Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.
about
Novel control of cardiac myofilament response to calcium by S-glutathionylation at specific sites of myosin binding protein CStructural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAINPhosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectivesMyocardial infarction-induced N-terminal fragment of cardiac myosin-binding protein C (cMyBP-C) impairs myofilament function in human myocardiumDetermination of the critical residues responsible for cardiac myosin binding protein C's interactionsThe N-terminal domains of myosin binding protein C can bind polymorphically to F-actin.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.Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure.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.Germinal center-specific protein human germinal center associated lymphoma directly interacts with both myosin and actin and increases the binding of myosin to actinThe myosin mesa and a possible unifying hypothesis for the molecular basis of human hypertrophic cardiomyopathyMyosin binding protein-C: a regulator of actomyosin interaction in striated muscleModulation of striated muscle contraction by binding of myosin binding protein C to actin.Cardiac myosin binding protein-C: redefining its structure and function.Ablation of cardiac myosin-binding protein-C accelerates contractile kinetics in engineered cardiac tissue.Phosphorylation modulates the mechanical stability of the cardiac myosin-binding protein C motif.Cross-species mechanical fingerprinting of cardiac myosin binding protein-CA gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin.E258K HCM-causing mutation in cardiac MyBP-C reduces contractile force and accelerates twitch kinetics by disrupting the cMyBP-C and myosin S2 interaction.Myosin-binding protein C displaces tropomyosin to activate cardiac thin filaments and governs their speed by an independent mechanism.Molecular modulation of actomyosin function by cardiac myosin-binding protein C.In vivo definition of cardiac myosin-binding protein C's critical interactions with myosinPhosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filamentsInvited review: probing the structures of muscle regulatory proteins using small-angle solution scattering.Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?Cardiac myosin binding protein-C: a structurally dynamic regulator of myocardial contractility.The genetic landscape of cardiomyopathy and its role in heart failure.The cMyBP-C HCM variant L348P enhances thin filament activation through an increased shift in tropomyosin position.Cardiac myosin binding protein C and its phosphorylation regulate multiple steps in the cross-bridge cycle of muscle contraction.Electron microscopy and 3D reconstruction of F-actin decorated with cardiac myosin-binding protein C (cMyBP-C).Modulation of thin filament activation of myosin ATP hydrolysis by N-terminal domains of cardiac myosin binding protein-C.Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog.N-terminal phosphorylation of cardiac troponin-I reduces length-dependent calcium sensitivity of contraction in cardiac muscle.Sarcomeric protein modification during adrenergic stress enhances cross-bridge kinetics and cardiac output.Association of Cardiomyopathy With MYBPC3 D389V and MYBPC3Δ25bpIntronic Deletion in South Asian Descendants.
P2860
Q21129240-AF00574A-D2AE-4FB9-9229-477B9FD0063FQ27676683-EBA1E545-A6B3-4484-92E7-E185DD238D70Q28078785-445BE9DE-81B6-4F1A-96F7-D84A5EBDC6C0Q28307520-5E0516F6-A6B5-4988-9D35-DD6997763367Q28590116-9B5F4FCE-E328-4BED-B4C7-1868FA17E3ADQ30424900-F2BADED4-6B59-4BAD-BAE7-7D9CFC411E0BQ30502467-9DA241CD-70A9-4C91-B1F4-75D3BBAA5EEFQ30541578-BAC14E36-3770-4817-97E8-794649BA173DQ33561540-50AC6E00-3C5D-49E8-8707-777ACB4A3F7FQ34042167-D48A2B6A-2A2E-442E-A45B-D30F211D725FQ34990222-7EC8BBEF-6F74-444B-91A7-0A4CB7870029Q35147071-84CC4533-8042-44DE-BEF9-402DBC8CDF41Q35389621-D4759A73-A68E-447E-AD9C-A4D99469BC64Q35914096-858CE06C-B6BF-4558-9C15-4C99962E342EQ36030150-729C27ED-117F-4B0A-A40A-96257F6F120BQ36507217-2DA66265-F73E-47CA-B2C2-6130B9EF1C4EQ36554361-E4C9FE03-1BE5-4AB9-B77E-9B8A59AF39E9Q36903669-A1B64154-308E-4D46-A0E5-B7036935A17FQ37048313-EE900ED0-BA87-4D64-B42E-112D18A4F172Q37121972-DE012F92-AFDC-4CE7-8A0E-5A2A5229FA96Q37587694-B94F3183-2685-48B3-86A3-AB59BD8CA987Q37599166-67701327-B8CD-45A7-B940-7C31F2225E1AQ37641092-C23E89CC-9027-4A5C-82A6-BE1652F5F342Q37682309-C61EA52D-237C-479B-82CA-F741C3D82B17Q37858478-CB8D46D9-DE7D-4103-BF9B-E79776720EDEQ38004917-EC07DA4A-18BF-4A8B-9728-B11EAFD865A5Q38182406-3E57FFA2-4D36-4F8A-9D25-BB0BB2F26A1AQ38343935-847F783C-9300-4B91-B06B-F186A816677EQ38603190-03DC887E-CE94-49CB-8726-C01E6DD63A9DQ41080319-142A47D5-762C-4EE4-81EE-F40E757E300EQ41836341-C64A4129-E63D-4D5D-8465-1EC130C56689Q42965023-5E7B9554-1DF1-4DC9-AD98-3DF9D6D37A5FQ44024035-70BCAB4C-C803-4F6A-BDC6-8EAFBAA7FBB9Q44281385-749ED4BC-12D8-4F5E-BA8B-7C784C7573DCQ51291160-BE9C8A97-3836-4036-8601-F0C77509EB43Q52594002-28549C52-B54A-4E98-AD82-BD4A7CEE3A93
P2860
Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.
@en
type
label
Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.
@en
prefLabel
Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.
@en
P2093
P2860
P1476
Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.
@en
P2093
Justin F Shaffer
Robert W Kensler
Samantha P Harris
P2860
P356
10.1016/J.JSB.2010.12.003
P577
2010-12-14T00:00:00Z