An ATP Gate Controls Tubulin Binding by the Tethered Head of Kinesin-1
Open accessAbstract
Kinesin-1 is a two-headed molecular motor that walks along microtubules, with each step gated by adenosine triphosphate (ATP) binding. Existing models for the gating mechanism propose a role for the microtubule lattice. We show that unpolymerized tubulin binds to kinesin-1, causing tubulin-activated release of adenosine diphosphate (ADP). With no added nucleotide, each kinesin-1 dimer binds one tubulin heterodimer. In adenylyl-imidodiphosphate (AMP-PNP), a nonhydrolyzable ATP analog, each kinesin-1 dimer binds two tubulin heterodimers. The data reveal an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of a steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Kinesin dimers labeled with fluorescent ADP analog release one ADP upon microtubule binding, and release of second requires ATP.
“It has long been known39 that kinesin dimers labeled with a fluorescent ADP analog will release just one ADP molecule upon binding the microtubule, while release of the second ADP requires the further addition of ATP39,40.”
From A universal pathway for kinesin stepping (2011) · cites this paper as [40]
The passage discussing Fig. 3 reports that fluorescent mantADP is released from one kinesin head on binding unpolymerised tubulin, with release from the second head requiring an ATP or AMPPNP chase. It also describes the same two-stage ADP-release pattern on microtubule binding, but does not say that the microtubule result used fluorescently labeled ADP. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe data do not support models in which both kinesin heads bind the microtubule until ATP binding triggers release of the rear head, nor models in which one head is parked against the forward face of its microtubule-bound partner in the waiting state.
“Our data do not support models where both kinesin heads bind to the MT until ATP binding triggers release of the rear head4,8, nor where one head is parked against the forward face of its MT-bound partner in the waiting state10.”
From Direct observation of the binding state of the kinesin head to the microtubule (2009) · cites this paper as [10]
WT kinesin usually adopts a configuration with one head strongly bound to the microtubule and the other ADP-bearing head largely detached, especially at low ATP.
“This conformational state is partially suppressed in WT kinesin, which tends to adopt a configuration where just one head is strongly attached to the microtubule39,40, while the partner head, carrying ADP, is more-or-less free of the microtubule34–36, particularly at low ATP concentrations.”
From A universal pathway for kinesin stepping (2011) · cites this paper as [40]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Yildiz, A., Tomishige, M., Vale, R. D., & Selvin, P. R. (2004) · Science · doi:10.1126/science.1093753 · Cited by 965 · see citing works
Movement of microtubules by single kinesin molecules
Howard, J., Hudspeth, A. J., & Vale, R. D. (1989) · Nature · doi:10.1038/342154a0 · Cited by 885 · see citing works
A structural change in the kinesin motor protein that drives motility
Rice, S., Lin, A. W., Safer, D., Hart, C. L., Naber, N., Carragher, B. O., Cain, S. M., Pechatnikova, E., Wilson-Kubalek, E. M., Whittaker, M., et al. (1999) · Nature · doi:10.1038/45483 · Cited by 798 · see citing works
Carter, N. J., & Cross, R. A. (2005) · Nature · doi:10.1038/nature03528 · Cited by 743 · see citing works
Self-citationKinesin Moves by an Asymmetric Hand-Over-Hand Mechanism
Asbury, C. L., Fehr, A. N., & Block, S. M. (2003) · Science · doi:10.1126/science.1092985 · Cited by 511 · see citing works
Coupling of kinesin steps to ATP hydrolysis
Hua, W., Young, E. C., Fleming, M. L., & Gelles, J. (1997) · Nature · doi:10.1038/41118 · Cited by 358 · see citing works
Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis.
Hackney, D. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.6865 · Cited by 351 · see citing works
Chemomechanical coupling of the forward and backward steps of single kinesin molecules
Nishiyama, M., Higuchi, H., & Yanagida, T. (2002) · Nature Cell Biology · doi:10.1038/ncb857 · Cited by 327 · see citing works
The kinetic mechanism of kinesin.
