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1 in a computational model of loss of cMyBP-C (myosin binding protein-C).
2 with cardiac troponins and cMyBP-C (cardiac myosin-binding protein C).
3 7 (beta-myosin heavy chain) and MYBPC3 (beta-myosin-binding protein C).
4 ost probably related to reduced abundance of myosin binding protein C.
5 cardiac sarcomere or from the truncation of myosin binding protein C.
6 response to Ca(2+) with glutathionylation of myosin binding protein C.
7 ms of the thick-filament-associated protein, myosin binding protein-C.
8 orylation of the myofilament protein cardiac myosin binding protein-C.
9 thers, filamin C and the slow isoform of the myosin-binding protein C.
10 ed PKA phosphorylation of the PKA substrate, myosin-binding protein C.
11 utations) were predicted to truncate cardiac myosin-binding protein C.
12 drugs and in cells expressing low levels of myosin-binding protein C.
13 t the stability of that motif is affected by myosin-binding protein C.
14 hin filaments in resting muscle, potentially myosin-binding protein C.
15 roteins, the commonest being MYBPC3 encoding myosin-binding protein C.
16 osphorylation of its targets, troponin I and myosin-binding protein C.
17 pendent of AMPK increased phosphorylation of myosin-binding protein C.
18 hs-cTn I, 0.71 [95% CI, 0.67-0.74]; cardiac myosin-binding protein C, 0.67 [95% CI, 0.61-0.73]; C-te
19 yses revealed 8 sequence variants in cardiac myosin binding protein-C (1 nonsense, 1 splice acceptor
20 orm identification, endogenous human cardiac myosin binding protein C (140 kDa) was identified for th
21 eased phosphorylation of Ser(273) of cardiac myosin binding protein-C, a cGMP-dependent protein kinas
23 he thin filament: phosphorylation of cardiac myosin binding protein-C accelerates cross bridge bindin
25 ies, PKA increased phosphorylation levels of myosin binding protein C and troponin I, and reduced Ca(
26 pectroscopy revealed hyperphosphorylation of myosin-binding protein C and phosphorylation of atypical
27 ments contain additional nonmyosin proteins, myosin-binding protein C and titin, the latter being the
28 ple myofibrillar substrates including titin, myosin-binding protein-C and cardiac troponin I (cTnI),
32 een the myosin heads, the cardiac isoform of myosin-binding protein-C, and titin will aid in understa
33 We confirm that the nine stripes ascribed to myosin binding protein-C are not related to the titin se
34 variants in MYBPC3, encoding cardiac MyBP-C (myosin binding protein C), are the most common cause of
35 r 170 normal chromosomes; 1 variant (cardiac myosin binding protein-C Arg326Gln) also occurred in a h
36 ryanodine receptor, troponin I, and cardiac myosin-binding protein C at PKA sites was increased in p
38 vs 115 [28-576] ng/L; P < .001), and cardiac myosin-binding protein C (at presentation: median [IQR],
39 ol myocytes with phosphorylation of cTnI and myosin binding protein C (C-protein) in myocytes with in
42 degradation of myosin heavy chain 6, cardiac myosin binding protein C, calcineurin (PPP3CB), and p-MT
43 st four N-terminal domains (NTDs) of cardiac myosin binding protein C (cMyBP-C) (e.g. C0, C1, M and C
44 A-mediated (PKA) phosphorylation of cardiac myosin binding protein C (cMyBP-C) accelerates the kinet
45 rylation of the cardiac myofilament proteins myosin binding protein C (cMyBP-C) and troponin I (cTnI)
53 traction, and its accessory protein, cardiac myosin binding protein C (cMyBP-C), are the two most com
57 We investigated the influence of cardiac myosin binding protein-C (cMyBP-C) and its constitutivel
59 RLC) by myosin light chain kinase (MLCK) and myosin binding protein-C (cMyBP-C) by protein kinase A (
72 opy, we examined the contribution of cardiac myosin binding protein-C (cMyBP-C) to thick-filament len
73 advances in the molecular biology of cardiac myosin binding protein-C (cMyBP-C), little is understood
75 the gene encoding cardiac C-protein [cardiac myosin binding protein-C (cMyBP-C)] are one of the princ
88 bait, identified cardiac troponin I (cTnI), myosin-binding protein C (cMyBP-C), and telethonin as PK
89 ariants in MYBPC3, the gene encoding cardiac myosin-binding protein C (cMyBP-C), are the leading caus
90 potential regulator of these motors, cardiac myosin-binding protein C (cMyBP-C), cause hypertrophic c
91 esolve the structure and dynamics of cardiac myosin-binding protein C (cMyBP-C), focusing on the N-te
92 arcomeric PKA targets, troponin I (cTnI) and myosin-binding protein C (cMyBP-C), lead to these effect
93 ion to myosin, the filaments contain cardiac myosin-binding protein C (cMyBP-C), which modulates cont
94 ardiac cells derived from both wild-type and myosin-binding protein C (cMyBP-C)-null mouse hearts.
96 ice with gene targeted deficiency of cardiac myosin-binding protein-C (cMyBP-C(-/-), n=6) or muscle L
103 n is the major regulatory subunit of cardiac myosin-binding protein-C (cMyBP-C) that modulates actin
104 ardiac muscle-specific myofibrillar protein, myosin-binding protein-C (cMyBP-C), is down-regulated.
