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ADP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
ATP + H2O + a kinesin associated with a microtubule at position n =
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r
Alexa Fluor 647 ATP + H2O + a kinesin associated with a microtubule at position n
Alexa Fluor 647 ADP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Alexa Fluor 647 ATP, a fluorescent ATP analog, activity determined by FRET-based assays, Förster resonance energy transfer assays. The fluorescent ATP analog can fuel kinesin-1'S processsive motion and is a suitable substrate analog, but it alters the motor's kinetic parameters
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
methylanthraniloyl-ATP + H2O + a kinesin associated with a microtubule at position n
methylanthraniloyl-ADP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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unconventional ATPase cycle, adapted for microtubule depolymerization, low basal activity is accelerated by tubulin and microtubles
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additional information
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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conventional kinesin is required for the microtubule plus-end accumulation of cytoplasmic dynein and dynactin but not for NUDF
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Chlamydomonas sp.
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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the movement of newly assembled african swine fever virus particles from the factory to the cell surface is dependent on conventional kinesin
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
kinesin-13 neck sequence makes a significant contribution to depolymerization afficiency, and is essential to enable these motors to control cellular microtubule dynamics
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
microtubules and kinesin I are required for the selective accumulation of oskar mRNA at the posterior cortex of the Drosophila melanogaster oocyte
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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centralspindlin is a plus-end-directed motor. Centralspindlin cannot utilize MgGTP to generate force for microtubule movement
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Drosophila sp. (in: flies)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Drosophila sp. (in: flies)
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kinesin motor domain interacts with both alpha- and beta-tubulin
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Drosophila sp. (in: flies)
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kinesin switches from weak to strong binding via ADP release, and back again via ADP trapping
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Eh Klp5 is a divergent member of the kinesin 5 family that regulates genome content and microtubular assembly
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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the enzyme KIF3 promotes microtubule gliding
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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-
210541, 210544, 210545, 210546, 210550, 210552, 210554, 210555, 210556, 656244, 668409, 669467, 670380, 670970, 685523, 687306, 697234, 699906, 701009, 711485, 719361, 719412, 719907, 720197, 734241 -
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
analysis of structures of ADP-bound kinesin
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
in regulating plus end motility, KIF16B governs the spatial distribution of early endosomes in vivo and the balance between receptor recycling and degradation
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
kinesin-2 is required for the normal steady-state localization of late endosomes/lysosomes but not early ensosomes or recycling endosomes. Kinesin-2 contributes significantly to the plus-end-directed movement of late endosomes and lysosomes
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
monomeric kinesin Eg5 has a motor tightly bound to the microtubule during a majority of its ATPase cycle to generate and sustain force in the mitotic spindle
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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plus-end-enriched motor that targets regions of podosome turnover. Kinesin KIF1C is a central player in the microtubule-dependent regulation of podosomes. The KIF1C-myosin IIA interface may play a role in facilitating podosomes dynamics in a subcellular fine-tuned manner
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Eg5 is a homotetrameric kinesin-5 involved in centrosome separation and assembly of the bipolar mitotic spindle. The stable dimer Eg5-513 promotes robust plus-end-directed microtubule gliding at a rate similar to that of homotetrameric Eg5 in vitro. Eg5-513 exhibits slow ATP turnover, high affinity for ATP, and a weakened affinity for microtubules when compared to monomeric Eg5
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
KIF16B is a plus end-directed motor
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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MCAK moves along the microtubule lattice in one-dimensional random walk
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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plus-end-enriched motor that targets regions of podosome turnover
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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the microtubule-Eg5 complex binds MgATP tightly, followed by rapid ATP hydrolysis with a subsequent slow step that limits steady-state turnover. Presence of microtubules accelerates the kinetics of each step in the ATPase pathway and amplifies the nucleotide-dependent structural transitions required for force generation. Phosphate product release and Eg5 detachment from the microtubule are coupled with a step occuring at the slow rate after ATP hydrolysis followed by the second step occuring more rapidly
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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unconventional ATPase cycle, adapted for microtubule depolymerization, low basal activity is accelerated by tubulin and microtubles
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
modeling reveals key nucleotide-dependent changes in the structure and flexibility of the nucleotide-binding pocket and the tubulin-binding site, and allosterically coupled motions driving the APO to ATP transition of ATPase states, extension and shortening of alpha4 helix during the ATPase cycle
structural mechanism of ADP release
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
the enzyme has a critical role during the metaphase-anaphase transition and cytokinesis. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. The footprint of the MKLP2 motor domain on the microtubule surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
the Kif18A motor domain depolymerizes microtubule plus and minus ends
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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210547, 210549, 210550, 210552, 210553, 210568, 654443, 656860, 656864, 687450, 697787 -
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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a single ATP hydrolysis triggers a single stepping movement of a single KIF1A monomer
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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kinesin I and cytoplasmic dynein orchestrate glucose-stimulated insulin-containing vesicle movements in clonal MIN6 beta-cells. The majority of transport of large dense-core vesicles in beta-cells is mediated by kinesin I, whilst dynein probably contributes to the recovery of vesicles after rapid kiss-and-run exocytosis
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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the majority of moving phagosomes are minus-end directed, the remainder moves towards microtubule plus-ends and a small subset moves bi-directionally. Minus-end movement showes pharmacological characteristics expected for dyneins, plus-end movement displayed pharmacological properties of kinesin
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
nucleotide-induced conformational change catalytic method
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
the enzyme has a critical role during the metaphase-anaphase transition and cytokinesis. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. The footprint of the MKLP2 motor domain on the microtubule surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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plus-end directed kinesin motor moves in a non-processive fashion to its destination
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
AK065586
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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alternating site ATPase pathway, including a captive head state as an intermediate in the kinesin ATPase cycle
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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KIF4 moves along microtubules toward the plus-end
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Kip3p destabilizes microtubules by depolymerizing them. Kip3p disassembles microtubules exclusively at the plus end and depolymerizes longer microtubules faster than shorter ones
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Kip3P is both a plus-end-specific depolymerase and a plus end-directed motor
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
kinesin-8/Kip3 uses ATP hydrolysis for stepping on the microtubule lattice, but at the plus-end, Kip3 undergoes a switch. Its ATPase activity is suppressed when it binds tightly to the curved conformation of tubulin. This prolongs plus-end binding, stabilizes protofilament curvature, and ultimately promotes microtubule disassembly
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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the DASH complex and Klp5/Klp6 kinesin coordinate bipolar chromosome attachment in fission yeast
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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kinesin-8 expressed in insect cells forms a heterodimer that hydrolyzes ATP in a microtubule-dependent manner and moves on microtubules toward their plus ends
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Kin5 is an intraciliary transport motor
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
in vitro ATPase activity of the purified motor domain of TbKIN-D
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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kinesin-1 supports long-range hyphal growth. Kinesin-1, kinesin-3 and myosin-V cooperate in polarized growth. Kinesin-3 participates in acid phosphatase secretion in hyphae
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
kinesin-1 motor is required for efficient microtubule bundling and participates in microtubule bending in vivo
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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the rate of ER tubule extensions toward microtubule plus ends is lower than minus end-directed motility. Initiation of plus end-directed ER motility in somatic cytosol is likely to occur via activation of membrane-associated kinesin
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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kinesin MCAK/XKCM1destabilizes microtubules. Kinesin MCAK/XKCM1 is essential for controlling the distribution of microtubules by inducing their depolymerization
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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kinesin-5 Eg5 drives the sliding of microtubules depending on their relative orientation. Eg5 has the capability of simultaneously moving at about 20 nm/s towards the plus-ends of each of the two microtubules it crosslinks. For anti-parallel microtubules, this results in relative sliding at about 40 nm/s, comparable to spindle pole separation rates in vivo. Eg5 can tether microtubule plus-ends, suggesting an additional microtubule-binding mode for Eg5
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
Chlamydomonas sp.
