(1987): Myosin binding to actin: Structural analysis using myosin fragments. J . Mol. Biol. 196:955-960.Castellani, L., Elliot, B.W., Winkelmann, D.A., Vibert, P., Cohen, C., 1987. Myosin binding to actin. Structural analysis using myosin fragments. J. Mol. Biol. 196, 955-960...
Myosin binding to actin 喜欢 0 阅读量: 30 作者: Castellani, Loriana,Elliott, Bruce W.,Winkelmann, Donald A.,Vibert, Peter,Cohen, Carolyn 摘要: The actin-binding property of the myosin head 20 K (K = 103 Mr) fragment has been examined by a structural assay. A new fragment is produced...
1b) to the experimental chamber, using TIRF microscopy, we observed anillin-GFP binding to actin filaments (Fig. 1c–e). At an anillin-GFP concentration of 0.12 nM, actin filaments were decorated by anillin-GFP molecules (Fig. 1a, f), which in accordance with previously published data...
The 2K peptide inhibited the acto-S1 ATPase activity without inhibiting the binding of S1 to actin in the presence of ATP. On the other hand, the dansylated 2K peptide (DNS-2K peptide) inhibited not only the acto-S1 ATPase activity but also the binding of S1 to actin in the presence ...
The Myosin-binding Protein C Motif Binds to F-actin in a Phosphorylation-sensitive Manner Cardiac (cMyBP-C) is a regulatory protein expressed in cardiac that is known to interact with , , and . cMyBP-C modulates interactions in a -dependent way,... JF Shaffer,RW Kensler,SP Harris - 《...
Some actin binding or actin regulated proteins have been demonstrated to regulate dynamic changes of the actin-containing structures. Myosin, actin-dependent molecular motor, plays an important role during spermatogenesis, such as involving in acrosome biogenesis, vesicle transport, gene transcription and...
that the binding of the skeletal muscle myosin motor domain (S1) to actin filament always saturates at one S1 bound to one actin monomer (or two S1 per actin dimer), whether S1 was added slowly (17 min between additions) or rapidly (10 s between additions) to an excess of F-actin. ...
Much interest has centered on two surface loops in the motor domain to explain the differences in enzymatic and mechanical properties of myosin isoforms. We showed that two invariant lysines at the C-terminal end of loop 2, which is part of the actin-binding interface, are required to obtain...
The overall evidence presented demonstrates that in situ HMM binding can be used as an effective ultrastructural cytochemical probe for determining the distribution and possible functions of actin like microfilaments in nonmuscle cells. Since actin like proteins appear to represent a large proportion of...
Cardiac myosin binding protein-C (cMyBP-C) is a thick filament protein that interacts with titin, myosin and actin to regulate sarcomeric structure and regulation of acto-myosin cross-bridge cycling (Fig. 1) [51,52]. Mutations in cMyBP-C gene MYBPC3 are the most abundant HCM gene...