Recent studies have shown that in addition to Ca, the first four N-terminal domains (NTDs) of cardiac myosin binding protein C (cMyBP-C) (e.g. C0, C1, M and C2), are potent modulators of the TF activity, but the mechanism of their collective action is poorly understood. Previously, ...
We have previously shown that binding of cMyBP-C N-terminal fragments (C0C2, C0C3) to thin filaments, in the absence of Ca2+, shifts tropomyosin to the “closed” position, which favors weak cross-bridge formation13. We hypothesized that binding of the skeletal MyBP-C isoforms to thin fi...
The unique myosin binding protein-c "motif" near the N-terminus of myosin binding protein-C (MyBP-C) binds myosin S2. Previous studies demonstrated that recombinant proteins containing the motif and flanking regions (e.g., C1C2) affect thin filament movement in motility assays using heavy mero...
Nitrovasodilators relax vascular smooth-muscle cells in part by modulating the interaction of the C-terminal coiled-coil domain (CC) and/or the leucine zipper (LZ) domain of the myosin light-chain phosphatase component, myosin-binding subunit (MBS), with the N-terminal LZ domain of protein ...
Furthermore, in order to verify that it is the C1-C2 region of cMyBPC that interacts with MMGL isoform 4, specifically, and does so in the absence of the GAL4 regions of the Y2H bait protein, we used in vitro co-immunoprecipitation assays. We also used these assays to assess whether ...
The protein contains a putative C2 domain at its N terminus (aa 1–100), suggesting electrostatic interactions with acidic phospholipids37. To directly test interaction of this region with lipids in vitro, purified GST-tagged ForA-C2 was assessed by co-flotation assays with liposomes containing ...
Myosin-Binding Protein C (MyBP-C) in Cardiac Muscle and Contractility Both the MyBP-C motif between C1 and C2 and the C5 module are important regions for implementing the effect of MyBP-C on myosin and on contractility but in... S Winegrad - 《Oxygen Transport to Tissue XXXIII》 被引...
interaction of myosin with regulated actin filaments containing tropomyosin and troponin, the roles of regulatory light chain phosphorylation on the functions of the system, and the possible roles of myosin binding protein-C and titin, important regulatory components of both cardiac and skeletal muscles...
MYO5B is an essential protein for the recycling of ABCB11 and ABCC2, the canalicular transporter of bilirubin, from Rab8 and Rab11 positive compartments. When MYO5B is mutated or truncated in vitro, ABCC2 displays an intracellular localization in Rab8 and Rab11 positive compartments. Therefore...
Note: If you have problems viewing the PDF, please make sure you have the latest version of Adobe Acrobat. Back to full textHome Search Services Contact us © 2004-2024 FreePatentsOnline.com. All rights reserved. Privacy Policy & Terms of Use....