Cross, R. (2004) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2004.04.010 · Cited by 204 · see citing works
Self-citationRosenfeld, S. S., Fordyce, P. M., Jefferson, G. M., King, P. H., & Block, S. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300849200 · Cited by 188 · see citing works
Interacting Head Mechanism of Microtubule-Kinesin ATPase
Ma, Y.-Z., & Taylor, E. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.2.724 · Cited by 181 · see citing works
Alternate fast and slow stepping of a heterodimeric kinesin molecule
Kaseda, K., Higuchi, H., & Hirose, K. (2003) · Nature Cell Biology · doi:10.1038/ncb1067 · Cited by 179 · see citing works
Alternating Site Mechanism of the Kinesin ATPase
Gilbert, S. P., Moyer, M. L., & Johnson, K. A. (1998) · Biochemistry · doi:10.1021/bi971117b · Cited by 172 · see citing works
Role of the kinesin neck linker and catalytic core in microtubule-based motility
Case, R. B., Rice, S. E., Hart, C. L., Ly, B., & Vale, R. D. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00316-x · Cited by 160 · see citing works
Controlling Kinesin by Reversible Disulfide Cross-Linking
Tomishige, M., & Vale, R. D. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.5.1081 · Cited by 141 · see citing works
Thermodynamic properties of the kinesin neck-region docking to the catalytic core.
Rice, S. E., Cui, Y., Sindelar, C., Naber, N., Matuska, M., Vale, R., & Cooke, R. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74992-3 · Cited by 140 · see citing works
Backsteps induced by nucleotide analogs suggest the front head of kinesin is gated by strain
Guydosh, N. R., & Block, S. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600931103 · Cited by 132 · see citing works
Asenjo, A., Weinberg, Y., & Sosa, H. (2006) · Nature Structural &Molecular Biology · doi:10.1038/nsmb1109 · Cited by 90 · see citing works
Kinesin: walking, crawling or sliding along?
YILDIZ, A., & Selvin, P. R. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.12.007 · Cited by 86 · see citing works
ATP Reorients the Neck Linker of Kinesin in Two Sequential Steps
Rosenfeld, S. S., Jefferson, G. M., & King, P. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103899200 · Cited by 84 · see citing works
Hirose, K., Löwe, J., Alonso, M. C., Cross, R. A., & Amos, L. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.6.2063 · Cited by 79 · see citing works
Self-citationCoupled chemical and mechanical reaction steps in a processive Neurospora kinesin
Crevel, I., Carter, N., Schliwa, M., & Cross, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5863 · Cited by 70 · see citing works
Self-citationCarter, N. J., & Cross, R. A. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.12.009 · Cited by 52 · see citing works
Self-citationHackney, D. D. (2002) · Biochemistry · doi:10.1021/bi0159229 · Cited by 46 · see citing works
The conformational cycle of kinesin
Cross, R. A., Crevel, I., Carter, N. J., Alonso, M. C., Hirose, K., & Amos, L. A. (2000) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.2000.0587 · Cited by 39 · see citing works
Self-citationKinesin’s Biased Stepping Mechanism: Amplification of Neck Linker Zippering
Mather, W., & Fox, R. F. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.087049 · Cited by 31 · see citing works
Feedback of the Kinesin-1 Neck-linker Position on the Catalytic Site
Hahlen, K., Ebbing, B., Reinders, J., Mergler, J., Sickmann, A., & Woehlke, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m508019200 · Cited by 30 · see citing works
ESR reveals the mobility of the neck linker in dimeric kinesin
Sugata, K., Nakamura, M., Ueki, S., Fajer, P. G., & Arata, T. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.12.093 · Cited by 20 · see citing works
Kinesin-8s: motoring and depolymerizing
Walczak, C. (2006) · Nature Cell Biology · doi:10.1038/ncb0906-903 · Cited by 6 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [5]Yildiz A Tomishige M Vale RD Selvin PR Science 2004 303 676 14684828
Cited by
Sorted by citations
Intramolecular Strain Coordinates Kinesin Stepping Behavior along Microtubules
Yildiz, A., Tomishige, M., Gennerich, A., & Vale, R. D. (2008) · Cell · doi:10.1016/j.cell.2008.07.018 · Cited by 313 · see citing works
Walking the walk: how kinesin and dynein coordinate their steps
Gennerich, A., & Vale, R. D. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.12.002 · Cited by 301 · see citing works
Finding the weakest link – exploring integrin-mediated mechanical molecular pathways
Roca‐Cusachs, P., Iskratsch, T., & Sheetz, M. P. (2012) · Journal of Cell Science · doi:10.1242/jcs.095794 · Cited by 258 · see citing works
A universal pathway for kinesin stepping
Clancy, B. E., Behnke-Parks, W. M., Andreasson, J. O. L., Rosenfeld, S. S., & Block, S. M. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2104 · Cited by 202 · see citing works
Molecular machines working on surfaces and at interfaces.