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
Drosophila sp. (in: flies)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
additional information
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during morphogenesis of the Drosophila embryo mitotic spindle, KLP61F's crosslinking and sliding activities can facilitate the gradual accumulation of KLP61F within antiparallel interpolar microtubules at the equator, where the motor can generate force to drive poleward flux and pole-pole separation
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additional information
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KLP61F displays a 3fold higher preference for crosslinking microtubules in the antiparallel orientation, this polarity preference is observed in the presence of ADP or ATP plus AMPPNP, but not AMPPNP alone
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additional information
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NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including adenosine-5'-(beta,gamma-imido)triphosphate, are weakened, NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis.
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additional information
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the binding of tail peptides to head dimers is fast and readily reversible, the second tail peptide in a folded kinesin-1 may be available to bind other molecules while kinesin-1 remains folded
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additional information
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during the ATP-waiting state, the mobile tethered head of kinesin1 containing ADP can transiently interact with the microtubule
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additional information
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KIF4 regulates Gag stability and trafficking
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additional information
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kinesin spindle protein is essential for mitotic spindle assembly in dividing human cells and is required for cell cycle progression through mitosis
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additional information
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the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release
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additional information
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key residues involved in kinesin-tubulin binding
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additional information
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key residues involved in kinesin-tubulin binding
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additional information
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animals survive lowered amounts of KIF3A and KIF3B through heterozygosity. Only in complete absence of KI3A do photoreceptor cells die, and homozygous null mutants of Kif3a are embryonic lethal in mice
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additional information
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kinesin-2 binds the full-length variant of Hippel-Lindau tumour suppressor protein (pVHL30) in primary kidney cells, and mediate its association to microtubules
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additional information
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KIF4 specifically binds to the microtubule, enzyme interaction with tubulin, the KIF4-specific Q248 and K249 form possible hydrogen bonds with Y108 of helix H3' of alpha-tubulin. Microtubule filament binding by enzyme KIF4, around the center line of the microtubule protofilament, the helix-alpha4-mediated microtubule-binding site is located and fitted into the intra-tubulin dimer groove
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additional information
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kinesin-8 contributes both to chromosome congression to the metaphase plate and to the coupling of spindle microtubules to kinetochores during anaphase A
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additional information
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enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin
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additional information
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enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin
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additional information
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full-length Eg5's motility comprises an unbiased, diffusive mode independent of ATP hydrolysis and a plus end-directed processive mode that requires ATP hydrolysis, Eg5 can switch from diffusive motility to directional motility upon binding to a second microtubule
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
additional information
?
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
conventional kinesin is required for the microtubule plus-end accumulation of cytoplasmic dynein and dynactin but not for NUDF
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Chlamydomonas sp.
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Drosophila sp. (in: flies)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Drosophila sp. (in: flies)
-
kinesin motor domain interacts with both alpha- and beta-tubulin
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Eh Klp5 is a divergent member of the kinesin 5 family that regulates genome content and microtubular assembly
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
the enzyme KIF3 promotes microtubule gliding
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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210541, 210544, 210545, 210546, 210550, 210552, 210554, 210555, 210556, 656244, 668409, 669467, 670380, 719361, 734241 -
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
in regulating plus end motility, KIF16B governs the spatial distribution of early endosomes in vivo and the balance between receptor recycling and degradation
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
kinesin-2 is required for the normal steady-state localization of late endosomes/lysosomes but not early ensosomes or recycling endosomes. Kinesin-2 contributes significantly to the plus-end-directed movement of late endosomes and lysosomes
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
monomeric kinesin Eg5 has a motor tightly bound to the microtubule during a majority of its ATPase cycle to generate and sustain force in the mitotic spindle
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
plus-end-enriched motor that targets regions of podosome turnover. Kinesin KIF1C is a central player in the microtubule-dependent regulation of podosomes. The KIF1C-myosin IIA interface may play a role in facilitating podosomes dynamics in a subcellular fine-tuned manner
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
the enzyme has a critical role during the metaphase-anaphase transition and cytokinesis. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. The footprint of the MKLP2 motor domain on the microtubule surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
the Kif18A motor domain depolymerizes microtubule plus and minus ends
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
kinesin I and cytoplasmic dynein orchestrate glucose-stimulated insulin-containing vesicle movements in clonal MIN6 beta-cells. The majority of transport of large dense-core vesicles in beta-cells is mediated by kinesin I, whilst dynein probably contributes to the recovery of vesicles after rapid kiss-and-run exocytosis
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
the majority of moving phagosomes are minus-end directed, the remainder moves towards microtubule plus-ends and a small subset moves bi-directionally. Minus-end movement showes pharmacological characteristics expected for dyneins, plus-end movement displayed pharmacological properties of kinesin
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
the enzyme has a critical role during the metaphase-anaphase transition and cytokinesis. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. The footprint of the MKLP2 motor domain on the microtubule surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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alternating site ATPase pathway, including a captive head state as an intermediate in the kinesin ATPase cycle
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Kip3p destabilizes microtubules by depolymerizing them. Kip3p disassembles microtubules exclusively at the plus end and depolymerizes longer microtubules faster than shorter ones
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Kip3P is both a plus-end-specific depolymerase and a plus end-directed motor
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Kin5 is an intraciliary transport motor
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
kinesin-1 supports long-range hyphal growth. Kinesin-1, kinesin-3 and myosin-V cooperate in polarized growth. Kinesin-3 participates in acid phosphatase secretion in hyphae
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
the rate of ER tubule extensions toward microtubule plus ends is lower than minus end-directed motility. Initiation of plus end-directed ER motility in somatic cytosol is likely to occur via activation of membrane-associated kinesin
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ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
kinesin MCAK/XKCM1destabilizes microtubules. Kinesin MCAK/XKCM1 is essential for controlling the distribution of microtubules by inducing their depolymerization
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?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
kinesin-5 Eg5 drives the sliding of microtubules depending on their relative orientation. Eg5 has the capability of simultaneously moving at about 20 nm/s towards the plus-ends of each of the two microtubules it crosslinks. For anti-parallel microtubules, this results in relative sliding at about 40 nm/s, comparable to spindle pole separation rates in vivo. Eg5 can tether microtubule plus-ends, suggesting an additional microtubule-binding mode for Eg5
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
Chlamydomonas sp.
