Titlebook: Actin-Monomer-Binding Proteins; Pekka Lappalainen Book 2007 Springer-Verlag New York 2007 biology.cell.cell biology.cellular processes.cyt

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https://doi.org/10.1007/978-3-319-64027-3 prevent the assembly of actin monomers into filament ends. In addition to monomeric actin, twinfilins also bind and cap actin filament barbed ends, and interact direcdy with heterodimeric capping proteins. Interaction with capping protein is necessary for twinfilins localization to the cortical act

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Mahdokht Kalantari,Philipp Rauschnabels and, with one exception, absent in mammals in which the classical single repeat β-thymosins appear dominant. The repeated nature in combination with sequence variation in the consecutive modules renders these proteins different actin modulating capacities as compared to the classical β-thymosins.

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Anna Samira Praetorius,Daniel G?rlichcleation and elongation of actin filaments, which can be catalysed by a limited number of proteins or protein complexes, the best studied of which is the Arp2/3-complex. The activity of the Arp2/3 complex is tightly regulated and controlled through signal-dependent association with nucleation promot

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Augmented Reality and Virtual Realityllular transport. A large number of actin-binding proteins (ABPs) participate in this process, regulating the assembly of actin filaments into functional networks. ABPs are extremely diverse, both structurally and functionally, but they most seem to share a common binding area on the actin surface,

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Actin-Monomer-Binding Proteins978-0-387-46407-7Series ISSN 1431-0414

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