Direct long-term observation of kinesin processivity at low load

Current Biology

Volumn 12, Issue 4, 2002, Pages 301-306

  Yajima, Junichiro ^a   Alonso, Maria C ^b   Cross, Robert A ^b   Toyoshima, Yoko Y ^a,c  

^a UNIVERSITY OF TOKYO   (Japan)

^b MARIE CURIE RESEARCH INSTITUTE   (United Kingdom)

^c +81 3 5454 6752 ^*  (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GELSOLIN; GREEN FLUORESCENT PROTEIN; KINESIN; MOLECULAR MOTOR; PHOTOPROTEIN;

ANIMAL; ARTICLE; BIOLOGICAL MODEL; KINETICS; METABOLISM; MICROTUBULE; RAT; TIME;

ACTINS; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; GELSOLIN; GREEN FLUORESCENT PROTEINS; KINESIN; KINETICS; LUMINESCENT PROTEINS; MICROTUBULES; MODELS, BIOLOGICAL; MOLECULAR MOTOR PROTEINS; RATS; TIME FACTORS;

EID: 0037133038     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(01)00683-2     Document Type: Article

References (36)

1. Movement of microtubules by single kinesin molecules
2. Direct observation of single kinesin molecules moving along microtubules
3. Direct observation of kinesin stepping by optical trapping interferometry
4. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
5. Single kinesin molecules studied with a molecular force clamp
6. The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain
7. The way things move: Looking under the hood of molecular motor proteins
8. The conformational cycle of kinesin
9. Force production by single kinesin motors
10. Conformational changes during kinesin motility
11. Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
12. Interacting head mechanism of microtubule-kinesin ATPase
13. Alternating site mechanism of the kinesin ATPase
14. Coupled chemical and mechanical reaction steps in a processive Neurospora kinesin
15. Kinesin hydrolyses one ATP per 8-nm step
16. Coupling of kinesin steps to ATP hydrolysis
17. Kinesin takes one 8-nm step for each ATP that it hydrolyzes
18. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
19. Direct inhibition of microtubule-based kinesin motility by local anesthetics
20. Role of the kinesin neck region in processive microtubule-based motility
21. Autofluorescent proteins in single-molecule research: Applications to live cell imaging microscopy
22. Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking
23. The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation
24. Single-fluorophore imaging with an unmodified epifluorescence microscope and conventional video camera
25. Processivity of the motor protein kinesin requires two heads
26. Weak and strong states of kinesin and ncd
27. Equilibrium studies of kinesin-nucleotide intermediates
28. Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains
29. Assaying processive movement of kinesin by fluorescence microscopy
30. Kinesin follows the microtubule's protofilament axis
31. ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy
32. Properties of the depolymerization products of microtubules from mammalian brain
33. Preparation of modified tubulins
34. The regulation of rabbit skeletal muscle contraction. 1. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
35. 1-ATPase
36. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay