Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain.
about
A common MYBPC3 (cardiac myosin binding protein C) variant associated with cardiomyopathies in South AsiaMyosin binding protein C: implications for signal-transductionThe ubiquitin-proteasome system and cardiovascular diseaseStructural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAINThe myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive mannerA critical function for Ser-282 in cardiac Myosin binding protein-C phosphorylation and cardiac functionPathogenic properties of the N-terminal region of cardiac myosin binding protein-C in vitroGSK3β phosphorylates newly identified site in the proline-alanine-rich region of cardiac myosin-binding protein C and alters cross-bridge cycling kinetics in human: short communicationRadial displacement of myosin cross-bridges in mouse myocardium due to ablation of myosin binding protein-CUnderstanding the organisation and role of myosin binding protein C in normal striated muscle by comparison with MyBP-C knockout cardiac muscleAblation of myosin-binding protein-C accelerates force development in mouse myocardiumDoxorubicin-induced carbonylation and degradation of cardiac myosin binding protein C promote cardiotoxicityMyocardial infarction-induced N-terminal fragment of cardiac myosin-binding protein C (cMyBP-C) impairs myofilament function in human myocardiumIn the thick of it: HCM-causing mutations in myosin binding proteins of the thick filamentCardiac myosin-binding protein-C phosphorylation and cardiac functionDetermination of the critical residues responsible for cardiac myosin binding protein C's interactionsConvergent evolution of marine mammals is associated with distinct substitutions in common genesA cardiac myosin binding protein C mutation in the Maine Coon cat with familial hypertrophic cardiomyopathy.Three-dimensional structure of vertebrate cardiac muscle myosin filaments.Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle.Loss of actomyosin regulation in distal arthrogryposis myopathy due to mutant myosin binding protein-C slow.Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Functional differences between the N-terminal domains of mouse and human myosin binding protein-C.Association of 25 bp deletion in MYBPC3 gene with left ventricle dysfunction in coronary artery disease patients.Unique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain.Myosin binding protein C interaction with actin: characterization and mapping of the binding site.Head-head interactions of resting myosin crossbridges in intact frog skeletal muscles, revealed by synchrotron x-ray fiber diffractionLength-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation.Signaling and myosin-binding protein C.Muscle giants: molecular scaffolds in sarcomerogenesis.Structural changes of cross-bridges on transition from isometric to shortening state in frog skeletal muscle.Myosin binding protein-C: a regulator of actomyosin interaction in striated muscleMyosin binding protein C: structural abnormalities in familial hypertrophic cardiomyopathy.Modulation of striated muscle contraction by binding of myosin binding protein C to actin.Axial distribution of myosin binding protein-C is unaffected by mutations in human cardiac and skeletal muscleCardiac myosin binding protein-C: redefining its structure and function.Multiple forms of cardiac myosin-binding protein C exist and can regulate thick filament stabilityCardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Atomic model of the human cardiac muscle myosin filament.Phosphorylation modulates the mechanical stability of the cardiac myosin-binding protein C motif.
P2860
Q24645034-3F151ACB-D767-4B70-9DD5-2478375C16BFQ26865973-6F6440E1-A18A-4420-8672-045DA9623392Q27021582-051FBC64-644D-40E1-B99D-1E926FF4E679Q27676683-306F1CAF-5BDF-4B7E-A81D-87C1F7678B6BQ28237568-C06A86B4-DF9F-4A79-A784-7EA136FBAAE5Q28238191-40221225-908D-409E-BB93-656BB2973439Q28265173-7A712538-228B-4F9B-B3F5-1D21EBC79EAEQ28282353-D69B931F-1500-4A0B-80D5-2706FEDA4538Q28285084-EC4E9CAB-2EB8-40BC-8472-4D900AA12816Q28295237-F4E5C9A6-BD81-4C72-A8CA-04FDD38A3655Q28300076-5C9CC176-29E4-42B3-B0F0-FDE52E0FCD63Q28306329-A214C5C6-CA8D-4929-84A1-F5F2B7D8FB27Q28307520-021470AA-D163-48AE-9070-9125B2575C4CQ28307598-75124205-74E5-433D-A406-A0FFAD49C406Q28584863-8F85E047-91EF-4F42-8ADC-0AFC7C98AC89Q28590116-1FBF39EF-DE3F-42E0-AC22-72C579A101F4Q28607668-E1880D51-7BDF-4A71-8AAC-B29F72B88865Q30351668-7C4F3290-2114-4106-950A-3BEDABD7C319Q30481472-F3C6BC01-4B9C-44E5-A90C-17AC16407439Q30502467-76626652-3720-4417-BAF3-82FC1A9AEC3DQ30541578-A6270B26-6C58-4E21-B42D-826A40D6E0C4Q33608126-D9218C55-C79A-4412-A78B-71564F6DE218Q33773355-47E2D1DF-C64B-478D-BF98-04AF8403CA02Q34018918-C4D95DE2-B084-4F2E-A807-FAB34E5ED6C2Q34042167-B63D0C59-87F2-40F4-9613-E382859685CAQ34503162-407D4AED-973D-4FCA-81BD-BE654A9AE954Q34533860-891AE768-6D74-4F30-B7B0-C129DFFCCF57Q34608313-0198F808-34FA-4472-9E1A-45DE658138D1Q34696154-9258E13C-BA49-40DE-AFCF-6EEA1AB8FE1BQ34793699-36208C31-992F-4C4F-BF7C-B62927A448A7Q35128927-046A3BC6-A4D7-48CA-AA24-3850E2F4AABDQ35389621-D49AB0D1-874E-4D58-8E35-2F999CAFD380Q35759293-21A246E7-9394-470A-9DC6-AD275EDC940AQ35914096-C2D368AB-EFC5-4936-BD26-952D22801BEBQ35957619-DF831272-608D-424C-B69A-E6064A31E217Q36030150-35B6DB3A-A181-4E4B-93A0-FD751A46DF7FQ36299735-3E6A6075-FC68-45DF-8CEB-AA71570D1890Q36483549-967EC5B2-03DD-4867-A206-A836992A3F6DQ36512285-3DE13A73-A9C7-4762-9DE7-1BDA03CC6458Q36554361-ABCB9661-E239-4B5A-9E36-06CE5D6BE310
P2860
Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain.
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Structural evidence for the in ...... possible actin-binding domain.
@ast
Structural evidence for the in ...... possible actin-binding domain.
@en
Structural evidence for the interaction of C-protein
@nl
type
label
Structural evidence for the in ...... possible actin-binding domain.
@ast
Structural evidence for the in ...... possible actin-binding domain.
@en
Structural evidence for the interaction of C-protein
@nl
prefLabel
Structural evidence for the in ...... possible actin-binding domain.
@ast
Structural evidence for the in ...... possible actin-binding domain.
@en
Structural evidence for the interaction of C-protein
@nl
P50
P1476
Structural evidence for the in ...... possible actin-binding domain
@en
P2093
Carlo Knupp
P304
P356
10.1016/S0022-2836(03)00781-2
P407
P577
2003-08-01T00:00:00Z