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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
22                                      Cardiac myosin-binding protein C, a cardiac-specific myofilament
23 he thin filament: phosphorylation of cardiac myosin binding protein-C accelerates cross bridge bindin
24            Mutations in the gene for cardiac myosin-binding protein C account for approximately 15 pe
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),
29 enes, most commonly beta myosin heavy chain, myosin binding protein C, and cardiac troponin T.
30 iac myocyte proteins (alpha-actinin, cardiac myosin-binding protein C, and cardiac troponin I).
31  phosphorylation of cTnI, cTnT, tropomyosin, myosin-binding protein C, and desmin.
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
37 at Ser16, phospholemman at Ser68 and cardiac myosin-binding protein C at Ser282, was unaltered.
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
40      Several other proteins such as synemin, myosin binding protein C (C-protein), glycogen debranchi
41 n of troponin T (TnT), troponin I (TnI), and myosin-binding protein C (C-protein).
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)
46       In the cardiac sarcomere, both cardiac myosin binding protein C (cMyBP-C) and troponin-I (cTnI)
47                                      Cardiac myosin binding protein C (cMyBP-C) appears to modulate t
48                         Mutations in cardiac myosin binding protein C (cMyBP-C) are a leading cause o
49                                      Cardiac myosin binding protein C (cMyBP-C) has a key regulatory
50                                      Cardiac myosin binding protein C (cMyBP-C) has three phosphoryla
51                                      Cardiac myosin binding protein C (cMyBP-C) modulates cardiac con
52                        Protein expression of myosin binding protein C (cMyBP-C) was significantly low
53 traction, and its accessory protein, cardiac myosin binding protein C (cMyBP-C), are the two most com
54                                      Cardiac myosin binding protein C (cMyBP-C), bound to the sarcome
55                 The cardiac isoform [cardiac myosin binding protein C (cMyBP-C)] is essential for nor
56                   Phosphorylation of cardiac myosin binding protein-C (cMyBP-C) accelerates cardiac c
57     We investigated the influence of cardiac myosin binding protein-C (cMyBP-C) and its constitutivel
58  myofilaments PKA targets troponin I (cTnI), myosin binding protein-C (cMyBP-C) and titin.
59 RLC) by myosin light chain kinase (MLCK) and myosin binding protein-C (cMyBP-C) by protein kinase A (
60                Although mutations in cardiac myosin binding protein-C (cMyBP-C) cause heart disease,
61          Although phosphorylation of cardiac myosin binding protein-C (cMyBP-C) has been recognized a
62                   Phosphorylation of cardiac myosin binding protein-C (cMyBP-C) is a determinant of c
63                                      Cardiac myosin binding protein-C (cMyBP-C) is a member of the im
64                                              Myosin binding protein-C (cMyBP-C) is a thick filament a
65                                      Cardiac myosin binding protein-C (cMyBP-C) is a thick filament a
66                                      Cardiac myosin binding protein-C (cMyBP-C) is a thick filament-a
67                                      Cardiac myosin binding protein-C (cMyBP-C) is a thick-filament p
68                                      Cardiac myosin binding protein-C (cMyBP-C) is an important regul
69            We examined the effect of cardiac myosin binding protein-C (cMyBP-C) on contractile effici
70                          The role of cardiac myosin binding protein-C (cMyBP-C) phosphorylation in ca
71                                      Cardiac myosin binding protein-C (cMyBP-C) phosphorylation modul
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
74 ns, most often MYBPC3, which encodes cardiac myosin binding protein-C (cMyBP-C).
75 the gene encoding cardiac C-protein [cardiac myosin binding protein-C (cMyBP-C)] are one of the princ
76 23/24) of cardiac troponin I (cTnI), cardiac myosin-binding protein C (cMyBP-C) and titin.
77                         Mutations in cardiac myosin-binding protein C (cMyBP-C) are a leading cause o
78                                      Cardiac myosin-binding protein C (cMyBP-C) interacts with actin
79                                      Cardiac myosin-binding protein C (cMyBP-C) is a component of the
80                       The cardiac isoform of myosin-binding protein C (cMyBP-C) is a key regulatory p
81                                      Cardiac myosin-binding protein C (cMyBP-C) is a regulatory prote
82                                      Cardiac myosin-binding protein C (cMyBP-C) is a sarcomeric prote
83                                      Cardiac myosin-binding protein C (cMyBP-C) is a thick filament-a
84                                      Cardiac myosin-binding protein C (cMyBP-C) is a thick-filament-a
85            The N-terminal modules of cardiac myosin-binding protein C (cMyBP-C) play a regulatory rol
86                                      Cardiac myosin-binding protein C (cMyBP-C) plays a modulatory ro
87                                      Cardiac myosin-binding protein C (cMyBP-C) regulates actin-myosi
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.