Balzani, V., Credi, A., & Venturi, M. (2008) · ChemPhysChem · doi:10.1002/cphc.200700528 · Cited by 167 · see citing works
Prime movers: the mechanochemistry of mitotic kinesins
Cross, R. A., & McAinsh, A. D. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3768 · Cited by 190 · see citing works
Self-citationHow kinesin waits between steps
Mori, T., Vale, R. D., & Tomishige, M. (2007) · Nature · doi:10.1038/nature06346 · Cited by 171 · see citing works
Structure of a kinesin–tubulin complex and implications for kinesin motility
Gigant, B., Wang, W., Dreier, B., Jiang, Q., Pecqueur, L., Plückthun, A., Wang, C.-G., & Knossow, M. (2013) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.2624 · Cited by 167 · see citing works
Direct observation of intermediate states during the stepping motion of kinesin-1
Isojima, H., Iino, R., Niitani, Y., Noji, H., & Tomishige, M. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2028 · Cited by 141 · see citing works
One-step purification of assembly-competent tubulin from diverse eukaryotic sources
Widlund, P. O., Podolski, M., Reber, S., Alper, J., Storch, M., Hyman, A. A., Howard, J., & Drechsel, D. N. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-06-0444 · Cited by 141 · see citing works
Kinetochore kinesin CENP-E is a processive bi-directional tracker of dynamic microtubule tips
Гудимчук, Н. Б., Vitre, B., Kim, Y., Kiyatkin, A. B., Cleveland, D. W., Ataullakhanov, F. I., & Grishchuk, E. L. (2013) · Nature Cell Biology · doi:10.1038/ncb2831 · Cited by 139 · see citing works
Braun, M., Drummond, D. R., Cross, R. A., & McAinsh, A. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1878 · Cited by 120 · see citing works
Self-citationThe mechanisms of kinesin motor motility: lessons from the monomeric motor KIF1A
Hirokawa, N., Nitta, R., & Okada, Y. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2807 · Cited by 127 · see citing works
Direct observation of the binding state of the kinesin head to the microtubule
Guydosh, N. R., & Block, S. M. (2009) · Nature · doi:10.1038/nature08259 · Cited by 121 · see citing works
Kinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle
Mickolajczyk, K. J., Deffenbaugh, N. C., Arroyo, J. O., Andrecka, J., Kukura, P., & Hancock, W. O. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517638112 · Cited by 120 · see citing works
The Mechanism of Tubulin Assembly into Microtubules: Insights from Structural Studies
Knossow, M., Campanacci, V., Khodja, L. A., & Gigant, B. (2020) · iScience · doi:10.1016/j.isci.2020.101511 · Cited by 117 · see citing works
Kinesin expands and stabilizes the GDP-microtubule lattice
Peet, D. R., Burroughs, N. J., & Cross, R. A. (2018) · Nature Nanotechnology · doi:10.1038/s41565-018-0084-4 · Cited by 106 · see citing works
Self-citationChang, X., Zhou, S., Liu, J., Wang, Y., Guan, X., Wu, Q., Zhang, Q., Liu, Z., & Liu, R. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117371 · Cited by 101 · see citing works
Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin
Nitta, R., Okada, Y., & Hirokawa, N. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1487 · Cited by 100 · see citing works
Toprak, E., Yildiz, A., Hoffman, M. T., Rosenfeld, S. S., & Selvin, P. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808396106 · Cited by 94 · see citing works
Morikawa, M., Yajima, H., Nitta, R., Inoué, S., Ogura, T., Sato, C., & Hirokawa, N. (2015) · The EMBO Journal · doi:10.15252/embj.201490588 · Cited by 91 · see citing works
The Kinesin-1 Chemomechanical Cycle: Stepping Toward a Consensus
Hancock, W. O. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.02.025 · Cited by 92 · see citing works
