process converting calcium binding by troponin C (TnC) into interactions between thin and thic

232 Troponin C (TnC) is an EF-hand Ca(2+) binding protein th

233 Cardiac troponin C (TnC) is composed of two globular domains con

234 Troponin C (TnC) is implicated in the initiation of myoc

235 diated modifications of the Ca2+ affinity of troponin C (TnC) may explain the fluctuations in [Ca2+]i

236 tory sites by measuring the concentration of troponin C (TNC) molecules, 33.8 mumol per kg wet weight

237 reated fibers reconstituted with cardiac TnI.troponin C (TnC) or ssTnI.TnC significantly increased Ca

238 dues in the N-terminal, regulatory domain of troponin C (TnC) so we could investigate their role in t

239 a(2+) sensor for cardiac muscle contraction, troponin C (TnC) stands out as an obvious and versatile

240 nitor the effect of sarcomere length (SL) on troponin C (TnC) structure during Ca2+ activation in sin

241 Calcium binding to the troponin C (TnC) subunit causes a change in its dynamics

242 which in turn enhances Ca(2+) binding to the troponin C (TnC) subunit of the troponin complex.

243 TnT tethers troponin I (TnI) and troponin C (TnC) to the thin filament via tropomyosin (T

244 Ca(2+) binding in the NH(2)-lobe of subunit troponin C (TnC) was abolished by mutagenesis, and effec

245 er troponin components, troponin I (TnI) and troponin C (TnC) was examined by using the yeast two hyb

246 The native troponin C (TnC) was extracted and replaced with either

247 Native troponin C (TnC) was extracted from single, de-membranat

248 probes attached along four alpha helices of troponin C (TnC) was measured in permeabilized skeletal

249 rms of in vitro binding to troponin I (TnI), troponin C (TnC), actin-tropomyosin (actin-Tm), and acto

250 The switch is a dimeric complex of troponin C (TnC), an allosteric sensor for Ca(2+), and t

251 e under the control of different isoforms of troponin C (TnC), F1 and F2, which are responsible for s

252 Troponin C (TnC), present in all striated muscle, is the

253 w this signal is transmitted between TnI and troponin C (TnC), resulting in accelerated Ca(2+) releas

254 The Tn complex consists of three subunits, troponin C (TnC), troponin I (TnI), and troponin T (TnT)

255 tes of rabbit skeletal troponin I (TnI) with troponin C (TnC), troponin T (TnT), tropomyosin (Tm) and

256 Mutations in the Ca(2+) sensor, troponin C (TnC), were generated to increase/decrease th

257 reported here reflect changes in Ca bound to troponin C (TnC).

258 binding to the regulatory domain of skeletal troponin C (TnC).

259 (96-115)] free in solution and when bound to troponin C (TnC).

260 using polarized fluorescence from probes on troponin C (TnC).

261 it skeletal troponin-I (TnI) and residues in troponin-C (TnC) and in actin.

262 e binding of Ca2+ to the triggering sites in troponin-C (TnC) causes the opening of the N-terminal hy

263 e Cys133 of troponin-I (TnI) with respect to troponin-C (TnC) in the ternary troponin complex and the

264 s indirect flight muscle has two isoforms of troponin C, TnC-F1 and F2, which are unusual in having o

265 39% and 51%, troponin T to 64% and 53%, and troponin C to 73% and 97% of controls, respectively, and

266 ion of mutant troponin T with troponin I and troponin C to form an active troponin complex.

267 The ability of calcium-bound human cardiac troponin C to neutralize the inhibition of K206I was gre

268 nt proteins influence the ability of cardiac troponin C to sense and respond to Ca(2+).

269 cific adapter to couple the Ca(2+) receptor, troponin C, to the actin-myosin contractile machinery.

270 tigated the functional overlap of two muscle Troponin C (TpnC) genes that are expressed in the adult

271 -dependent network to the interactions among troponin C, troponin I, and actin is discussed in light

272 al regions of troponin T (TnT) interact with troponin C, troponin I, and tropomyosin to regulate stri

273 Western immunoblots for actin, tropomyosin, troponin C, troponin T, myosin light chain-1, and myosin

274 ractions are comparable to those observed in troponin C-troponin I complexes.

275 e to troponin I(129-166) binding the cardiac troponin C/troponin I(1-80) complex correlate with parti

276 rdiac troponin I(129-166) binding to cardiac troponin C/troponin I(1-80) was 43.3 +/- 3.2 microM.

277 ar magnetic resonance studies of the cardiac troponin C/troponin I(1-80)/troponin I(129-166) complex

278 he NH2- and COOH-terminal domains of cardiac troponin C tumble with similar correlation times when bo

279 onformational and dynamic changes in cardiac troponin C upon binding a phosphomimetic troponin I, hav

280 m dissociation from the regulatory domain of troponin C upon incorporation into the troponin complex.

281 regulatory regions of Aldolase A and Cardiac troponin C via Trex/MEF3 sites.

282 rescence was significantly greater than when troponin C was present.

283 From ED5 to 15, troponin C was the major Ca(2+) binding moiety, followed

284 When the presence of calcium-insensitive troponin-C was simulated in the model, both calcium sens

285 -terminal domain (N-domain) of human cardiac troponin C, we substituted Phe at position 27 with Trp,

286 to photolysis and the subsequent binding to troponin C were assessed using a Ca2+ fluorophore.

287 Tropomyosin and troponin C were associated with actin filaments in the m

288 en/deuterium exchange rates in the C-lobe of troponin C were compared in complexes containing either

289 changes in the regulatory domain of cardiac troponin C were monitored in complexes with troponin I-(

290 placement with functional and mutant cardiac troponin C were used to evaluate the relationship betwee

291 cium and the mobile segment of troponin-I to troponin-C were described by a simple kinetic scheme.

292 gulatory domain of calcium-saturated cardiac troponin C when bound to the NH2-terminal domain of card

293 e contraction is caused by Ca(2+) binding to troponin C, which triggers the cross-bridge power stroke

294 lcium binding to the calcium sensory protein troponin-C, which is one of the three components of the

295 myoepithelial sheath, and the association of troponin C with actin was dependent on tropomyosin.

296 decrease in the unbinding rate of calcium to troponin C with increasing active tension was much lower

297 n for a new system: the N-terminal domain of Troponin C with its natural substrate Ca2+.

298 (corresponding to residues 34-71) to cardiac troponin C with the D145E mutation was not able to recov

299 keletal calcium-binding subunit of troponin, troponin C, with mixtures of functional cardiac and muta

300 bridge kinetics and Ca(2+) dissociation from troponin C work together to modulate the rate of cardiac