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1 7 (beta-myosin heavy chain) and MYBPC3 (beta-myosin-binding protein C).
2 cardiac sarcomere or from the truncation of myosin binding protein C.
3 response to Ca(2+) with glutathionylation of myosin binding protein C.
4 ms of the thick-filament-associated protein, myosin binding protein-C.
5 drugs and in cells expressing low levels of myosin-binding protein C.
6 roteins, the commonest being MYBPC3 encoding myosin-binding protein C.
7 thers, filamin C and the slow isoform of the myosin-binding protein C.
8 osphorylation of its targets, troponin I and myosin-binding protein C.
9 ed PKA phosphorylation of the PKA substrate, myosin-binding protein C.
10 utations) were predicted to truncate cardiac myosin-binding protein C.
11 pendent of AMPK increased phosphorylation of myosin-binding protein C.
12 yses revealed 8 sequence variants in cardiac myosin binding protein-C (1 nonsense, 1 splice acceptor
14 he thin filament: phosphorylation of cardiac myosin binding protein-C accelerates cross bridge bindin
16 ies, PKA increased phosphorylation levels of myosin binding protein C and troponin I, and reduced Ca(
17 pectroscopy revealed hyperphosphorylation of myosin-binding protein C and phosphorylation of atypical
18 ple myofibrillar substrates including titin, myosin-binding protein-C and cardiac troponin I (cTnI),
22 een the myosin heads, the cardiac isoform of myosin-binding protein-C, and titin will aid in understa
23 r 170 normal chromosomes; 1 variant (cardiac myosin binding protein-C Arg326Gln) also occurred in a h
25 ol myocytes with phosphorylation of cTnI and myosin binding protein C (C-protein) in myocytes with in
28 degradation of myosin heavy chain 6, cardiac myosin binding protein C, calcineurin (PPP3CB), and p-MT
29 A-mediated (PKA) phosphorylation of cardiac myosin binding protein C (cMyBP-C) accelerates the kinet
30 rylation of the cardiac myofilament proteins myosin binding protein C (cMyBP-C) and troponin I (cTnI)
36 traction, and its accessory protein, cardiac myosin binding protein C (cMyBP-C), are the two most com
39 We investigated the influence of cardiac myosin binding protein-C (cMyBP-C) and its constitutivel
41 RLC) by myosin light chain kinase (MLCK) and myosin binding protein-C (cMyBP-C) by protein kinase A (
50 opy, we examined the contribution of cardiac myosin binding protein-C (cMyBP-C) to thick-filament len
51 advances in the molecular biology of cardiac myosin binding protein-C (cMyBP-C), little is understood
53 the gene encoding cardiac C-protein [cardiac myosin binding protein-C (cMyBP-C)] are one of the princ
61 bait, identified cardiac troponin I (cTnI), myosin-binding protein C (cMyBP-C), and telethonin as PK
62 potential regulator of these motors, cardiac myosin-binding protein C (cMyBP-C), cause hypertrophic c
63 esolve the structure and dynamics of cardiac myosin-binding protein C (cMyBP-C), focusing on the N-te
64 ardiac cells derived from both wild-type and myosin-binding protein C (cMyBP-C)-null mouse hearts.
65 ice with gene targeted deficiency of cardiac myosin-binding protein-C (cMyBP-C(-/-), n=6) or muscle L
71 n is the major regulatory subunit of cardiac myosin-binding protein-C (cMyBP-C) that modulates actin
72 ardiac muscle-specific myofibrillar protein, myosin-binding protein-C (cMyBP-C), is down-regulated.
79 nd heterozygous variant in a candidate gene (myosin binding protein C, fast type [MYBPC2] and vacuola
81 hese results suggest that the 40-kDa cardiac myosin-binding protein C fragment, which is produced at
84 f 50 years who had a mutation in the cardiac myosin-binding protein C gene (68 of 117 patients) had c
86 re events between the myosin heavy chain and myosin-binding protein C genotype-positive patients.
87 nt rates seen between myosin heavy chain and myosin-binding protein C genotype-positive patients.
88 osin light chain MLY2, myosin heavy chain 6, myosin-binding protein C), glucose metabolism proteins (
92 e suggesting that phosphorylation of cardiac myosin binding protein-C is a key regulator of the kinet
93 ression of mutations in the gene for cardiac myosin-binding protein C is often delayed until middle a
100 eta-adrenergic stimulation increases cardiac myosin binding protein C (MyBP-C) and troponin I phospho
101 quasi-helical order of the myosin heads and myosin binding protein C (MyBP-C) decreased in the sarco
102 (FHC), individuals bearing a mutant cardiac myosin binding protein C (MyBP-C) gene usually have a be
104 s contractile proteins, troponin-I (TnI) and myosin binding protein C (MyBP-C) in the heart and induc
110 f mice to reduce the level of troponin I and myosin binding protein C (MyBP-C) phosphorylation in the
111 c proteins, including the cardiac isoform of myosin binding protein C (MyBP-C), and multiple mutation
122 myofilaments proteins, troponin I (TnI) and myosin binding protein-C (MyBP-C), are phosphorylated fo
124 s mutant mice expressing a truncated form of myosin-binding protein C (MyBP-C(t/t)) develop severe di
125 r fasting, atrophying muscles show a loss of myosin-binding protein C (MyBP-C) and myosin light chain
126 ally phosphorylate the myofibrillar proteins myosin-binding protein C (MyBP-C) and the regulatory lig
127 ther changes in the phosphorylation state of myosin-binding protein C (MyBP-C) are a potential cause
134 ther with a depression in phosphorylation of myosin-binding protein-C (MyBP-C) and troponin I (TnI).
140 thm missed a pathogenic 18 bp duplication in myosin binding protein C (MYBPC3) because of low coverag
143 the frequency and phenotype of mutations in myosin binding protein C (MYBPC3) in a large outpatient
145 tudies suggest that mutations in the cardiac myosin binding protein-C (MYBPC3) gene cause late-onset,
146 k filament components myosin heavy chain and myosin binding protein C (MYH7 and MYBPC3) together expl
147 -dependent phosphorylation of troponin I and myosin binding protein C on isoproterenol stimulation wa
148 domains of titin and the cardiac isoform of myosin-binding protein-C on the surface of the myosin fi
149 s in thick filament proteins such as cardiac myosin binding protein-C or titin, cause familial hypert
154 analysed, myosin heavy and light chains and myosin-binding protein C require Mef2 for normal express
155 MYBPC3, encoding beta-myosin heavy chain and myosin-binding protein C, respectively, are the 2 most c
156 2 domain of obscurin with a novel isoform of myosin binding protein-C slow (MyBP-C slow), correspondi
161 phic cardiomyopathy is the recurrent MYBPC3 (myosin-binding protein-C) variant c.1504C>T, p.Arg502Trp
163 of cardiac troponin inhibitor (cTnI) and the myosin-binding protein C was reduced by 26 and 35%, resp
165 ble 40-kDa fragment is produced from cardiac myosin-binding protein C when the heart is stressed usin
166 ansgenic (TG) mouse model expressing cardiac myosin binding protein-C with a non-phosphorylatable Ser
168 e suggested that the interactions of cardiac myosin-binding protein-C with its binding partners vary
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