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
-
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
Drosophila sp. (in: flies)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
-
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
-
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?
additional information
?
-
-
during morphogenesis of the Drosophila embryo mitotic spindle, KLP61F's crosslinking and sliding activities can facilitate the gradual accumulation of KLP61F within antiparallel interpolar microtubules at the equator, where the motor can generate force to drive poleward flux and pole-pole separation
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?
additional information
?
-
-
KLP61F displays a 3fold higher preference for crosslinking microtubules in the antiparallel orientation, this polarity preference is observed in the presence of ADP or ATP plus AMPPNP, but not AMPPNP alone
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-
?
additional information
?
-
-
NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including adenosine-5'-(beta,gamma-imido)triphosphate, are weakened, NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis.
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?
additional information
?
-
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the binding of tail peptides to head dimers is fast and readily reversible, the second tail peptide in a folded kinesin-1 may be available to bind other molecules while kinesin-1 remains folded
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additional information
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during the ATP-waiting state, the mobile tethered head of kinesin1 containing ADP can transiently interact with the microtubule
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additional information
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KIF4 regulates Gag stability and trafficking
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additional information
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kinesin spindle protein is essential for mitotic spindle assembly in dividing human cells and is required for cell cycle progression through mitosis
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additional information
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the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release
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additional information
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animals survive lowered amounts of KIF3A and KIF3B through heterozygosity. Only in complete absence of KI3A do photoreceptor cells die, and homozygous null mutants of Kif3a are embryonic lethal in mice
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additional information
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kinesin-2 binds the full-length variant of Hippel-Lindau tumour suppressor protein (pVHL30) in primary kidney cells, and mediate its association to microtubules
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additional information
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KIF4 specifically binds to the microtubule, enzyme interaction with tubulin, the KIF4-specific Q248 and K249 form possible hydrogen bonds with Y108 of helix H3' of alpha-tubulin. Microtubule filament binding by enzyme KIF4, around the center line of the microtubule protofilament, the helix-alpha4-mediated microtubule-binding site is located and fitted into the intra-tubulin dimer groove
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additional information
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kinesin-8 contributes both to chromosome congression to the metaphase plate and to the coupling of spindle microtubules to kinetochores during anaphase A
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additional information
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enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin
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additional information
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enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin
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additional information
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full-length Eg5's motility comprises an unbiased, diffusive mode independent of ATP hydrolysis and a plus end-directed processive mode that requires ATP hydrolysis, Eg5 can switch from diffusive motility to directional motility upon binding to a second microtubule
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((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methanamine
-
(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)(1-methylpiperidin-3-yl)methanone
-
(2R)-2-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-methylbutan-1-one
-
(2R)-2-amino-3-((1,1,2-triphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1,1-bis(4-chlorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1,1-bis(4-fluorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1,1-bis(4-methylphenyl)-2-phenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(2-fluorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(3,4-dichlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(3-chlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(3-chlorophenyl)-1-(4-chlorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(3-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(4-chlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(4-fluorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(4-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(4-methylphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((2-(3,4-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((2-(3-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((2-(4-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-[(1,1,3-triphenylpropyl)sulfanyl]propanoic acid
-
-
(2R,4aS,5R,10bS)-2-((1H-1,2,4-triazol-1-yl)methyl)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(2S)-2-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-methylbutan-1-one
-
(4aS,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,10bS)-9-(tert-butyl)-5-(3-chlorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,10bS)-9-(tert-butyl)-5-(3-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline-9-carbonitrile
-
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline-9-carboxylic acid
-
(4aS,5R,10bS)-5-phenyl-9-(trifluoromethoxy)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-5-phenyl-9-propyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-7,9-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-7-fluoro-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-8,10-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-8,9-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-8-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-8-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(pentafluoro-lambda6-sulfanyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(1H-imidazol-2-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(2-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-chlorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-fluoro-4-methoxyphenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(4-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(pyridin-3-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(thiazol-2-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-chloro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-ethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-isopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-methyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-N,N-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-amine
