Cited by 177Microtubule and mitosis dynamicsProtein Structure and DynamicsForce Microscopy Techniques and Applications

The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.

Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains

Hackney, David D.·1995·Nature

Open this paper in CoChat — free account

Abstract

Studies of immobilized kinesin have shown that a single dimeric molecule can maintain contact with and drive sliding of a microtubule. In solution, however, native kinesin binds microtubules too weakly and hydrolyses ATP too slowly to produce the high sliding velocities seen in motility assay. This apparent inhibition in solution appears to be caused by the binding of kinesin's tail domains to its motor (head) domains in a folded conformation. DKH392, a construct containing two heads but no tails, has been shown to display both tight binding to microtubules and high ATPase rates. Furthermore, it retains one molecule of ADP per dimer when bound to microtubules, which could facilitate a 'hand-over-hand' mechanism for processive motion. Here we show that DKH392 hydrolyses more than 100 ATP molecules per diffusional encounter with a microtubule, even in the high-salt conditions encountered physiologically. This provides direct evidence that kinesin's activity is highly processive, with the motor remaining attached to a microtubule through many cycles of ATP hydrolysis.

Integrity signals

Registry

Crossref · 10.1038/377448a0

Cites

13 of 13 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993
Direct observation of kinesin stepping by optical trapping interferometry
Svoboda, K., Schmidt, C. F., Schnapp, B. J., & Block, S. M. (1993) · Nature · doi:10.1038/365721a0 · Cited by 1,910
Bead movement by single kinesin molecules studied with optical tweezers
Block, S. M., Goldstein, L. S. B., & Schnapp, B. J. (1990) · Nature · doi:10.1038/348348a0 · Cited by 1,038
Movement of microtubules by single kinesin molecules
Howard, J., Hudspeth, A. J., & Vale, R. D. (1989) · Nature · doi:10.1038/342154a0 · Cited by 885
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
Self-citation
Pathway of processive ATP hydrolysis by kinesin
Gilbert, S. P., Webb, M. R., Brune, M., & Johnson, K. A. (1995) · Nature · doi:10.1038/373671a0 · Cited by 252
Kinesin ATPase: rate-limiting ADP release
Hackney, D. D. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.17.6314 · Cited by 239
Self-citation
Kinesin undergoes a 9 S to 6 S conformational transition
Hackney, D. D., Levitt, J. D., & Suhan, J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42499-4 · Cited by 175
Self-citation
Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization
Huang, T. G., & Hackney, D. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34033-4 · Cited by 174
Self-citation
Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli.
Huang, T. G., Suhan, J. P., & Hackney, D. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34034-6 · Cited by 90
Self-citation

Flagged first, then by citations

Show all 13 references

Research works printed but not linked: 2

Hackney, D. D. Biophys. J. 68, s267–s270 (1995).
Hackney, D. D. & Nagy, J. M. Biophys. J. 68, a286 (1995).

