Myosin-X and disease.
Chapel Hill, United States. In Exp Cell Res, Jun 2015
Myosin-X (Myo10) is a motor protein best known for its role in filopodia formation.
Cargo recognition and cargo-mediated regulation of unconventional myosins.
Hong Kong, Hong Kong. In Acc Chem Res, 2014
The structures of the MyTH4-FERM tandems from myosin-VIIa and myosin-X in complex with their respective targets reveal that MyTH4 and FERM domains extensively interact with each other forming structural and functional supramodules in both motors and demonstrate that the structurally similar MyTH4-FERM tandems of the two motors display totally different target binding modes.
An overview of tools for the validation of protein NMR structures.
Leicester, United Kingdom. In J Biomol Nmr, 2014
To discuss their relative merits we have applied the tools to two representative examples from the PDB: a small, globular monomeric protein (Staphylococcal nuclease from S. aureus, PDB entry 2kq3) and a small, symmetric homodimeric protein (a region of human myosin-X, PDB entry 2lw9).
Myosin-X: a MyTH-FERM myosin at the tips of filopodia.
Chapel Hill, United States. In J Cell Sci, 2011
Myosin-X (Myo10) is an unconventional myosin with MyTH4-FERM domains that is best known for its striking localization to the tips of filopodia and its ability to induce filopodia.
Filopodia and adhesion in cancer cell motility.
Finland. In Cell Adh Migr, 2011
Integrins are cell surface adhesion receptors critically implicated in cell migration and they are transported actively to filopodia tips by an unconventional myosin, myosin-X.
Myosin VI undergoes cargo-mediated dimerization.
Hong Kong, Hong Kong. In Cell, 2009
The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.