Review: Mechanochemistry of the kinesin‐1 ATPase
Cross, R. A. (2016) · Biopolymers · doi:10.1002/bip.22862 · Cited by 74 · see citing works
Self-citationThe kinesin‐13 MCAK has an unconventional ATPase cycle adapted for microtubule depolymerization
Friel, C. T., & Howard, J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.290 · Cited by 87 · see citing works
Design, Synthesis, and Operation of Small Molecules That Walk along Tracks
von Delius, M., Geertsema, E. M., Leigh, D. A., & Tang, D. D. (2010) · Journal of the American Chemical Society · doi:10.1021/ja106486b · Cited by 84 · see citing works
Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin
Wang, W., Cantos-Fernandes, S., Lv, Y., Kuerban, H., Ahmad, S., Wang, C., & Gigant, B. (2017) · Nature Communications · doi:10.1038/s41467-017-00091-9 · Cited by 83 · see citing works
A Tubulin Binding Switch Underlies Kip3/Kinesin-8 Depolymerase Activity
Arellano-Santoyo, H., Geyer, E. A., Stokasimov, E., Chen, G.-Y., Su, X., Hancock, W. O., Rice, L. M., & Pellman, D. S. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.06.011 · Cited by 72 · see citing works
A mobile kinesin-head intermediate during the ATP-waiting state
Asenjo, A. B., & Sosa, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808355106 · Cited by 64 · see citing works
Electrostatically biased binding of kinesin to microtubules
Grant, B. J., M. Gheorghe, D., Zheng, W., Alonso, M., Huber, G., Dlugosz, M., McCammon, J. A., & Cross, R. A. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001207 · Cited by 67 · see citing works
Self-citationThe role of microtubules in processive kinesin movement
Kikkawa, M. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.01.002 · Cited by 66 · see citing works
Insight into the molecular mechanism of the multitasking kinesin‐8 motor
Peters, C., Brejc, K., Belmont, L. D., Bodey, A. J., Lee, Y., Yu, M., Guo, J., Sakowicz, R., Hartman, J. J., & Moores, C. A. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.220 · Cited by 65 · see citing works
Closed Mechanoelectrochemical Cycles of Individual Single‐Chain Macromolecular Motors by AFM
Shi, W., Giannotti, M. I., Zhang, X., Hempenius, M. A., Schönherr, H., & Vancso, G. J. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200702387 · Cited by 60 · see citing works
Podolski, M., Mahamdeh, M., & Howard, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.584300 · Cited by 58 · see citing works
Kinesin Processivity Is Determined by a Kinetic Race from a Vulnerable One-Head-Bound State
Mickolajczyk, K. J., & Hancock, W. O. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.05.007 · Cited by 52 · see citing works
Kinesin’s backsteps under mechanical load
Hyeon, C., Klumpp, S., & Onuchic, J. N. (2009) · Physical Chemistry Chemical Physics · doi:10.1039/b903536b · Cited by 51 · see citing works
Strain through the neck linker ensures processive runs: a DNA‐kinesin hybrid nanomachine study
Miyazono, Y., Hayashi, M., Karagiannis, P., Harada, Y., & Tadakuma, H. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.319 · Cited by 51 · see citing works
S. pombe Kinesins-8 Promote Both Nucleation and Catastrophe of Microtubules
Erent, M., Drummond, D. R., & Cross, R. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030738 · Cited by 47 · see citing works
Self-citationMechanism of Processive Movement of Monomeric and Dimeric Kinesin Molecules
Xie, P. (2010) · International Journal of Biological Sciences · doi:10.7150/ijbs.6.665 · Cited by 46 · see citing works
Kinesin motility is driven by subdomain dynamics
Hwang, W., Lang, M. J., & Karplus, M. (2017) · eLife · doi:10.7554/elife.28948 · Cited by 43 · see citing works