-
(4aS,5S,10bS)-9-(tert-butyl)-5-cyclohexyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
1-((2R,4aS,5R,10bS)-5-(4-fluorophenyl)-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
-
1-((2R,4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
-
1-((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
-
1-((2R,4aS,5R,10bS)-9-cyclopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
-
1-(1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
i.e. tetrahydro-beta-carboline
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-(piperidin-1-yl)propan-1-one
-
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
-
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
1-(2-(dimethylamino)ethyl)-3-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)urea
-
1-(3,6-dibromo-9H-carbazol-9-yl)-3-phenethylamino-2-propanol
-
-
1-(3,6-dichloro-9H-carbazol-9-yl)-3-phenethylamino-2-propanol
-
induces cell death
1-(3-hydroxypropyl)-3-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)urea
-
1-(4'-tert-butylbiphenyl-4-yl)urea
-
-
1-(4'-[(trifluoromethyl)sulfonyl]biphenyl-4-yl)urea
-
-
1-(4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenyl)ethanone
-
1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-2-(piperidin-4-yl)ethanone
-
1-(benzenesulfinyl)-2,4-dinitrobenzene
-
1-(benzenesulfinyl)-2-nitrobenzene
-
1-(benzenesulfonyl)-2,4-dinitrobenzene
-
1-(benzenesulfonyl)-2-nitro-4-(trifluoromethyl)benzene
-
1-(benzenesulfonyl)-2-nitrobenzene
-
1-(benzenesulfonyl)-4-chloro-2-nitrobenzene
i.e. BTB-1, reversibly inhibits the microtubule-stimulated ATPase activity of Kif18A
1-(benzenesulfonyl)-4-fluoro-2-nitrobenzene
-
1-phenethylamino-3-phenothiazin-10-yl-propan-2-ol
-
induces strong mitotic arrest followed by cell death. More than 90% of cells exhibit the monoastral spindle instead of the normal mitotic spindle. Inhibitor selectively kills transformed culture cells; the inhibitor selectively kills transformed cell cultures
1-[(4-chlorophenyl)methanesulfonyl]-2,4-dinitrobenzene
-
1-[(4-methoxyphenyl)methanesulfinyl]-2-nitrobenzene
-
1-[(4-methoxyphenyl)methanesulfonyl]-2-nitrobenzene
-
1-[(4-methylphenyl)methanesulfinyl]-2,4-dinitrobenzene
-
1-[(4-methylphenyl)methanesulfonyl]-2,4-dinitrobenzene
-
1-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]urea
-
-
1-[3'-nitro-4'-(trifluoromethyl)biphenyl-4-yl]urea
-
-
1-[3-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]urea
-
-
1-[4'-(propan-2-yl)biphenyl-4-yl]urea
-
-
1-[4'-(trifluoromethyl)biphenyl-4-yl]thiourea
-
-
1-[4'-(trifluoromethyl)biphenyl-4-yl]urea
-
-
1-[4-(1,3-benzodioxol-5-yl)phenyl]urea
-
-
1-[4-(2,2,3,3-tetrafluoro-2,3-dihydro-1,4-benzodioxin-6-yl)phenyl]urea
-
-
2-((((2R,4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)(ethyl)amino)ethanol
-
2-((((2R,4aS,5R,10bS)-9-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)amino)ethanol
-
2-((1,1,2-triphenylethyl)sulfanyl)ethanaminium tetrafluoroborate
-
-
2-((1,1-bis(4-chlororophenyl)-2-phenylethyl)sulfanyl)ethanamine
-
-
2-((1,1-bis(4-fluorophenyl)-2-phenylethyl)sulfanyl)ethanamine
-
-
2-((1,1-bis(4-methylphenyl)-2-phenylethyl)sulfanyl)ethanamine
-
-
2-((1-(2-fluorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
-
-
2-((1-(3,4-dichlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
-
-
2-((1-(3-chlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanaminium tetrafluoroborate
-
-
2-((1-(3-chlorophenyl)-1-(4-chlorophenyl)-2-phenylethyl)sulfanyl)ethanamine
-
-
2-((1-(3-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
-
-
2-((1-(4-chlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
-
-
2-((1-(4-fluorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
-
-
2-((1-(4-hydroxylphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
-
-
2-((1-(4-methylphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
-
-
2-((2R,4aS,5R,10bS)-9-(tert-butyl)-2-((methylamino)methyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
-
2-((4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-yl)acetonitrile
-
2-((4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-yl)ethanol
-
2-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)-4-chlorobenzenethiol
-
2-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
-
2-((diphenyl(pyridin-4-yl)methyl)sulfanyl)ethanamine
-
-
2-(2,4-difluorophenyl)-9-(3,4-dimethylphenyl)-8-oxo-8,9-dihydro-7H-purine-6-carboxamide
-
-
2-(2-sulfanylethoxy)ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
-
2-(4-chloro-2-nitrobenzene-1-sulfinyl)naphthalene
-
2-(4-chloro-2-nitrobenzene-1-sulfonyl)thiophene
-
2-(dimethylamino)ethyl (((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)carbamate
-
2-(methylamino)-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)ethanesulfonothioamide
-
2-(tritylthio)ethanamine
-
-
2-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
-
2-[1-(4-methoxyphenyl)-5-oxo-3-[2-(thiophen-2-yl)ethyl]-2-thioxoimidazolidin-4-yl]-N-phenylacetamide
-
-
2-[2-(acetylsulfanyl)ethoxy]ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
-
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)aniline
-
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
-
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
-
3-(2-((2-aminoethyl)sulfonyl)-6-chloro-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)phenol
-
3-(dimethylamino)-N-(((2R,4aS,5R,10bS)-9-isopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)propane-1-sulfonamide
-
3-amino-1-(1-(2-aminopyridin-4-yl)-6-chloro-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-fluorophenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-6-(trifluoromethoxy)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-6-isopropyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-6-phenyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-methoxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-bromo-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-chloro-1-cyclohexyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-ethyl-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-fluoro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-hydroxy-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-methyl-1-phenyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-N-methyl-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)propane-1-sulfonothioamide
-
4'-(trifluoromethyl)biphenyl-4-yl sulfamate
-
-
4-((((2R)-2-ammonio-2-carboxyethyl)sulfanyl)(diphenyl)-methyl)pyridinium tetrafluoroborate
-
-
4-((2R,4aS,5R,10bS)-2-((methylamino)methyl)-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
-
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)-2-fluorophenol
