Zobrazeno 1 - 10
of 1 974
pro vyhledávání: '"Actin monomer binding"'
Profilin’s Affinity for Formin Regulates the Availability of Filament Ends for Actin Monomer Binding
Autor:
Zweifel, Mark E., Courtemanche, Naomi
Publikováno v:
In Journal of Molecular Biology 4 December 2020 432(24)
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Publikováno v:
In Journal of Biological Chemistry 22 October 2010 285(43):33265-33280
Profilin’s affinity for formin regulates the availability of filament ends for actin monomer binding
Autor:
Naomi Courtemanche, Mark E. Zweifel
Publikováno v:
J Mol Biol
Nucleation-promoting proteins tightly regulate actin polymerization in cells. Whereas many of these proteins bind actin monomers directly, formins use the actin-binding protein profilin to dynamically load actin monomers onto their flexible Formin Ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeafb0377fd8be19f35e590b320fe022
https://europepmc.org/articles/PMC7738411/
https://europepmc.org/articles/PMC7738411/
Publikováno v:
In Trends in Cell Biology 2004 14(7):386-394
Autor:
Paavilainen, Ville O. ‡, §, Merckel, Michael C. ¶, Falck, Sandra ‡, Ojala, Pauli J. ‡, Pohl, Ehmke ‖, Wilmanns, Matthias ‖, Lappalainen, Pekka ‡, **
Publikováno v:
In Journal of Biological Chemistry 8 November 2002 277(45):43089-43095
Publikováno v:
Journal of Biological Chemistry. 285:33265-33280
Many actin-binding proteins have been shown to possess multiple activities to regulate filament dynamics. Tropomodulins (Tmod1–4) are a conserved family of actin filament pointed end-capping proteins. Our previous work has demonstrated that Tmod3 b
Autor:
Sandra Falck, Pekka Lappalainen, Matthias Wilmanns, Michael C. Merckel, Pauli J. Ojala, Ville O. Paavilainen, Ehmke Pohl
Publikováno v:
Journal of Biological Chemistry. 277:43089-43095
Twinfilin is an evolutionarily conserved actin monomer-binding protein that regulates cytoskeletal dynamics in organisms from yeast to mammals. It is composed of two actin-depolymerization factor homology (ADF-H) domains that show approximately 20% s
Autor:
Pekka Lappalainen
The actin cytoskeleton plays a central role in many cellular processes including cell motility, cytokinesis, endocytosis and phagocytosis. The structure and dynamics of the actin cytoskeleton is regulated by a large number of proteins that interact w