Literature DB >> 2530455

Movement of microtubules by single kinesin molecules.

J Howard1, A J Hudspeth, R D Vale.   

Abstract

Kinesin is a motor protein that uses energy derived from ATP hydrolysis to move organelles along microtubules. Using a new technique for measuring the movement produced in vitro by individual kinesin molecules, it is shown that a single kinesin molecule can move a microtubule for several micrometers. New information about the mechanism of force generation by kinesin is presented.

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Year:  1989        PMID: 2530455     DOI: 10.1038/342154a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  237 in total

1.  Processive movement of single 22S dynein molecules occurs only at low ATP concentrations.

Authors:  E Hirakawa; H Higuchi; Y Y Toyoshima
Journal:  Proc Natl Acad Sci U S A       Date:  2000-03-14       Impact factor: 11.205

2.  Direct inhibition of microtubule-based kinesin motility by local anesthetics.

Authors:  Y Miyamoto; E Muto; T Mashimo; A H Iwane; I Yoshiya; T Yanagida
Journal:  Biophys J       Date:  2000-02       Impact factor: 4.033

Review 3.  The conformational cycle of kinesin.

Authors:  R A Cross; I Crevel; N J Carter; M C Alonso; K Hirose; L A Amos
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-04-29       Impact factor: 6.237

4.  Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin.

Authors:  Y Okada; N Hirokawa
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-18       Impact factor: 11.205

5.  Kinetic equilibrium of forces and molecular events in muscle contraction.

Authors:  E W Becker
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-04       Impact factor: 11.205

6.  Theoretical formalism for kinesin motility I. Bead movement powered by single one-headed kinesins.

Authors:  Y d Chen
Journal:  Biophys J       Date:  2000-01       Impact factor: 4.033

7.  Lethal kinesin mutations reveal amino acids important for ATPase activation and structural coupling.

Authors:  K M Brendza; D J Rose; S P Gilbert; W M Saxton
Journal:  J Biol Chem       Date:  1999-10-29       Impact factor: 5.157

8.  Characterization of single actomyosin rigor bonds: load dependence of lifetime and mechanical properties.

Authors:  T Nishizaka; R Seo; H Tadakuma; K Kinosita; S Ishiwata
Journal:  Biophys J       Date:  2000-08       Impact factor: 4.033

9.  Controlling the direction of kinesin-driven microtubule movements along microlithographic tracks.

Authors:  Y Hiratsuka; T Tada; K Oiwa; T Kanayama; T Q Uyeda
Journal:  Biophys J       Date:  2001-09       Impact factor: 4.033

10.  Protein-protein ratchets: stochastic simulation and application to processive enzymes.

Authors:  C J Brokaw
Journal:  Biophys J       Date:  2001-09       Impact factor: 4.033

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