Sorted by citations

Artificial Molecular Machines
Erbaş-Çakmak, S., Leigh, D. A., McTernan, C. T., & Nussbaumer, A. L. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00146 · Cited by 2,016
Molecular motors
Schliwa, M., & Woehlke, G. (2003) · Nature · doi:10.1038/nature01601 · Cited by 1,089
Kinesin hydrolyses one ATP per 8-nm step
Schnitzer, M. J., & Block, S. M. (1997) · Nature · doi:10.1038/41111 · Cited by 771
Direct observation of single kinesin molecules moving along microtubules
Vale, R. D., Funatsu, T., Pierce, D. W., Romberg, L., Harada, Y., & Yanagida, T. (1996) · Nature · doi:10.1038/380451a0 · Cited by 711
Force production by single kinesin motors
Schnitzer, M. J., Visscher, K., & Block, S. M. (2000) · Nature Cell Biology · doi:10.1038/35036345 · Cited by 572
Intracellular Transport and Kinesin Superfamily Proteins, KIFs: Structure, Function, and Dynamics
Hirokawa, N., & Noda, Y. (2008) · Physiological Reviews · doi:10.1152/physrev.00023.2007 · Cited by 528
Molecular motors: structural adaptations to cellular functions
Howard, J. (1997) · Nature · doi:10.1038/39247 · Cited by 489
A Processive Single-Headed Motor: Kinesin Superfamily Protein KIF1A
Okada, Y., & Hirokawa, N. (1999) · Science · doi:10.1126/science.283.5405.1152 · Cited by 468
The design plan of kinesin motors
Vale, R. D., & Fletterick, R. J. (1997) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.13.1.745 · Cited by 474
The Kinesin-Related Protein MCAK Is a Microtubule Depolymerase that Forms an ATP-Hydrolyzing Complex at Microtubule Ends
Hunter, A. W., Caplow, M., Coy, D. L., Hancock, W. O., Diez, S., Wordeman, L. G., & Howard, J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00049-2 · Cited by 398
The Directional Preference of Kinesin Motors Is Specified by an Element outside of the Motor Catalytic Domain
Case, R. B., Pierce, D. W., Hom-Booher, N., Hart, C. L., & Vale, R. D. (1997) · Cell · doi:10.1016/s0092-8674(00)80360-8 · Cited by 354
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
Processivity of the Motor Protein Kinesin Requires Two Heads
Hancock, W. O., & Howard, J. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.6.1395 · Cited by 299
Engineering the Processive Run Length of the Kinesin Motor
Thorn, K. S., Ubersax, J. A., & Vale, R. D. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.5.1093 · Cited by 279
Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules
Verhey, K. J., Lizotte, D. L., Abramson, T., Barenboim, L., Schnapp, B. J., & Rapoport, T. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.1053 · Cited by 266
“This value agrees with the apparent binding constant for MTs based on activation of the ATPase activity of purified dimeric kinesin constructs ( Hackney, 1994, 1995; Rosenfeld et al., 1996; Jiang et al., 1997).”
Background
Switches, latches, and amplifiers: common themes of G proteins and molecular motors.
Vale, R. D. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.2.291 · Cited by 259
Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro
Valentine, M. T., Fordyce, P. M., Krzysiak, T. C., Gilbert, S. P., & Block, S. M. (2006) · Nature Cell Biology · doi:10.1038/ncb1394 · Cited by 260
Walking molecules
von Delius, M., & Leigh, D. A. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15005g · Cited by 256
Kinesin’s processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains
Hancock, W. O., & Howard, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13147 · Cited by 243
Kinetic Mechanism and Regulation of Myosin VI
De La Cruz, E. M., Ostap, E. M., & Sweeney, H. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104136200 · Cited by 234
The kinetic mechanism of kinesin
Cross, R. A. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.04.010 · Cited by 225
Transport of ER vesicles on actin filaments in neurons by myosin V
Tabb, J. S., Molyneaux, B. J., Cohen, D. L., Kuznetsov, S. A., & Langford, G. M. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3221 · Cited by 204
Kinesin’s IAK tail domain inhibits initial microtubule-stimulated ADP release
Hackney, D. D., & Stock, M. F. (2000) · Nature Cell Biology · doi:10.1038/35010525 · Cited by 198
Self-citation
Distinguishing Inchworm and Hand-Over-Hand Processive Kinesin Movement by Neck Rotation Measurements
Hua, W., Chung, J., & Gelles, J. (2002) · Science · doi:10.1126/science.1063089 · Cited by 194
Examining kinesin processivity within a general gating framework