-
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzene-1,2-diol
-
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
-
4-((4aS,5S,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)butan-1-ol
-
4-(2-[1-(2,4,6-trifluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
-
4-(2-[1-(2,4-difluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
-
4-(2-[1-(2,6-difluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
-
4-(2-[1-(2-fluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
-
4-(2-[1-(4-chlorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
-
4-(2-[1-(4-fluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
treatmebnt of cells results in inhibition of proliferation and induction of caspase 3 activity with EC50 values of 0.0017 and 0.0011 mM, respectively. Compound induces monoastral spindles in A2780 cells when incubated at concentrations above that required to induce a full mitotic arrest
4-(benzenesulfonyl)-1-chloro-2-nitrobenzene
-
4-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)butan-1-one
-
4-chloro-1-(4-methoxybenzene-1-sulfinyl)-2-nitrobenzene
-
4-chloro-1-[(4-chlorophenyl)methanesulfonyl]-2-nitrobenzene
-
4-chloro-1-[(4-methoxyphenyl)methanesulfonyl]-2-nitrobenzene
-
4-chloro-1-[(4-methylphenyl)methanesulfonyl]-2-nitrobenzene
-
4-chloro-2-nitro-1-phenoxybenzene
-
4-[2-(1-phenylcyclopropyl)-1,3-thiazol-4-yl]pyridine 1-oxide
-
4-[[3-(methoxycarbonyl)-2-methyl-5a,9a-dihydronaphtho[1,2-b]furan-5-yl]sulfamoyl]benzoic acid
-
-
5-(2-(3-aminopropanoyl)-6-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)benzo[d]oxazol-2(3H)-one
-
5-(2-fluorophenyl)-2,9-dimethyl-5,6-dihydropyrazolo[1,5-c]quinazoline
-
-
5-[2-(1-phenylcyclopropyl)-1,3-thiazol-4-yl]pyridine-2-carbonitrile
-
6-(4-chloro-2-nitrobenzene-1-sulfonyl)-1,4-dihydronaphthalene
-
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
-
-
actin
AK065586
inhibition in the presence of microtubles
adenosine 5'-[beta,gamma-imido]triphosphate
-
nonhydrolyzable analogue of ATP, blocks enzyme by rapid replacement of ATP
adenylylimidodiphosphate
-
AMP-PNP
AMP-PNP
-
binding structure
BTB-1
BTB-1 inhibits both of the microtubule-based Kif18A activities. Allosteric BTB-1-binding site near loop5, where it blocks the ATP-dependent conformational changes
Calmodulin
-
activated calmodulin inhibits KCBP interaction with microtubules thereby abolishing its motor- and microtubules-dependent ATPase activity
ethyl 3-acetyl-4-[3-(acetyloxy)phenyl]-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
no inhibition in vitro, inhibitory in cell-based assay
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
i.e. monastrol
ethyl 4-[3-(acetyloxy)phenyl]-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
no inhibition in vitro, inhibitory in cell-based assay
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
-
-
ispinesib
-
SB-715992, a potent and selective inhibitor of kinesin spindle protein
kinesin spindle protein activator-1
-
inhibits kinesin spindle protein ATP turnover in the presence of microtubules
-
N-(((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)-4-(dimethylamino)butanamide
-
N-(((2R,4aS,5R,10bS)-9-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)-2-(dimethylamino)ethanesulfonamide
-
N-(2-((((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)amino)ethyl)acetamide
-
N-(2-aminoethyl)-4-methyl-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)benzamide
-
N-(3-(2-(3-aminopropanoyl)-6-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)phenyl)methanesulfonamide
-
N-(3-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-oxopropyl)methanesulfonamide
-
N-(3-aminopropyl)-N-[(1R)-1-(3-benzyl-7-chloro-4-oxo-3,4-dihydroquinazolin-2-yl)-2-methylpropyl]-3-fluoro-4-methylbenzamide
-
-
N-(4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenyl)acetamide
-
N-(4-fluorophenyl)-2-[1-(4-fluorophenyl)-3-[2-(3-methylthiophen-2-yl)ethyl]-5-oxo-2-thioxoimidazolidin-4-yl]acetamide
-
-
N-(4-methoxyphenyl)-2-[3-[2-(3-methylthiophen-2-yl)ethyl]-5-oxo-1-phenyl-2-thioxoimidazolidin-4-yl]acetamide
-
-
N-[3-amino-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
-
-
N-[3-chloro-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
-
-
N-[3-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
-
-
N-[3-methoxy-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
-
-
N-[4'-(trifluoromethyl)biphenyl-4-yl]methanesulfonamide
-
-
N-[4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
-
-
N1-phenyl-N1-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)ethane-1,2-diamine
-
PVZB1194
allosteric inhibitor, biphenyl-type inhibitor, binding structure of the inhibitor in complex with the Eg5 motor domain: inhibitor PVZB1194 binds to the alpha4/alpha6 allosteric pocket 15 A from the ATP-binding pocket, which differs from conventional allosteric inhibitors that bind to the allosteric L5/alpha2/alpha 3 pocket of Eg5. Binding of the inhibitor is involved in the neck-linker conformation and also causes conformational changes around the ATP-binding pocket through Tyr104 to affect the interaction of ATP with the pocket. Folding rearrangement of enzyme Eg5 induced by PVZB1194 in the absence of nucleotides and microtubules. Residue Tyr104 is involved in ATP-competitive inhibition by PVZB1194
monastrol
-
0.2 mM, 25% inhibition. Compared to vertebrate Eg5, Eh Klp5 is less sensitive to monastrol
monastrol
-
model for dimeric Eg5 in which monastrol stabilizes a conformation with the neck linker of each motor domain locked onto its catalytic core, resulting in dissociation of the MT. Eg5 complex or an inhibition of MT binding
monastrol
-
suppresses the directional processive motility of microtubule-bound Eg5
S-trityl-L-cysteine
-
tight binding inhibitor, specific for kinesin Eg5. Inhibits Eg5-driven microtubule sliding velocity in a reversible fashion with a IC50 of 500 nM. The S and D-enantiomers of tritylcysteine are nearly equally potent. No inhibition of KIF2A/Kif2 (kinesin-13 family), KIF2C/MCAK (kinesin-13 family), KIF5B/HsuKHC (kinsin-1 family), KIF19/HsCENP-E (kinesin-7 family), KIF20A/HsRabK6 (kinsin-6 family), KIF22A/HsKid (kinesin-10 family), KIF23/HsMKLP1 (kinesin-6 family), KIFC1/HsKIFC1 (kinesin-14 family)
V5+
-
-
additional information
-
synthetic peptides derived from the tail of kinesin inhibit the protein's ATPase and motor activities. A peptide that spans residues 904-933 exhibits the strongest inhibitory effect on steady-state motility and ATPase activity, reflecting diminished binding of the ADP-bound kinesin head to the microtubule. Tail-mediated inhibition of kinesin activity is mainly the product of allosteric inhibition induced by the intramolecular binding of kinesin tail domain to the motor domain
-
additional information
study of the discovery and optimization of hexahydro-2H-pyranol[3,2-c]quinolines, HHPQs, as inhibitors. Crystallographic data demonstrate that these potent and selectve inhibitors bind in an allosteric pocket of kinesin-5 distant from the nucleotide and microtubule binding sites; the activity assay for inhibition analysis are performed with a coupled ATP regeneration system with a total concentration of the kinesin-5 protein of approximately 50 nM in the reaction
