prof. dr. Jan Gettemans
Show
Sort by
-
Selected BTB/POZ-kelch proteins bind ATP.
-
PIP2-PDZ domain binding controls the association of syntenin with the plasma membrane.
-
A novel endogenous PP2C-like phosphatase dephosphorylates casein kinase II-phosphorylated Physarum fragmin.
-
Identification of Tyr438 as the major in vitro c-Src phosphorylation site in human gelsolin: A mass spectrometric approach.
-
Introduction to the histology and cell biology of the actin cytoskeleton.
-
The crystal structure of the Physarum polycephalum actin-fragmin kinase: an atypical protein kinase with a specialized substrate-binding domain.
-
Physarum amoebae express a distinct fragmin-like actin-binding protein that controls in vitro phosphorylation of actin by the actin-fragmin kinase.
-
Disruption of the actin cytoskeleton of mammalian cells by the capping complex actin-fragmin is inhibited by actin phosphorylation and regulated by Ca2+ ions.
-
Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid.
-
Molecular cloning, over-expression, developmental regulation and immunolocalization of fragminP, a gelsolin-related actin-binding protein from Physarum polycephalum plasmodia.