81 research outputs found
Phosphorylation of pig brain microtubule proteins. General properties and partial characterization of endogenous substrate and cyclic AMP-dependent protein kinase
Evidence that phorbol ester interferes with stimulated Ca2+ redistribution by activating Ca2+ efflux in neutrophil leucocytes
Transmembrane linkage between surface glycoproteins and components of the cytoplasm in neutrophil leukocytes.
Colchicine binding to bovine anterior pituitary slices and inhibition of growth-hormone release
Polymer Induced Bundling of F-actin and the Depletion Force
The inert polymer polyethylene glycol (PEG) induces a "bundling" phenomenon
in F-actin solutions when its concentration exceeds a critical onset value C_o.
Over a limited range of PEG molecular weight and ionic strength, C_o can be
expressed as a function of these two variables. The process is reversible, but
hysteresis is also observed in the dissolution of the bundles, with ionic
strength having a large influence. Additional actin filaments are able to join
previously formed bundles. Little, if any, polymer is associated with the
bundle structure.
Continuum estimates of the Asakura-Oosawa depletion force, Coulomb repulsion,
and van der Waals potential are combined for a partial explanation of the
bundling effect and hysteresis. Conjectures are presented concerning the
apparent limit in bundle size
The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling
The Z-disc, appearing as a fine dense line forming sarcomere boundaries in striated muscles, when studied in detail reveals crosslinked filament arrays that transmit tension and house myriads of proteins with diverse functions. At the Z-disc the barbed ends of the antiparallel actin filaments from adjoining sarcomeres interdigitate and are crosslinked primarily by layers of α-actinin. The Z-disc is therefore the site of polarity reversal of the actin filaments, as needed to interact with the bipolar myosin filaments in successive sarcomeres. The layers of α-actinin determine the Z-disc width: fast fibres have narrow (~30–50 nm) Z-discs and slow and cardiac fibres have wide (~100 nm) Z-discs. Comprehensive reviews on the roles of the numerous proteins located at the Z-disc in signalling and disease have been published; the aim here is different, namely to review the advances in structural aspects of the Z-disc
Endogenous phosphorylation and dephosphorylation of microtubule-associated proteins isolated from bovine anterior pituitary
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