Andreasson, J. O. L., Milic, B., Chen, G.-Y., Guydosh, N. R., Hancock, W. O., & Block, S. M. (2015) · eLife · doi:10.7554/elife.07403 · Cited by 199
Higher plant myosin XI moves processively on actin with 35 nm steps at high velocity
Tominaga, M., Kojima, H., Yokota, E., Orii, H., Nakamori, R., Katayama, E., Anson, M., Shimmen, T., & Oiwa, K. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg130 · Cited by 187
Transport of Beads by Several Kinesin Motors
Beeg, J., Klumpp, S., Dimova, R., Gracià, R. S., Unger, E., & Lipowsky, R. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.097881 · Cited by 178
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
Models of Motor-Assisted Transport of Intracellular Particles
Smith, D. A., & Simmons, R. M. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75994-2 · Cited by 173
The C-Terminus of Tubulin Increases Cytoplasmic Dynein and Kinesin Processivity
Wang, Z., & Sheetz, M. P. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76743-9 · Cited by 166
Role of the Kinesin Neck Region in Processive Microtubule-based Motility
Romberg, L., Pierce, D. W., & Vale, R. D. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.6.1407 · Cited by 155
A Kinesin-like Motor Inhibits Microtubule Dynamic Instability
Bringmann, H., Skiniotis, G., Spilker, A. C., Kandels-Lewis, S. E., Vernos, I., & Surrey, T. (2004) · Science · doi:10.1126/science.1094838 · Cited by 152
Substeps within the 8-nm step of the ATPase cycle of single kinesin molecules
Nishiyama, M., Muto, E., Inoue, Y., Yanagida, T., & Higuchi, H. (2001) · Nature Cell Biology · doi:10.1038/35070116 · Cited by 142
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 142
The Role of the Dynactin Complex in Intracellular Motility
Holleran, E. A., Karki, S., & Holzbaur, E. L. F. (1998) · International review of cytology · doi:10.1016/s0074-7696(08)62168-3 · Cited by 144
Detection of fractional steps in cargo movement by the collective operation of kinesin-1 motors
Leduc, C., Ruhnow, F., Howard, J., & Diez, S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701864104 · Cited by 135
Cytoplasmic streaming in Drosophila oocytes varies with kinesin activity and correlates with the microtubule cytoskeleton architecture
Ganguly, S., Williams, L. S., Palacios, I. M., & Goldstein, R. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203575109 · Cited by 126
Three-dimensional cryoelectron microscopy of dimeric kinesin and ncd motor domains on microtubules.
Hirose, K., Lockhart, A., Cross, R. A., & Amos, L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9539 · Cited by 131
Towards the application of cytoskeletal motor proteins in molecular detection and diagnostic devices
Korten, T., Månsson, A., & Diez, S. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.05.001 · Cited by 131
Organelle transport along microtubules — the role of KIFs
Hirokawa, N. (1996) · Trends in Cell Biology · doi:10.1016/0962-8924(96)10003-9 · Cited by 131
The 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 133
Autoinhibition of a Neuronal Kinesin UNC-104/KIF1A Regulates the Size and Density of Synapses
Niwa, S., Lipton, D. M., Morikawa, M., Zhao, C. L., Hirokawa, N., Lu, H., & Shen, K. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.043 · Cited by 128
Disease-associated mutations hyperactivate KIF1A motility and anterograde axonal transport of synaptic vesicle precursors
Chiba, K., Takahashi, H., Chen, M., Obinata, H., Arai, S., Hashimoto, K., Oda, T., McKenney, R. J., & Niwa, S. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1905690116 · Cited by 133
Detection of sub-8-nm movements of kinesin by high-resolution optical-trap microscopy.
Coppin, C. M., Finer, J. T., Spudich, J. A., & Vale, R. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.5.1913 · Cited by 121
Molecular Machines
Mavroidis, C., Dubey, A., & Yarmush, M. L. (2004) · Annual Review of Biomedical Engineering · doi:10.1146/annurev.bioeng.6.040803.140143 · Cited by 120
Dynamic Concentration of Motors in Microtubule Arrays
Nédélec, F., Surrey, T., & Maggs, A. C. (2001) · Physical Review Letters · doi:10.1103/physrevlett.86.3192 · Cited by 115
Kinetic Characterization of a Monomeric Unconventional Myosin V Construct
Trybus, K. M., Krementsova, E. B., & Freyzon, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27448 · Cited by 112
Engineering Cooperativity in Biomotor-Protein Assemblies