A model of processive movement of dimeric kinesin
Guo, S., Wang, P., & Xie, P. (2016) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2016.11.023 · Cited by 45 · see citing works
Operation modes of the molecular motor kinesin
Liepelt, S., & Lipowsky, R. (2009) · Physical Review E · doi:10.1103/physreve.79.011917 · Cited by 44 · see citing works
Kinesin Walks the Line: Single Motors Observed by Atomic Force Microscopy
Schaap, I. A. T., Carrasco, C., de Pablo, P. J., & Schmidt, C. F. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.04.015 · Cited by 42 · see citing works
Kinesin's step dissected with single-motor FRET
Verbrugge, S., Lánský, Z., & Peterman, E. J. G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905177106 · Cited by 40 · see citing works
Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines
Cochran, J. C. (2015) · Biophysical Reviews · doi:10.1007/s12551-014-0150-6 · Cited by 38 · see citing works
The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5
Muretta, J. M., Jun, Y., Gross, S. P., Major, J. A., Thomas, D. D., & Rosenfeld, S. S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512305112 · Cited by 37 · see citing works
Backstepping Mechanism of Kinesin-1
Toleikis, A., Carter, N. J., & Cross, R. A. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.09.034 · Cited by 44 · see citing works
Self-citationGutiérrez-Medina, B., Fehr, A. N., & Block, S. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907133106 · Cited by 37 · see citing works
Structural Basis for the ATP-Induced Isomerization of Kinesin
Chang, Q., Nitta, R., Inoué, S., & Hirokawa, N. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.03.004 · Cited by 37 · see citing works
Wang, W., Jiang, Q., Argentini, M., Cornu, D., Gigant, B., Knossow, M., & Wang, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.317859 · Cited by 34 · see citing works
Hotta, T., Fujita, S., Uchimura, S., Noguchi, M., Demura, T., Muto, E., & Hashimoto, T. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.01173 · Cited by 34 · see citing works
Microtubule Regulation in Plants: From Morphological Development to Stress Adaptation
Hsiao, A., & Huang, J.-Y. (2023) · Biomolecules · doi:10.3390/biom13040627 · Cited by 34 · see citing works
A Structural Perspective on the Dynamics of Kinesin Motors
Hyeon, C., & Onuchic, J. N. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.10.037 · Cited by 32 · see citing works
Pressure-Induced Changes in the Structure and Function of the Kinesin-Microtubule Complex
Nishiyama, M., Kimura, Y., Nishiyama, Y., & Terazima, M. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.10.023 · Cited by 34 · see citing works
Shi, X., Guo, S., Wang, P., Chen, H., & Xie, P. (2019) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25833 · Cited by 32 · see citing works
Kinesin Steps Do Not Alternate in Size
Fehr, A. N., Asbury, C. L., & Block, S. M. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.126839 · Cited by 31 · see citing works
Insight into the chemomechanical coupling mechanism of kinesin molecular motors
Xie, P. (2021) · Communications in Theoretical Physics · doi:10.1088/1572-9494/abecd8 · Cited by 30 · see citing works
Processivity of dimeric kinesin‐1 molecular motors
Guo, S., Shi, X., Wang, P., & Xie, P. (2018) · FEBS Open Bio · doi:10.1002/2211-5463.12486 · Cited by 29 · see citing works
Hackney, D. D. (2007) · Science · doi:10.1126/science.1141549 · Cited by 29 · see citing works
Sugata, K., Song, L., Nakamura, M., Ueki, S., Fajer, P. G., & Arata, T. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.079 · Cited by 28 · see citing works
Modeling Motility of the Kinesin Dimer from Molecular Properties of Individual Monomers†
