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Complementary activities of TPX2 and chTOG constitute an efficient importin-regulated microtubule nucleation module.Phototriggerable 2',7-caged paclitaxelA designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus endReconstitution of a microtubule plus-end tracking system in vitroMotor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in the regulation of centrosome duplicationNucleotide-induced conformations in the neck region of dimeric kinesin.Folding and membrane insertion of the trimeric beta-barrel protein OmpF.Kinetics of folding and membrane insertion of a beta-barrel membrane protein.Processive movement of single kinesins on crowded microtubules visualized using quantum dots.Aster migration determines the length scale of nuclear separation in the Drosophila syncytial embryo.Synthesis and biological evaluation of new tetrahydro-beta-carbolines as inhibitors of the mitotic kinesin Eg5.Selection of genetically encoded fluorescent single domain antibodies engineered for efficient expression in Escherichia coli.Llama-derived single-chain antibody fragments directed to rotavirus VP6 protein possess broad neutralizing activity in vitro and confer protection against diarrhea in mice.Phosphorylation by Cdk1 increases the binding of Eg5 to microtubules in vitro and in Xenopus egg extract spindlesMotor-mediated cortical versus astral microtubule organization in lipid-monolayered droplets.A minimal midzone protein module controls formation and length of antiparallel microtubule overlaps.GTPgammaS microtubules mimic the growing microtubule end structure recognized by end-binding proteins (EBs).Chromophore-assisted light inactivation and self-organization of microtubules and motors.Mutations in Human Tubulin Proximal to the Kinesin-Binding Site Alter Dynamic Instability at Microtubule Plus- and Minus-Ends.Poleward transport of Eg5 by dynein-dynactin in Xenopus laevis egg extract spindlesCLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites.Obstacles on the microtubule reduce the processivity of Kinesin-1 in a minimal in vitro system and in cell extract.Microtubule aging probed by microfluidics-assisted tubulin washout.Fluorescence microscopy assays on chemically functionalized surfaces for quantitative imaging of microtubule, motor, and +TIP dynamics.End-binding proteins and Ase1/PRC1 define local functionality of structurally distinct parts of the microtubule cytoskeleton.Regulation of processive motion and microtubule localization of cytoplasmic dynein.EB1 accelerates two conformational transitions important for microtubule maturation and dynamics.Self-organization of motors and microtubules in lipid-monolayered droplets.A theoretical model of mitotic spindle elongation under experimental constraints.The size of the EB cap determines instantaneous microtubule stability.Important factors determining the nanoscale tracking precision of dynamic microtubule ends.An unconventional interaction between Dis1/TOG and Mal3/EB1 in fission yeast promotes the fidelity of chromosome segregation.Micropattern-guided assembly of overlapping pairs of dynamic microtubules.Reconstitution of a hierarchical +TIP interaction network controlling microtubule end tracking of dynein.Structural insight into TPX2-stimulated microtubule assembly.Physical properties determining self-organization of motors and microtubules.Combinatorial regulation of the balance between dynein microtubule end accumulation and initiation of directed motility.A single Drosophila embryo extract for the study of mitosis ex vivo.A kinesin-like motor inhibits microtubule dynamic instability.Development and biological evaluation of potent and specific inhibitors of mitotic Kinesin Eg5.
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P50
description
European-American biochemist
@en
europäisch-amerikanischer Biochemiker
@de
onderzoeker
@nl
հետազոտող
@hy
name
Thomas Surrey
@ast
Thomas Surrey
@de
Thomas Surrey
@en
Thomas Surrey
@es
Thomas Surrey
@nl
Thomas Surrey
@sl
label
Thomas Surrey
@ast
Thomas Surrey
@de
Thomas Surrey
@en
Thomas Surrey
@es
Thomas Surrey
@nl
Thomas Surrey
@sl
prefLabel
Thomas Surrey
@ast
Thomas Surrey
@de
Thomas Surrey
@en
Thomas Surrey
@es
Thomas Surrey
@nl
Thomas Surrey
@sl
P106
P166
P21
P31
P496
0000-0001-9082-1870