95 +) levels, active cross-bridges, and cardiac myosin-binding protein C (cMyBP-C).
96 ice with gene targeted deficiency of cardiac myosin-binding protein-C (cMyBP-C(-/-), n=6) or muscle L
97                   Phosphorylation of cardiac myosin-binding protein-C (cMyBP-C) by protein kinase A a
98                                      Cardiac myosin-binding protein-C (cMyBP-C) is a thick filament p
99                                      Cardiac myosin-binding protein-C (cMyBP-C) is a thick filament-a
100                                      Cardiac myosin-binding protein-C (cMyBP-C) is a thick-filament-a
101                                      Cardiac myosin-binding protein-C (cMyBP-C) is highly phosphoryla
102 P sensitivity highly correlated with cardiac myosin-binding protein-C (cMyBP-C) protein level.
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.
105 omology with the carboxy-terminus of cardiac myosin-binding protein-C (cMyBP-C).
106 tations in MYBPC3, the gene encoding cardiac myosin-binding protein C, (cMyBP-C) occur in ~20%-25% of
107              Decreased expression of cardiac myosin binding protein C (cMyBPC) as a result of genetic
108              Decreased expression of cardiac myosin binding protein C (cMyBPC) in the heart has been
109                                      Cardiac myosin binding protein C (cMyBPC) phosphorylation is ess
110                                      Cardiac myosin-binding protein C (cMyC) is a cardiac-restricted
111                                      Cardiac myosin-binding protein C (cMyC) is a cardiac-specific sa
112                           Homozygous cardiac myosin binding protein C-deficient (Mybpc(t/t)) mice dev
113 e mutation leads to reduced cMyBP-C (cardiac myosin binding protein-C) expression, supporting haploin
114             This Ag is a novel member of the myosin binding protein-C family, which we call masticato
115 nd heterozygous variant in a candidate gene (myosin binding protein C, fast type [MYBPC2] and vacuola
116                                Fast skeletal myosin-binding protein-C (fMyBP-C) is one of three MyBP-
117                                      MYBPC3 (Myosin-binding protein C) founder mutations account for
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
120                                Extraction of myosin binding protein-C from skinned muscle normalized
121                     Mutations in the cardiac myosin binding protein-C gene (cMyBP-C) are among the mo
122 f 50 years who had a mutation in the cardiac myosin-binding protein C gene (68 of 117 patients) had c
123 heritable nature of mutations in the cardiac myosin-binding protein C gene.
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
128 rs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.
129                   Ser/Thr phosphorylation of myosin-binding protein C increased primarily by PKCzeta
130                                              Myosin binding protein C is a thick filament protein of
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
133                             cMyBP-C (cardiac myosin-binding protein-C) is a critical regulator of hea
134            MYBPC3, encoding cMyBP-C (cardiac myosin-binding protein C), is the most frequently mutate
135                                          The myosin-binding protein C isoform 3 (MYBPC3) variant Arg5
136                           Among these is the myosin-binding protein C (MBP-C).
137  protein-C family, which we call masticatory myosin binding protein-C (mMyBP-C).
138           In this G+LVH- population, cardiac myosin-binding protein C mutation carriers had twice the
139  familial hypertrophic cardiomyopathy mutant myosin binding protein C (MyBP-C(MUT)) expression.
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
143         The large multidomain muscle protein myosin binding protein C (MyBP-C) has been implicated fo
144 s contractile proteins, troponin-I (TnI) and myosin binding protein C (MyBP-C) in the heart and induc
145                                              Myosin binding protein C (MyBP-C) is a component of the
146                                              Myosin binding protein C (MyBP-C) is a thick filament pr
147                                              Myosin binding protein C (MyBP-C) is an integral part of
148                                              Myosin binding protein C (MyBP-C) is expressed in striat
149                                              Myosin binding protein C (MyBP-C) is one of a group of m
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
152 , titin, and the cardiac modulatory protein, myosin binding protein C (MyBP-C).
