about
Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement.Building bridges toward invasion: tumor promoter treatment induces a novel protein kinase C-dependent phenotype in MCF10A mammary cell aciniFHOD1 interaction with nesprin-2G mediates TAN line formation and nuclear movement.Identification of an essential domain in the herpesvirus VP1/2 tegument protein: the carboxy terminus directs incorporation into capsid assemblonsLamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement.KASHing up with the nucleus: novel functional roles of KASH proteins at the cytoplasmic surface of the nucleus.Orientation and function of the nuclear-centrosomal axis during cell migration.Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1.MyTH4-FERM myosins have an ancient and conserved role in filopod formationResponsive microtubule dynamics promote cell invasion by Trypanosoma cruzi.Quantitative Brightness Analysis of Protein Oligomerization in the Nuclear Envelope.TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement.Ubiquitination of both adeno-associated virus type 2 and 5 capsid proteins affects the transduction efficiency of recombinant vectors.LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia.Molecular Insights into the Mechanisms of SUN1 Oligomerization in the Nuclear Envelope.Fluorescence Fluctuation Spectroscopy Reveals Differential SUN Protein Oligomerization In Living Cells.Conserved SUN-KASH Interfaces Mediate LINC Complex-Dependent Nuclear Movement and PositioningHDAC6-pack: cortactin acetylation joins the brewContractile acto-myosin network on nuclear envelope remnants positions human chromosomes for mitosisFunction of Torsin AAA+ ATPases in Pseudorabies Virus Nuclear EgressDYT1 Dystonia Patient-Derived Fibroblasts Have Increased Deformability and Susceptibility to Damage by Mechanical ForcesA synthetic biology platform for the reconstitution and mechanistic dissection of LINC complex assemblyProtein oligomerization and mobility within the nuclear envelope evaluated by the time-shifted mean-segmented Q factorImbalanced nucleocytoskeletal connections create common polarity defects in progeria and physiological agingCorrection: A synthetic biology platform for the reconstitution and mechanistic dissection of LINC complex assembly (doi:10.1242/jcs.219451)
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description
researcher
@en
wetenschapper
@nl
name
G W Gant Luxton
@en
G W Gant Luxton
@nl
type
label
G W Gant Luxton
@en
G W Gant Luxton
@nl
prefLabel
G W Gant Luxton
@en
G W Gant Luxton
@nl
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P31
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0000-0002-6180-8906