about
CDC42 switches IRSp53 from inhibition of actin growth to elongation by clustering of VASPRickettsia Sca2 has evolved formin-like activity through a different molecular mechanismMechanism of IRSp53 inhibition and combinatorial activation by Cdc42 and downstream effectorsHigh-performance time-resolved fluorescence by direct waveform recording.Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chainArp you ready for actin in the nucleus?Structural analysis of the transitional state of Arp2/3 complex activation by two actin-bound WCAs.Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin.WHAMM links actin assembly via the Arp2/3 complex to autophagySubunit Rtt102 controls the conformation of the Arp7/9 heterodimer and its interactions with nucleotide and the catalytic subunit of SWI/SNF remodelersSite-directed spectroscopic probes of actomyosin structural dynamics.WHAMM Directs the Arp2/3 Complex to the ER for Autophagosome Biogenesis through an Actin Comet Tail MechanismThe Cytoskeleton-Autophagy Connection.Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin.Mechanism of IRSp53 inhibition by 14-3-3IRSp53 coordinates AMPK and 14-3-3 signaling to regulate filopodia dynamics and directed cell migration
P50
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P50
description
researcher ORCID ID = 0000-0002-1031-1211
@en
wetenschapper
@nl
name
David J Kast
@ast
David J Kast
@en
David J Kast
@es
David J Kast
@nl
type
label
David J Kast
@ast
David J Kast
@en
David J Kast
@es
David J Kast
@nl
prefLabel
David J Kast
@ast
David J Kast
@en
David J Kast
@es
David J Kast
@nl
P106
P1153
21742361300
P21
P31
P496
0000-0002-1031-1211