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Literature DB >> 17325011

Kinesin motor mechanics: binding, stepping, tracking, gating, and limping.

Steven M Block¹.

Abstract

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Year: 2007 PMID： 17325011 PMCID： PMC1852353 DOI： 10.1529/biophysj.106.100677

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

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60 in total

1. Alternate fast and slow stepping of a heterodimeric kinesin molecule.

Authors: Kuniyoshi Kaseda; Hideo Higuchi; Keiko Hirose
Journal: Nat Cell Biol Date: 2003-11-23 Impact factor: 28.824

2. Chemomechanical coupling of the forward and backward steps of single kinesin molecules.

Authors: Masayoshi Nishiyama; Hideo Higuchi; Toshio Yanagida
Journal: Nat Cell Biol Date: 2002-10 Impact factor: 28.824

3. Loading direction regulates the affinity of ADP for kinesin.

Authors: Sotaro Uemura; Shin'ichi Ishiwata
Journal: Nat Struct Biol Date: 2003-04

4. The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends.

Authors: Jonne Helenius; Gary Brouhard; Yannis Kalaidzidis; Stefan Diez; Jonathon Howard
Journal: Nature Date: 2006-05-04 Impact factor: 49.962

5. Bead movement by single kinesin molecules studied with optical tweezers.

Authors: S M Block; L S Goldstein; B J Schnapp
Journal: Nature Date: 1990-11-22 Impact factor: 49.962

6. One-dimensional diffusion of microtubules bound to flagellar dynein.

Authors: R D Vale; D R Soll; I R Gibbons
Journal: Cell Date: 1989-12-01 Impact factor: 41.582

Review 7. On the hand-over-hand footsteps of kinesin heads.

Authors: R A Cross
Journal: J Muscle Res Cell Motil Date: 1995-04 Impact factor: 2.698

8. Direct observation of kinesin stepping by optical trapping interferometry.

Authors: K Svoboda; C F Schmidt; B J Schnapp; S M Block
Journal: Nature Date: 1993-10-21 Impact factor: 49.962

9. Processivity of the motor protein kinesin requires two heads.

Authors: W O Hancock; J Howard
Journal: J Cell Biol Date: 1998-03-23 Impact factor: 10.539

10. Kinesin takes one 8-nm step for each ATP that it hydrolyzes.

Authors: D L Coy; M Wagenbach; J Howard
Journal: J Biol Chem Date: 1999-02-05 Impact factor: 5.157

106 in total

1. A structural perspective on the dynamics of kinesin motors.

Authors: Changbong Hyeon; José N Onuchic
Journal: Biophys J Date: 2011-12-07 Impact factor: 4.033

Review 2. Artificial Molecular Machines.

Authors: Sundus Erbas-Cakmak; David A Leigh; Charlie T McTernan; Alina L Nussbaumer
Journal: Chem Rev Date: 2015-09-08 Impact factor: 60.622

Kinesin motor mechanics: binding, stepping, tracking, gating, and limping.

1. Alternate fast and slow stepping of a heterodimeric kinesin molecule.

2. Chemomechanical coupling of the forward and backward steps of single kinesin molecules.

3. Loading direction regulates the affinity of ADP for kinesin.

4. The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends.

5. Bead movement by single kinesin molecules studied with optical tweezers.

6. One-dimensional diffusion of microtubules bound to flagellar dynein.

Review 7. On the hand-over-hand footsteps of kinesin heads.

8. Direct observation of kinesin stepping by optical trapping interferometry.

9. Processivity of the motor protein kinesin requires two heads.

10. Kinesin takes one 8-nm step for each ATP that it hydrolyzes.

1. A structural perspective on the dynamics of kinesin motors.

Review 2. Artificial Molecular Machines.

3. Kinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle.

Review 4. To step or not to step? How biochemistry and mechanics influence processivity in Kinesin and Eg5.

Review 5. Single-molecule biophysics: at the interface of biology, physics and chemistry.

6. Mechanical control of the directional stepping dynamics of the kinesin motor.

Review 7. Cargo transport: molecular motors navigate a complex cytoskeleton.

8. Kinesin's cover-neck bundle folds forward to generate force.

9. Pressure-induced changes in the structure and function of the kinesin-microtubule complex.

Review 10. Modeling stochastic kinetics of molecular machines at multiple levels: from molecules to modules.