Fan, D., Zheng, W., Hou, R., Li, F., & Wang, Z. (2008) · Biochemistry · doi:10.1021/bi800072p · Cited by 26 · see citing works
Single‐headed mode of kinesin‐5
Kaseda, K., Crevel, I. M.-T. C., Hirose, K., & Cross, R. A. (2008) · EMBO Reports · doi:10.1038/embor.2008.96 · Cited by 26 · see citing works
Self-citationStepping behavior of two-headed kinesin motors
Xie, P. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.040 · Cited by 24 · see citing works
Design principles governing chemomechanical coupling of kinesin
Sumi, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-01328-9 · Cited by 24 · see citing works
These motors were made for walking
Hunter, B., & Allingham, J. S. (2020) · Protein Science · doi:10.1002/pro.3895 · Cited by 21 · see citing works
ATP-Concentration- and Force-Dependent Chemomechanical Coupling of Kinesin Molecular Motors
Xie, P., Guo, S., & Chen, H. (2018) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00577 · Cited by 20 · see citing works
Xie, P., Guo, S., & Chen, H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194911 · Cited by 19 · see citing works
The Efficiency of Molecular Motors
Zhang, Y. (2009) · Journal of Statistical Physics · doi:10.1007/s10955-009-9695-3 · Cited by 19 · see citing works
Processive cytoskeletal motors studied with single‐molecule fluorescence techniques
Belyy, V., & Yıldız, A. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.05.040 · Cited by 19 · see citing works
Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin
Guan, R., Zhang, L., Su, Q. P., Mickolajczyk, K. J., Chen, G.-Y., Hancock, W. O., Sun, Y., Zhao, Y., & Chen, Z. (2017) · Nature Communications · doi:10.1038/ncomms14951 · Cited by 17 · see citing works
Wang, G., Gao, X., Huang, Y., Yao, Z., Shi, Q., & Wu, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100396 · Cited by 18 · see citing works
Three phase model of the processive motor protein kinesin
Zhang, Y. (2008) · Biophysical Chemistry · doi:10.1016/j.bpc.2008.04.002 · Cited by 17 · see citing works
The efficiency of the molecular motorsPreprint
Zhang, Y. (2009) · Cited by 21 · see citing works
Verbrugge, S., Lechner, B., Woehlke, G., & Peterman, E. J. G. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.02.073 · Cited by 16 · see citing works
Energetics of kinesin‐1 stepping mechanism
Kawaguchi, K. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.10.019 · Cited by 15 · see citing works
Are Coiled-Coils of Dimeric Kinesins Unwound during Their Walking on Microtubule?
Duan, Z.-W., Xie, P., Li, W., & Wang, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036071 · Cited by 14 · see citing works
A cool look at the structural changes in kinesin motor domains
Amos, L., & Hirose, K. (2007) · Journal of Cell Science · doi:10.1242/jcs.016931 · Cited by 14 · see citing works
Self-citationSubunits interactions in kinesin motors
Skowronek, K., Kocik, E., & Kasprzak, A. A. (2007) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2007.05.008 · Cited by 12 · see citing works
Dissection of Kinesin's Processivity
Adio, S., Jaud, J., Ebbing, B., Rief, M., & Woehlke, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004612 · Cited by 11 · see citing works
Li, Y., Zhu, S., Zhang, X., Liu, Y.-C., Xue, F., Zhao, L., & Sun, J. (2017) · BMC Biotechnology · doi:10.1186/s12896-017-0373-2 · Cited by 11 · see citing works
Impact of Slip Cycles on the Operation Modes and Efficiency of Molecular Motors
Liepelt, S., & Lipowsky, R. (2010) · Journal of Statistical Physics · doi:10.1007/s10955-010-0050-5 · Cited by 11 · see citing works
A common chemomechanical coupling model for orphan and conventional kinesin molecular motors.
