about
KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry.Rotary DNA motorsMechanistic analysis of the mitotic kinesin Eg5.Monastrol inhibition of the mitotic kinesin Eg5.Crystal structure of the kinesin motor domain reveals a structural similarity to myosinAn atomic-level mechanism for activation of the kinesin molecular motors.Pathway of ATP hydrolysis by monomeric kinesin Eg5ATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrolSwitches, latches, and amplifiers: common themes of G proteins and molecular motorsPhosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa.Family-specific Kinesin Structures Reveal Neck-linker Length Based on Initiation of the Coiled-coil.Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains.Antitumor activity of an allosteric inhibitor of centromere-associated protein-E.Kinesin-2 KIF3AB exhibits novel ATPase characteristicsKinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular MachinesFluorescent taxoids as probes of the microtubule cytoskeleton.Pressure-induced changes in the structure and function of the kinesin-microtubule complex.Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.The role of thermal activation in motion and force generation by molecular motors.Orphan kinesin NOD lacks motile properties but does possess a microtubule-stimulated ATPase activityDNA helicase-mediated packaging of adeno-associated virus type 2 genomes into preformed capsidsFluctuation in the microtubule sliding movement driven by kinesin in vitro.Structural intermediates in the assembly of taxoid-induced microtubules and GDP-tubulin double rings: time-resolved X-ray scattering.Motor protein mechanics: a stochastic model with minimal mechanochemical coupling.The shapes of the motor domains of two oppositely directed microtubule motors, ncd and kinesin: a neutron scattering study.Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin.Kinetic and equilibrium analysis of the myosin ATPase.Gamma-diketone axonopathy: analyses of cytoskeletal motors and highways in CNS myelinated axonsNucleotide-dependent movements of the kinesin motor domain predicted by simulated annealing.Direct tests of muscle cross-bridge theories: predictions of a Brownian dumbbell model for position-dependent cross-bridge lifetimes and step sizes with an optically trapped actin filament.A chemically reversible Brownian motor: application to kinesin and Ncd.Kinetics processivity and the direction of motion of Ncd.Revealingly odd couplesKinesin hydrolyses one ATP per 8-nm step.Backsteps induced by nucleotide analogs suggest the front head of kinesin is gated by strainProbing the kinesin reaction cycle with a 2D optical force clampMicrotubule-kinesin interface mutants reveal a site critical for communication.A kinesin mutation that uncouples motor domains and desensitizes the gamma-phosphate sensorKinesin Kar3Cik1 ATPase pathway for microtubule cross-linking.
P2860
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P2860
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Pathway of processive ATP hydrolysis by kinesin.
@ast
Pathway of processive ATP hydrolysis by kinesin.
@en
type
label
Pathway of processive ATP hydrolysis by kinesin.
@ast
Pathway of processive ATP hydrolysis by kinesin.
@en
prefLabel
Pathway of processive ATP hydrolysis by kinesin.
@ast
Pathway of processive ATP hydrolysis by kinesin.
@en
P2093
P2860
P356
P1433
P1476
Pathway of processive ATP hydrolysis by kinesin
@en
P2093
P2860
P2888
P304
P356
10.1038/373671A0
P407
P577
1995-02-01T00:00:00Z
P5875
P6179
1020580541