106 tations in MYBPC3, the gene encoding cardiac myosin-binding protein C, (cMyBP-C) occur in ~20%-25% of
113 e mutation leads to reduced cMyBP-C (cardiac myosin binding protein-C) expression, supporting haploin
115 nd heterozygous variant in a candidate gene (myosin binding protein C, fast type [MYBPC2] and vacuola
118 hese results suggest that the 40-kDa cardiac myosin-binding protein C fragment, which is produced at
119 ded] N'-terminal domains C0 to C7 of cardiac myosin binding protein-C) fragment and an insoluble C'-t
122 f 50 years who had a mutation in the cardiac myosin-binding protein C gene (68 of 117 patients) had c
124 re events between the myosin heavy chain and myosin-binding protein C genotype-positive patients.
125 nt rates seen between myosin heavy chain and myosin-binding protein C genotype-positive patients.
126 osin light chain MLY2, myosin heavy chain 6, myosin-binding protein C), glucose metabolism proteins (
127 regulation of S-glutathionylation of cardiac myosin binding protein-C in FTY720-treated Tm-E180G mice
131 e suggesting that phosphorylation of cardiac myosin binding protein-C is a key regulator of the kinet
132 ression of mutations in the gene for cardiac myosin-binding protein C is often delayed until middle a
140 eta-adrenergic stimulation increases cardiac myosin binding protein C (MyBP-C) and troponin I phospho
141 quasi-helical order of the myosin heads and myosin binding protein C (MyBP-C) decreased in the sarco
142 (FHC), individuals bearing a mutant cardiac myosin binding protein C (MyBP-C) gene usually have a be
144 s contractile proteins, troponin-I (TnI) and myosin binding protein C (MyBP-C) in the heart and induc
150 f mice to reduce the level of troponin I and myosin binding protein C (MyBP-C) phosphorylation in the
151 c proteins, including the cardiac isoform of myosin binding protein C (MyBP-C), and multiple mutation
164 myofilaments proteins, troponin I (TnI) and myosin binding protein-C (MyBP-C), are phosphorylated fo
166 s mutant mice expressing a truncated form of myosin-binding protein C (MyBP-C(t/t)) develop severe di
167 r fasting, atrophying muscles show a loss of myosin-binding protein C (MyBP-C) and myosin light chain
168 ally phosphorylate the myofibrillar proteins myosin-binding protein C (MyBP-C) and the regulatory lig
169 ther changes in the phosphorylation state of myosin-binding protein C (MyBP-C) are a potential cause
177 unclear, although it has been proposed that myosin-binding protein C (MyBP-C) may stabilize the SRX
180 ther with a depression in phosphorylation of myosin-binding protein-C (MyBP-C) and troponin I (TnI).
186 ing a heterozygous truncation variant in the myosin-binding protein C ( MYBPC3) gene, which causes hy
187 thm missed a pathogenic 18 bp duplication in myosin binding protein C (MYBPC3) because of low coverag
190 the frequency and phenotype of mutations in myosin binding protein C (MYBPC3) in a large outpatient
192 tudies suggest that mutations in the cardiac myosin binding protein-C (MYBPC3) gene cause late-onset,
193 k filament components myosin heavy chain and myosin binding protein C (MYH7 and MYBPC3) together expl
194 -dependent phosphorylation of troponin I and myosin binding protein C on isoproterenol stimulation wa
195 domains of titin and the cardiac isoform of myosin-binding protein-C on the surface of the myosin fi
196 s in thick filament proteins such as cardiac myosin binding protein-C or titin, cause familial hypert
200 rmed reduced abundance of sarcomeric protein myosin binding protein C, potentially playing a role in
202 analysed, myosin heavy and light chains and myosin-binding protein C require Mef2 for normal express
203 nd MYBPC3, encoding B-myosin heavy chain and myosin binding protein C, respectively, are the two most
204 MYBPC3, encoding beta-myosin heavy chain and myosin-binding protein C, respectively, are the 2 most c
206 ant] N'-terminal domains C0 to C7 of cardiac myosin binding protein-C)-sc returned pCa(50) and k(tr)
207 2 domain of obscurin with a novel isoform of myosin binding protein-C slow (MyBP-C slow), correspondi
211 lament signaling pathways based on titin and myosin-binding protein-C that couple thin and thick fila
212 e confined to the filament domain containing myosin binding protein-C, the "C-zone." Myosin motors in
213 osin, binds with the C0-C2 region of cardiac myosin-binding protein-C to regulate cardiac muscle cont
216 phic cardiomyopathy is the recurrent MYBPC3 (myosin-binding protein-C) variant c.1504C>T, p.Arg502Trp
217 oponin, tropomyosin, and the C0C2 domains of myosin-binding protein C was also observed, influencing
219 of cardiac troponin inhibitor (cTnI) and the myosin-binding protein C was reduced by 26 and 35%, resp
221 ble 40-kDa fragment is produced from cardiac myosin-binding protein C when the heart is stressed usin
222 ansgenic (TG) mouse model expressing cardiac myosin binding protein-C with a non-phosphorylatable Ser
224 e suggested that the interactions of cardiac myosin-binding protein-C with its binding partners vary