Zdenek Lansky
Lánský, Zdeněk, 1978-
VIAF ID: 85211347 (Personal)
Permalink: http://viaf.org/viaf/85211347
Preferred Forms
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- 100 0 _ ‡a Zdenek Lansky
4xx's: Alternate Name Forms (3)
Works
Title | Sources |
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Adaptive braking by Ase1 prevents overlapping microtubules from sliding completely apart | |
Anillin propels myosin-independent constriction of actin rings | |
Ca(2+) binding protein S100A1 competes with calmodulin and PIP2 for binding site on the C-terminus of the TPRV1 receptor. | |
Cell Biology: Kinesin-14 Backsteps to Organize Polymerizing Microtubules. | |
Changes in electrostatic surface potential of Na+/K+-ATPase cytoplasmic headpiece induced by cytoplasmic ligand(s) binding. | |
Changes in microtubule overlap length regulate kinesin-14-driven microtubule sliding. | |
The characterization of a novel S100A1 binding site in the N-terminus of TRPM1. | |
Cytoskeletal organization through multivalent interactions | |
Diffusible crosslinkers generate directed forces in microtubule networks. | |
Diffusive tail anchorage determines velocity and force produced by kinesin-14 between crosslinked microtubules. | |
Entropic forces drive contraction of cytoskeletal networks | |
Flagellar microtubule doublet assembly in vitro reveals a regulatory role of tubulin C-terminal tails | |
Human histone deacetylase 6 shows strong preference for tubulin dimers over assembled microtubules | |
The human kinesin-14 HSET tracks the tips of growing microtubules in vitro | |
The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase. | |
Integrative binding sites within intracellular termini of TRPV1 receptor | |
Kinesin's step dissected with single-motor FRET. | |
Kinetically distinct phases of tau on microtubules regulate kinesin motors and severing enzymes | |
Mitochondria-adaptor TRAK1 promotes kinesin-1 driven transport in crowded environments | |
The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site. | |
Studying kinesin's enzymatic cycle using a single-motor confocal motility assay, employing Förster resonance energy transfer |