Diehl, M. R., Zhang, K., Lee, H. J., & Tirrell, D. A. (2006) · Science · doi:10.1126/science.1122125 · Cited by 105
Synergy between Cyclase-associated protein and Cofilin accelerates actin filament depolymerization by two orders of magnitude
Shekhar, S., Chung, J., Kondev, J., Gelles, J., & Goode, B. L. (2019) · Nature Communications · doi:10.1038/s41467-019-13268-1 · Cited by 100
Distinct conformations of the kinesin Unc104 neck regulate a monomer to dimer motor transition
Al‐Bassam, J., Cui, Y., Klopfenstein, D. R., Carragher, B. O., Vale, R. D., & Milligan, R. A. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200308020 · Cited by 94
Modelling microtubule patterns
Karsenti, E., Nédélec, F., & Surrey, T. (2006) · Nature Cell Biology · doi:10.1038/ncb1498 · Cited by 95
Myosin learns to walk
Mehta, A. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.11.1981 · Cited by 90
Lethal Kinesin Mutations Reveal Amino Acids Important for ATPase Activation and Structural Coupling
Brendza, K. M., Rose, D. J., Gilbert, S. P., & Saxton, W. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31506 · Cited by 86
Demonstration of Coiled-Coil Interactions within the Kinesin Neck Region Using Synthetic Peptides
Tripet, B., Vale, R. D., & Hodges, R. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.8946 · Cited by 88
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 88
Structures of kinesin motor proteins
Marx, A., Hoenger, A., & Mandelkow�, E. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20392 · Cited by 84
Kinesins at a glance
Endow, S. A., Kull, F. J., & Liu, H. (2010) · Journal of Cell Science · doi:10.1242/jcs.064113 · Cited by 86
Kinetic evidence for low chemical processivity in ncd and Eg5
Crevel, I. M.-T. C., Lockhart, A., & Cross, R. A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1319 · Cited by 83
Trafficking of signaling modules by kinesin motors
Schnapp, B. J. (2003) · Journal of Cell Science · doi:10.1242/jcs.00488 · Cited by 82
Influence of the kinesin neck domain on dimerization and ATPase kinetics
Jiang, W., Stock, M. F., Li, X., & Hackney, D. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7626 · Cited by 75
Self-citation
Elevated polar ejection forces stabilize kinetochore–microtubule attachments
Cane, S., Ye, A. A., Luks-Morgan, S. J., & Maresca, T. J. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201211119 · Cited by 77
KIF1D is a fast non‐processive kinesin that demonstrates novel K‐loop‐dependent mechanochemistry
Rogers, K. R., Weiss, S., Crevel, I., Brophy, P. J., Geeves, M., & Cross, R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5101 · Cited by 73
Plus-end motors override minus-end motors during transport of squid axon vesicles on microtubules.
Mureşan, V., Godek, C. P., Reese, T. S., & Schnapp, B. J. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.2.383 · Cited by 72
Kinetics: A Tool to Study Molecular Motors
Gilbert, S. P., & Mackey, A. T. (2000) · Methods · doi:10.1006/meth.2000.1086 · Cited by 72
A model of the microtubule–kinesin complex based on electron cryomicroscopy and X-ray crystallography
Kozielski, F., Arnal, I., & Wade, R. H. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70083-1 · Cited by 68
Motile Properties of the Kinesin-related Cin8p Spindle Motor Extracted from Saccharomyces cerevisiae Cells
Gheber, L., Kuo, S. C., & Hoyt, M. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9564 · Cited by 65
Motor domains of kinesin and ncd interact with microtubule protofilaments with the same binding geometry
Hoenger, A., & Milligan, R. A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0757 · Cited by 60
The E-Hook of Tubulin Interacts with Kinesin’s Head to Increase Processivity and Speed
Lakämper, S., & Meyhöfer, E. (2005) · Biophysical Journal · doi:10.1529/biophysj.104.057505 · Cited by 63
Motility of Single One-Headed Kinesin Molecules Along Microtubules
Inoue, Y., Iwane, A. H., Miyai, T., Muto, E., & Yanagida, T. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75925-5 · Cited by 58
The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations
Kozielski, F., Bonis, S. D., Burmeister, W. P., Cohen‐Addad, C., & Wade, R. H. (1999) · Structure · doi:10.1016/s0969-2126(00)80030-1 · Cited by 58
Motor dynamics underlying cargo transport by pairs of kinesin-1 and kinesin-3 motors
