The disease-mutant desmin variants E245D and T453I exhibited increased binding affinity for nebulette delayed filament assembly kinetics and caused significant weakening of networks.
During fasting desmin phosphorylation increases and enhances Trim32-mediated degradation of the desmin cytoskeleton which appears to facilitate the breakdown of Z-bands and thin filaments.
the state of desmin-filament assembly is crucial for synemin anchorage and consequently might involve mechanical and functional stability of the cytoskeletal network
ability of Surfactant protein A to interact with desmin and vimentin and to prevent polymerization of desmin monomers shed light on unexpected and wider biological roles of this collectin
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