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Probing protein interactions in living mammalian cells on a microtubule benchPhosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubulesStudy of the DNA/ethidium bromide interactions on mica surface by atomic force microscope: influence of the surface friction.Atomic force microscopy imaging of DNA under macromolecular crowding conditions.YB-1 promotes microtubule assembly in vitro through interaction with tubulin and microtubules.Polyamine sharing between tubulin dimers favours microtubule nucleation and elongation via facilitated diffusion.Free mRNA in excess upon polysome dissociation is a scaffold for protein multimerization to form stress granules.mRNA and DNA selection via protein multimerization: YB-1 as a case study.Single molecule detection of PARP1 and PARP2 interaction with DNA strand breaks and their poly(ADP-ribosyl)ation using high-resolution AFM imaging.Role of tau in the spatial organization of axonal microtubules: keeping parallel microtubules evenly distributed despite macromolecular crowding.Role of microtubules in stress granule assembly: microtubule dynamical instability favors the formation of micrometric stress granules in cells.High-resolution imaging of microtubules and cytoskeleton structures by atomic force microscopy.The EcoRI-DNA complex as a model for investigating protein-DNA interactions by atomic force microscopy.A central role for polyamines in microtubule assembly in cells.Adsorption of DNA to mica mediated by divalent counterions: a theoretical and experimental study.The C terminus of tubulin, a versatile partner for cationic molecules: binding of Tau, polyamines, and calcium.Vectofusin-1, a Potent Peptidic Enhancer of Viral Gene Transfer forms pH-dependent α-Helical Nanofibrils, Concentrating Viral Particles.Spastin regulates VAMP7-containing vesicles trafficking in cortical neurons.High-resolution AFM imaging of single-stranded DNA-binding (SSB) protein--DNA complexes.Mica surface promotes the assembly of cytoskeletal proteins.Nanoscale Analysis Reveals the Maturation of Neurodegeneration-Associated Protein Aggregates: Grown in mRNA Granules then Released by Stress Granule Proteins.Polyamine signal through gap junctions: A key regulator of proliferation and gap-junction organization in mammalian tissues?Relation Between Stress Granules and Cytoplasmic Protein Aggregates Linked to Neurodegenerative DiseasesYB-1, an abundant core mRNA-binding protein, has the capacity to form an RNA nucleoprotein filament: a structural analysisCathodoluminescence imaging and spectroscopy by near-field detectionAtomic force microscopy reveals binding of mRNA to microtubules mediated by two major mRNP proteins YB-1 and PABPCharge inversion, condensation and decondensation of DNA and polystyrene sulfonate by polyethylenimineDetection of single DNA molecule hybridization on a surface by atomic force microscopyMicrotubules as platforms for probing liquid-liquid phase separation in cells - application to RNA-binding proteinsU2AF65 assemblies drive sequence-specific splice site recognitionPARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNAA Single-Molecule Atomic Force Microscopy Study of PARP1 and PARP2 Recognition of Base Excision Repair DNA Intermediates
P50
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P50
description
researcher ORCID ID = 0000-0002-3348-9514
@en
wetenschapper
@nl
name
David Pastre
@ast
David Pastre
@en
David Pastre
@es
David Pastre
@nl
type
label
David Pastre
@ast
David Pastre
@en
David Pastre
@es
David Pastre
@nl
prefLabel
David Pastre
@ast
David Pastre
@en
David Pastre
@es
David Pastre
@nl
P106
P1153
6603951855
P21
P31
P496
0000-0002-3348-9514