-
additional information
-
study of the discovery and optimization of hexahydro-2H-pyranol[3,2-c]quinolines, HHPQs, as inhibitors. Crystallographic data demonstrate that these potent and selectve inhibitors bind in an allosteric pocket of kinesin-5 distant from the nucleotide and microtubule binding sites; the activity assay for inhibition analysis are performed with a coupled ATP regeneration system with a total concentration of the kinesin-5 protein of approximately 50 nM in the reaction
-
additional information
development of small molecule inhibitors of the enzyme Kif11 ATPase activity
-
additional information
identification of optimized small molecule inhibitors of the mitotic kinesin Kif18A, usage of BTB-1 as a lead compound, structure-activity relationship studies and inhibition mechanism of BTB-1 and its analogues, overview
-
additional information
-
identification of optimized small molecule inhibitors of the mitotic kinesin Kif18A, usage of BTB-1 as a lead compound, structure-activity relationship studies and inhibition mechanism of BTB-1 and its analogues, overview
-
additional information
kinesin performs autoinhibition, addition of a negative charge at Ser175 favors the autoinhibited conformation of kinesin
-
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0.00002
((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methanamine
Homo sapiens
pH and temperature not specified in the publication
0.0009
(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)(1-methylpiperidin-3-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.0081
(2R)-2-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-methylbutan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000138
(2R)-2-amino-3-((1,1,2-triphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002518
(2R)-2-amino-3-((1,1-bis(4-chlorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001782
(2R)-2-amino-3-((1,1-bis(4-fluorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001065
(2R)-2-amino-3-((1,1-bis(4-methylphenyl)-2-phenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002168
(2R)-2-amino-3-((1-(2-fluorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001912
(2R)-2-amino-3-((1-(3,4-dichlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001289
(2R)-2-amino-3-((1-(3-chlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0005675
(2R)-2-amino-3-((1-(3-chlorophenyl)-1-(4-chlorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0000676
(2R)-2-amino-3-((1-(3-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0000586
(2R)-2-amino-3-((1-(4-chlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001505
(2R)-2-amino-3-((1-(4-fluorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001594
(2R)-2-amino-3-((1-(4-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001676
(2R)-2-amino-3-((1-(4-methylphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.005278
(2R)-2-amino-3-((2-(3,4-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002375
(2R)-2-amino-3-((2-(3-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0004558
(2R)-2-amino-3-((2-(4-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.01584
(2R)-2-amino-3-[(1,1,3-triphenylpropyl)sulfanyl]propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000006
(2R,4aS,5R,10bS)-2-((1H-1,2,4-triazol-1-yl)methyl)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00076
(2S)-2-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-methylbutan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.01
(4aS,10bS)-9-(tert-butyl)-5-(3-chlorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00087
(4aS,10bS)-9-(tert-butyl)-5-(3-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.0003
(4aS,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline-9-carbonitrile
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline-9-carboxylic acid
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.0037
(4aS,5R,10bS)-5-phenyl-9-(trifluoromethoxy)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00011
(4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00036
(4aS,5R,10bS)-5-phenyl-9-propyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-7,9-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00009
(4aS,5R,10bS)-7-fluoro-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-8,10-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00125
(4aS,5R,10bS)-8,9-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-8-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00054
(4aS,5R,10bS)-8-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00091
(4aS,5R,10bS)-9-(pentafluoro-lambda6-sulfanyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-9-(tert-butyl)-5-(1H-imidazol-2-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00017
(4aS,5R,10bS)-9-(tert-butyl)-5-(2-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.0068
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-chlorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-fluoro-4-methoxyphenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00035
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00027
(4aS,5R,10bS)-9-(tert-butyl)-5-(4-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.0011
(4aS,5R,10bS)-9-(tert-butyl)-5-(pyridin-3-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00053
(4aS,5R,10bS)-9-(tert-butyl)-5-(thiazol-2-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00012
(4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00072
(4aS,5R,10bS)-9-chloro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00013
(4aS,5R,10bS)-9-ethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00013
(4aS,5R,10bS)-9-isopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00042
(4aS,5R,10bS)-9-methyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.0053
(4aS,5R,10bS)-N,N-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-amine
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5S,10bS)-9-(tert-butyl)-5-cyclohexyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.000058
1-((2R,4aS,5R,10bS)-5-(4-fluorophenyl)-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
Homo sapiens
pH and temperature not specified in the publication
0.000004
1-((2R,4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
Homo sapiens
pH and temperature not specified in the publication
0.000003
1-((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
Homo sapiens
pH and temperature not specified in the publication
0.000011
1-((2R,4aS,5R,10bS)-9-cyclopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
Homo sapiens
pH and temperature not specified in the publication
0.0025
1-(1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
Homo sapiens
i.e. tetrahydro-beta-carboline, pH and temperature not specified in the publication
0.0001
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-(piperidin-1-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
Homo sapiens
pH and temperature not specified in the publication
0.00046
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000008
1-(2-(dimethylamino)ethyl)-3-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)urea
Homo sapiens
i.e. EMD 534085, pH and temperature not specified in the publication
0.00001
1-(3-hydroxypropyl)-3-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)urea