153            We have determined the effects of myosin binding protein-C (MyBP-C) and its domains on the
154       We hypothesize that phosphorylation of myosin binding protein-C (MyBP-C) and troponin I (TnI) a
155                                              Myosin binding protein-C (MyBP-C) exists in three major
156                                              Myosin binding protein-C (MyBP-C) is a key regulatory pr
157                                              Myosin binding protein-C (MyBP-C) is a multidomain prote
158                                              Myosin binding protein-C (MyBP-C) is a poorly understood
159                                              Myosin binding protein-C (MyBP-C) is a thick filament-as
160                                              Myosin binding protein-C (MyBP-C) is a thick-filament pr
161                                              Myosin binding protein-C (MyBP-C) is localized to the th
162          These structural changes also drive Myosin Binding Protein-C (MyBP-C) to promote first motor
163           Among these, mutations that affect myosin binding protein-C (MyBP-C), an abundant component
164  myofilaments proteins, troponin I (TnI) and myosin binding protein-C (MyBP-C), are phosphorylated fo
165 to phosphorylation of troponin I (TnI) or of myosin binding protein-C (MyBP-C).
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
170                                              Myosin-binding protein C (MyBP-C) is a long and flexible
171                                              Myosin-binding protein C (MyBP-C) is a multidomain prote
172                              Skeletal muscle myosin-binding protein C (MyBP-C) is a myosin thick fila
173                                              Myosin-binding protein C (MyBP-C) is a thick filament pr
174                                              Myosin-binding protein C (MyBP-C) is a thick filament pr
175                                              Myosin-binding protein C (MyBP-C) is an accessory protei
176                                              Myosin-binding protein C (MyBP-C) is an approximately 13
177  unclear, although it has been proposed that myosin-binding protein C (MyBP-C) may stabilize the SRX
178                     After phosphorylation of myosin-binding protein C (MyBP-C) with protein kinase A
179 imensional organization of myosin, titin and myosin-binding protein C (MyBP-C).
180 ther with a depression in phosphorylation of myosin-binding protein-C (MyBP-C) and troponin I (TnI).
181             To elucidate the role of cardiac myosin-binding protein-C (MyBP-C) in myocardial structur
182                                              Myosin-binding protein-C (MyBP-C) is a thick filament-as
183                                              Myosin binding protein C (MyBPC) is a multidomain protei
184 rotein was identified as the 140-kDa cardiac myosin binding protein C (MyBPC).
185                         Mutations in cardiac myosin-binding protein C (MyBPC) gene have been associat
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
188 eral sarcomeric genes, including the cardiac myosin binding protein C (MYBPC3) gene.
189 d in several sarcomeric genes, including the myosin binding protein C (MYBPC3) gene.
190  the frequency and phenotype of mutations in myosin binding protein C (MYBPC3) in a large outpatient
191 D cardiomyopathy genes, lamin A/C (LMNA) and myosin binding protein C (MYBPC3).
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
197                                          The myosin binding protein C, or C protein, has 4 sites that
198                                      Cardiac myosin binding protein-C phosphorylation plays an import
199 K gene ablation did not affect troponin-I or myosin-binding protein-C phosphorylation in vivo.
200 rmed reduced abundance of sarcomeric protein myosin binding protein C, potentially playing a role in
201 e myosin-binding motif (m-domain) of cardiac myosin-binding protein-C remains unclear.
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
205 treatment, which coincided with the level of myosin binding protein-C-S glutathionylation.
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
208                                              Myosin Binding Protein-C slow (sMyBP-C) is expressed in
209                                              Myosin Binding Protein-C slow (sMyBP-C), encoded by MYBP
210                          MYBPC1 encodes slow myosin binding protein-C (sMyBP-C), a modular sarcomeric
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
214                 Rather, mutations in cardiac myosin binding protein-C, troponin I, and alpha-cardiac
215                                              Myosin-binding protein C, troponin T, tropomyosin and my
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
218 mbers with mutations in the gene for cardiac myosin-binding protein C was assessed.
219 of cardiac troponin inhibitor (cTnI) and the myosin-binding protein C was reduced by 26 and 35%, resp
220               DNA sequences encoding cardiac myosin-binding protein C were determined in unrelated pa
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
223 nd disrupt the interaction of native cardiac myosin-binding protein C with the thin filament.
224 e suggested that the interactions of cardiac myosin-binding protein-C with its binding partners vary

 
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