Guo, S.-K., & Xie, P. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106427 · Cited by 8 · see citing works
Closed Mechanoelectrochemical Cycles of Individual Single‐Chain Macromolecular Motors by AFM
Shi, W., Giannotti, M. I., Zhang, X., Hempenius, M. A., Schönherr, H., & Vancso, G. J. (2007) · Angewandte Chemie · doi:10.1002/ange.200702387 · Cited by 10 · see citing works
Zheng, Y.-P., Tian, S., Peng, X.-L., Yang, J., Fu, Y.-H., Jiao, Y.-Y., Zhao, J., He, J., & Hong, T. (2016) · FEBS Letters · doi:10.1002/1873-3468.12137 · Cited by 9 · see citing works
Properties of the Kinesin‐3 NcKin3 motor domain and implications for neck function
Adio, S., & Woehlke, G. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07083.x · Cited by 7 · see citing works
Characterization of kinesin-like proteins in silkworm posterior silkgland cells
Wang, Q., Teng, J., Shen, B., Zhang, W., Guo, Y., Su, X., Zhang, C., Yu, A. C., & Chen, J. (2010) · Cell Research · doi:10.1038/cr.2010.47 · Cited by 7 · see citing works
Kinesin-Recruiting Microtubules Exhibit Collective Gliding Motion while Forming Motor Trails
Tsitkov, S., Song, Y., Rodriguez, J. B., Zhang, Y., & Hess, H. (2020) · ACS Nano · doi:10.1021/acsnano.0c03263 · Cited by 7 · see citing works
Amos, L., & Löwe, J. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-53047-5 · Cited by 7 · see citing works
Self-citationXie, P. (2025) · Biomolecules · doi:10.3390/biom15101453 · Cited by 6 · see citing works
Kramers-type elastic ratchet model for ATP gating during kinesin’s mechanochemical cycle
Wang, H.-Y., & Bao, J.-D. (2009) · Physica A Statistical Mechanics and its Applications · doi:10.1016/j.physa.2009.09.036 · Cited by 6 · see citing works
4.17 Kinesin Structure and Biochemistry
Gilbert, S. P., & Sardar, H. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374920-8.00421-5 · Cited by 6 · see citing works
Engineering Heterodimeric Kinesins through Genetic Incorporation of Noncanonical Amino Acids
Popchock, A. R., Jana, S., Mehl, R. A., & Qiu, W. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00399 · Cited by 6 · see citing works
Ökten, Z., & Schliwa, M. (2007) · Nature · doi:10.1038/450625a · Cited by 6 · see citing works
Shi, X., Liu, Y., & Xie, P. (2025) · Biomolecules · doi:10.3390/biom15050717 · Cited by 5 · see citing works
Ti, S.-C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.861648 · Cited by 4 · see citing works
Tether-scanning the kinesin motor domain reveals a core mechanical action
Sumiyoshi, R., Yamagishi, M., Furuta, A., Nishizaka, T., Furuta, K., Cross, R. A., & Yajima, J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2403739121 · Cited by 4 · see citing works
Self-citationWalking motion of an overdamped active particle in a ratchet potential
Lee, K.-J.-B., Kim, C. K., & Chung, M.-H. (2011) · Journal of Biological Physics · doi:10.1007/s10867-011-9249-1 · Cited by 4 · see citing works
Credi, A. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374396-1.00133-1 · Cited by 3 · see citing works
Kinesin's walk: Springy or gated head coordination?
Wilson, R. J. (2008) · Biosystems · doi:10.1016/j.biosystems.2008.12.002 · Cited by 3 · see citing works
Single molecule fluorescence spectroscopy for quantitative biological applications
Liu, R., Li, Y., & Liu, L. (2016) · Quantitative Biology · doi:10.1007/s40484-016-0083-0 · Cited by 3 · see citing works
- Authors
- Alonso, M. C., Drummond, D. R., Kain, S., Hoeng, J., Amos, L., & Cross, R. A.
- Affiliations
- Molecular Motors Group, Marie Curie Research Institute, The Chart, Oxted, Surrey RH8 0TL, UK.
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Cross, Robert A.
- Venue
- Science
- Published
- 2007-04-06
- Volume
- 316
- Issue
- 5821
- Pages
- 120-123
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2504013
- OpenAlex
- W2048354751
- Semantic Scholar
- 4023a802b290ff0886cd38b395a77277a3a9c487
- Cited by
- 120
- References
- 29
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 1 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 6 · 2019: 3 · 2018: 5 · 2017: 8 · 2016: 8 · 2015: 4 · 2014: 3 · 2013: 4 · 2012: 8
- FWCI
- 7.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- kinesin-1, tubulin binding, ADP release, microtubule lattice, AMP-PNP, allosteric regulation, microtubule motor proteins
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphate, Adenylyl Imidodiphosphate, Animals, Binding Sites, Microtubules, Models, Biological, Neurospora, Protein Conformation, Recombinant Fusion Proteins, Schizosaccharomyces, Tubulin, Kinesins, Dimerization, Molecular Motor Proteins, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
