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In the resting state, two proteins, troponin and tropomyosin, bind to actin molecules and inhibit interaction between actin and myosin, thereby blocking muscle contraction.
A recombinant lasp-1 fragment containing the LIM domain and two nebulin repeats has been shown to bind to actin molecules [25].
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Previous work has shown that type I NPFs including the N-WASP protein have a specialized domain called VCA that binds to both the Arp2/3 complex and to actin molecules.
Two types of NPFs have been identified: type I interact with individual actin molecules, while type II bind to actin filaments.
Hence, remodeling of the actin cytoskeleton architecture depends on a large group of signaling molecules that bind to actin and modulate the assembly of the actin network (see [ 1] for a comprehensive overview).
Our present and previous work indicates that the tropomyosin coiled coil is locally destabilized at regions of the molecule that bind to actin and other proteins, and that these regions contribute to the overall affinity and cooperativity of binding to actin in a sequence-specific fashion.
Signaling molecules can likewise bind to actin filaments, which was reported for NF- κB and its inhibitor I κB [ 31].
These data suggest that some of the effects of expressing these constructs result not from their ability to bind to actin, but perhaps because they recruit other signaling molecules differentially.
These proteins can bind to actin monomers (G-actin) and filaments and stimulate depolymerization and fragmentation of F-actin [12].
Phosphorylation of myosin allows it to bind to actin.
Intriguingly, it has been reported that LATS1 can bind to actin and inhibit actin polymerisation [ 147].
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