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Molecular motors: thermodynamics and the random walk
scientific article
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Statements
instance of
scholarly article
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review article
1 reference
stated in
Europe PubMed Central
title
Molecular motors: thermodynamics and the random walk
(English)
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main subject
molecular motor
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thermodynamics
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author name string
N Thomas
series ordinal
1
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Y Imafuku
series ordinal
2
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K Tawada
series ordinal
3
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language of work or name
English
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publication date
22 October 2001
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published in
Proceedings of the Royal Society B
1 reference
stated in
PubMed
volume
268
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issue
1481
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page(s)
2113-22
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cites work
Myosin-V is a processive actin-based motor
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PubMed Central
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The way things move: looking under the hood of molecular motor proteins
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A structural change in the kinesin motor protein that drives motility
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Kinesin and dynein superfamily proteins and the mechanism of organelle transport
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The ATP synthase--a splendid molecular machine
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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
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A myosin family tree.
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Myosin-V stepping kinetics: a molecular model for processivity
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Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains.
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Kinesin hydrolyses one ATP per 8-nm step
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Direct observation of single kinesin molecules moving along microtubules
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Direct observation of kinesin stepping by optical trapping interferometry
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Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
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29 September 2017
Mechanism of adenosine triphosphate hydrolysis by actomyosin
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29 September 2017
Bead movement by single kinesin molecules studied with optical tweezers
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29 September 2017
Protein motors and Maxwell's demons: does mechanochemical transduction involve a thermal ratchet?
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Coupling of kinesin steps to ATP hydrolysis.
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2 June 2018
Catalytic mechanism of F1-ATPase
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2 June 2018
Movement of microtubules by single kinesin molecules
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PubMed Central
reference URL
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Force production by single kinesin motors.
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27 November 2018
Two-headed binding of a processive myosin to F-actin.
1 reference
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PubMed Central
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27 November 2018
Kinesin takes one 8-nm step for each ATP that it hydrolyzes.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1088855
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27 November 2018
A kinesin family tree
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/11600075
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/11600075
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1098/RSPB.2001.1764
0 references
Fatcat ID
release_yzckaujjhjcjphsirnj7qheqie
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PMCID
1088855
0 references
PubMed ID
11600075
0 references
ResearchGate publication ID
11750459
0 references
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