Homo sapiens
pH and temperature not specified in the publication
0.000054
1-(4'-tert-butylbiphenyl-4-yl)urea
Homo sapiens
-
-
0.000058
1-(4'-[(trifluoromethyl)sulfonyl]biphenyl-4-yl)urea
Homo sapiens
-
-
0.01
1-(4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenyl)ethanone
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00086
1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-2-(piperidin-4-yl)ethanone
Homo sapiens
pH and temperature not specified in the publication
0.0102
1-(benzenesulfonyl)-2,4-dinitrobenzene
Homo sapiens
pH and temperature not specified in the publication
0.0103
1-(benzenesulfonyl)-2-nitro-4-(trifluoromethyl)benzene
Homo sapiens
pH and temperature not specified in the publication
0.003
1-(benzenesulfonyl)-2-nitrobenzene
Homo sapiens
pH and temperature not specified in the publication
0.0017
1-(benzenesulfonyl)-4-chloro-2-nitrobenzene
Homo sapiens
pH and temperature not specified in the publication
0.0048
1-(benzenesulfonyl)-4-fluoro-2-nitrobenzene
Homo sapiens
pH and temperature not specified in the publication
0.00152
1-phenethylamino-3-phenothiazin-10-yl-propan-2-ol
Homo sapiens
-
pH 6.8, 30°C
0.000015
1-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]urea
Homo sapiens
-
-
0.000028
1-[3'-nitro-4'-(trifluoromethyl)biphenyl-4-yl]urea
Homo sapiens
-
-
0.000015
1-[3-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]urea
Homo sapiens
-
-
0.000057
1-[4'-(propan-2-yl)biphenyl-4-yl]urea
Homo sapiens
-
-
0.000011
1-[4'-(trifluoromethyl)biphenyl-4-yl]thiourea
Homo sapiens
-
-
0.000039
1-[4'-(trifluoromethyl)biphenyl-4-yl]urea
Homo sapiens
-
-
0.000031
1-[4-(1,3-benzodioxol-5-yl)phenyl]urea
Homo sapiens
-
-
0.000067
1-[4-(2,2,3,3-tetrafluoro-2,3-dihydro-1,4-benzodioxin-6-yl)phenyl]urea
Homo sapiens
-
-
0.000019
2-((((2R,4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)(ethyl)amino)ethanol
Homo sapiens
pH and temperature not specified in the publication
0.000007
2-((((2R,4aS,5R,10bS)-9-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)amino)ethanol
Homo sapiens
pH and temperature not specified in the publication
0.0006845
2-((1,1,2-triphenylethyl)sulfanyl)ethanaminium tetrafluoroborate
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0004037
2-((1,1-bis(4-chlororophenyl)-2-phenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0005878
2-((1,1-bis(4-fluorophenyl)-2-phenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000261
2-((1,1-bis(4-methylphenyl)-2-phenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0007895
2-((1-(2-fluorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002293
2-((1-(3,4-dichlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000519
2-((1-(3-chlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanaminium tetrafluoroborate
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0004367
2-((1-(3-chlorophenyl)-1-(4-chlorophenyl)-2-phenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002561
2-((1-(3-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001409
2-((1-(4-chlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0005779
2-((1-(4-fluorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0006656
2-((1-(4-hydroxylphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001719
2-((1-(4-methylphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000005
2-((2R,4aS,5R,10bS)-9-(tert-butyl)-2-((methylamino)methyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
Homo sapiens
pH and temperature not specified in the publication
0.0005
2-((4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-yl)acetonitrile
Homo sapiens
pH and temperature not specified in the publication
0.01
2-((4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-yl)ethanol
Homo sapiens
pH and temperature not specified in the publication
0.0003
2-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)-4-chlorobenzenethiol
Homo sapiens
pH and temperature not specified in the publication
0.000025
2-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
Homo sapiens
pH and temperature not specified in the publication
0.0009422
2-((diphenyl(pyridin-4-yl)methyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0415
2-(2,4-difluorophenyl)-9-(3,4-dimethylphenyl)-8-oxo-8,9-dihydro-7H-purine-6-carboxamide
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.004 - 0.0055
2-(2-sulfanylethoxy)ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
0.0064
2-(4-chloro-2-nitrobenzene-1-sulfonyl)thiophene
Homo sapiens
pH and temperature not specified in the publication
0.000014
2-(dimethylamino)ethyl (((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)carbamate
Homo sapiens
pH and temperature not specified in the publication
0.000004
2-(methylamino)-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)ethanesulfonothioamide
Homo sapiens
pH and temperature not specified in the publication
0.0002412
2-(tritylthio)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000049
2-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
Homo sapiens
pH and temperature not specified in the publication
0.001
2-[1-(4-methoxyphenyl)-5-oxo-3-[2-(thiophen-2-yl)ethyl]-2-thioxoimidazolidin-4-yl]-N-phenylacetamide
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.0045 - 0.0115
2-[2-(acetylsulfanyl)ethoxy]ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
0.0023
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)aniline
Homo sapiens
pH and temperature not specified in the publication
0.00012
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
Homo sapiens
pH and temperature not specified in the publication
0.00004
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
Homo sapiens
pH and temperature not specified in the publication
0.000186
3-(2-((2-aminoethyl)sulfonyl)-6-chloro-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)phenol
Homo sapiens
pH and temperature not specified in the publication
0.000002
3-(dimethylamino)-N-(((2R,4aS,5R,10bS)-9-isopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)propane-1-sulfonamide
Homo sapiens
pH and temperature not specified in the publication
0.0066
3-amino-1-(1-(2-aminopyridin-4-yl)-6-chloro-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0001
3-amino-1-(1-(3-fluorophenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00063
3-amino-1-(1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
3-amino-1-(1-(3-hydroxyphenyl)-6-(trifluoromethoxy)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.025
3-amino-1-(1-(3-hydroxyphenyl)-6-isopropyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
above 0.025 mM, pH and temperature not specified in the publication
0.00002 - 0.000058
3-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
0.0017
3-amino-1-(1-(3-hydroxyphenyl)-6-phenyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.011
3-amino-1-(1-(3-methoxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000027
3-amino-1-(6-bromo-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000039
3-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00023
3-amino-1-(6-chloro-1-cyclohexyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000011
3-amino-1-(6-ethyl-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00076
3-amino-1-(6-fluoro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0045
3-amino-1-(6-hydroxy-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000175
3-amino-1-(6-methyl-1-phenyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000007
3-amino-N-methyl-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)propane-1-sulfonothioamide
Homo sapiens
pH and temperature not specified in the publication
0.000064
4'-(trifluoromethyl)biphenyl-4-yl sulfamate
Homo sapiens
-
-
0.0005142
4-((((2R)-2-ammonio-2-carboxyethyl)sulfanyl)(diphenyl)-methyl)pyridinium tetrafluoroborate
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000004
4-((2R,4aS,5R,10bS)-2-((methylamino)methyl)-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
Homo sapiens
pH and temperature not specified in the publication
0.000017
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)-2-fluorophenol
Homo sapiens
pH and temperature not specified in the publication
0.000095
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzene-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000034
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
Homo sapiens
pH and temperature not specified in the publication
0.01
4-((4aS,5S,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)butan-1-ol
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00023
4-(2-[1-(2,4,6-trifluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
-
0.00033
4-(2-[1-(2,4-difluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
-
0.00028
4-(2-[1-(2,6-difluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
-
0.0003
4-(2-[1-(2-fluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
-
0.00029
4-(2-[1-(4-chlorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
-
0.00054
4-(2-[1-(4-fluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
pH 6.8, 22°C
0.000086
4-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)butan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00047
4-[2-(1-phenylcyclopropyl)-1,3-thiazol-4-yl]pyridine 1-oxide
Homo sapiens
-
0.0791
4-[[3-(methoxycarbonyl)-2-methyl-5a,9a-dihydronaphtho[1,2-b]furan-5-yl]sulfamoyl]benzoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.025
5-(2-(3-aminopropanoyl)-6-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)benzo[d]oxazol-2(3H)-one
Homo sapiens
above 0.025 mM, pH and temperature not specified in the publication
0.0063
5-(2-fluorophenyl)-2,9-dimethyl-5,6-dihydropyrazolo[1,5-c]quinazoline
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.000532
5-[2-(1-phenylcyclopropyl)-1,3-thiazol-4-yl]pyridine-2-carbonitrile
Homo sapiens
-
0.00000045 - 0.000036
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
0.00000023 - 0.0000003
docetaxel
0.0625
ethyl 3-acetyl-4-[3-(acetyloxy)phenyl]-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
cell-based assay on monoastral spindles
0.0061 - 0.0513
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
0.05
ethyl 4-[3-(acetyloxy)phenyl]-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
cell-based assay on monoastral spindles
0.0015 - 0.0092
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
0.0023
kinesin spindle protein activator-1
Homo sapiens
-
-
-
0.000005
N-(((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)-4-(dimethylamino)butanamide
Homo sapiens
pH and temperature not specified in the publication
0.000002
N-(((2R,4aS,5R,10bS)-9-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)-2-(dimethylamino)ethanesulfonamide
Homo sapiens
pH and temperature not specified in the publication
0.000006
N-(2-((((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)amino)ethyl)acetamide
Homo sapiens
pH and temperature not specified in the publication
0.000065
N-(2-aminoethyl)-4-methyl-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.025
N-(3-(2-(3-aminopropanoyl)-6-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)phenyl)methanesulfonamide
Homo sapiens
above 0.025 mM, pH and temperature not specified in the publication
0.000155
N-(3-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-oxopropyl)methanesulfonamide
Homo sapiens
pH and temperature not specified in the publication
0.01
N-(4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenyl)acetamide
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.0006
N-(4-fluorophenyl)-2-[1-(4-fluorophenyl)-3-[2-(3-methylthiophen-2-yl)ethyl]-5-oxo-2-thioxoimidazolidin-4-yl]acetamide
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.0024
N-(4-methoxyphenyl)-2-[3-[2-(3-methylthiophen-2-yl)ethyl]-5-oxo-1-phenyl-2-thioxoimidazolidin-4-yl]acetamide
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.000024
N-[3-amino-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
Homo sapiens
-
-
0.000067
N-[3-chloro-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
Homo sapiens
-
-
0.000005
N-[3-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
Homo sapiens
-
-
0.000066
N-[3-methoxy-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
Homo sapiens
-
-
0.000018
N-[4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
Homo sapiens
-
-
0.000019
N1-phenyl-N1-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0001859 - 0.0005
S-trityl-L-cysteine
0.00000046 - 0.000903
SB-731489
0.004
2-(2-sulfanylethoxy)ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of basal ATPase activity
0.0055
2-(2-sulfanylethoxy)ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of microtubule-stimulated ATPase activity
0.0045
2-[2-(acetylsulfanyl)ethoxy]ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of basal ATPase activity
0.0115
2-[2-(acetylsulfanyl)ethoxy]ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of microtubule-stimulated ATPase activity
0.00002
3-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000058
3-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000045
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
Homo sapiens
-
mutant D130V, pH 6.8
0.000036
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
Homo sapiens
-
wild-type, pH 6.8
0.00000023
docetaxel
Homo sapiens
-
mutant D130V, pH 6.8
0.0000003
docetaxel
Homo sapiens
-
wild-type, pH 6.8
0.0061
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of basal ATPase activity
0.0123
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of microtubule-stimulated ATPase activity
0.0513
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
cell-based assay on monoastral spindles
0.0015
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
Homo sapiens
-
22°C, inhibition of basal ATPase activity
0.003
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
Homo sapiens
-
22°C, inhibition of microtubule-stimulated ATPase activity
0.0092
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
Homo sapiens
-
cell-based assay on monoastral spindles
0.0001859
S-trityl-L-cysteine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0005
S-trityl-L-cysteine
Homo sapiens
-
tight binding inhibitor, specific for kinesin Eg5. Inhibits Eg5-driven microtubule sliding velocity in a reversible fashion with a IC50 of 500 nM. The S and D-enantiomers of tritylcysteine are nearly equally potent. No inhibition of KIF2A/Kif2 (kinesin-13
0.00000046
SB-731489
Homo sapiens
-
wild-type, pH 6.8
0.000903
SB-731489
Homo sapiens
-
mutant D130V, pH 6.8
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