Arpağ, G., Norris, S. R., Mousavi, S. I., Soppina, V., Verhey, K. J., Hancock, W. O., & Tüzel, E. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.01.036 · Cited by 56
Kinetics Processivity and the Direction of Motion of Ncd
Pechatnikova, E., & Taylor, E. W. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)76951-1 · Cited by 57
Regulation of molecular motor proteins
Reilein, A. R., Rogers, S. L., Tuma, M. C., & Gelfand, V. I. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)04005-0 · Cited by 56
Bidirectional motility of kinesin-5 motor proteins: structural determinants, cumulative functions and physiological roles
Singh, S. K., Pandey, H., Al‐Bassam, J., & Gheber, L. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2754-7 · Cited by 53
Loop L5 Acts as a Conformational Latch in the Mitotic Kinesin Eg5*
Behnke-Parks, W. M., Vendome, J., Honig, B., Maliga, Z., Moores, C., & Rosenfeld, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.192930 · Cited by 63
An ALS ‐associated KIF5A mutant forms oligomers and aggregates and induces neuronal toxicity
Nakano, J., Chiba, K., & Niwa, S. (2022) · Genes to Cells · doi:10.1111/gtc.12936 · Cited by 51
Kinesin velocity increases with the number of motors pulling against viscoelastic drag
Gagliano, J., Walb, M. C., Blaker, B., Macosko, J. C., & Holzwarth, G. (2009) · European Biophysics Journal · doi:10.1007/s00249-009-0560-8 · Cited by 55
Rapid double 8‐nm steps by a kinesin mutant
Higuchi, H., Bronner, C. E., Park, H., & Endow, S. A. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600306 · Cited by 50
KIF14 Binds Tightly to Microtubules and Adopts a Rigor-Like Conformation
Arora, K., Talje, L., Asenjo, A. B., Andersen, P. L., Atchia, K., Joshi, M., Sosa, H., Allingham, J. S., & Kwok, B. H. B. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.05.030 · Cited by 49
Diffusion and Directed Movement
Furuta, K., Edamatsu, M., Maeda, Y., & Toyoshima, Y. Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803730200 · Cited by 43
Processive and Nonprocessive Models of Kinesin Movement
Endow, S. A., & Barker, D. S. (2003) · Annual Review of Physiology · doi:10.1146/annurev.physiol.65.092101.142550 · Cited by 47
Importance of a flexible hinge near the motor domain in kinesin‐driven motility
Grummt, M., Woehlke, G., Henningsen, U., Fuchs, S., Schleicher, M., & Schliwa, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5536 · Cited by 48
Nucleotide-dependent conformations of the kinesin dimer interacting with microtubules
Arnal, I., & Wade, R. H. (1998) · Structure · doi:10.1016/s0969-2126(98)00005-7 · Cited by 45
Single Fungal Kinesin Motor Molecules Move Processively along Microtubules
Lakämper, S., Kallipolitou, A., Woehlke, G., Schliwa, M., & Meyhöfer, E. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74991-1 · Cited by 44
Calcium-induced Mechanical Change in the Neck Domain Alters the Activity of Plant Myosin XI
Tominaga, M., Kojima, H., Yokota, E., Nakamori, R., Anson, M., Shimmen, T., & Oiwa, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346668 · Cited by 44
[18] Studies of molecular motors using caged compounds
Dantzig, J. A., Higuchi, H., & Goldman, Y. E. (1998) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(98)91021-7 · Cited by 43
Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa
Kallipolitou, A., Deluca, D., Majdic, U., Lakämper, S., Cross, R., Meyhöfer, E., Moroder, L., Schliwa, M., & Woehlke, G. (2001) · The EMBO Journal · doi:10.1093/emboj/20.22.6226 · Cited by 41
Processivity of the Kinesin-2 KIF3A Results from Rear Head Gating and Not Front Head Gating
Chen, G.-Y., Arginteanu, D., & Hancock, W. O. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.628032 · Cited by 40
Monomeric Kinesin Head Domains Hydrolyze Multiple ATP Molecules before Release from a Microtubule
Jiang, W., & Hackney, D. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5616 · Cited by 41
Self-citation
Arabidopsis thaliana protein, ATK1, is a minus‐end directed kinesin that exhibits non‐processive movement
Marcus, A. I., Ambrose, C., Blickley, L., Hancock, W. O., & Cyr, R. J. (2002) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.10045 · Cited by 42
The Molecular Mechanism of Organelle Transport along Microtubules: The Identification and Characterization of Kifs (Kinesin Superfamily Proteins).
Hirokawa, N. (1996) · Cell Structure and Function · doi:10.1247/csf.21.357 · Cited by 40
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
The Loop 5 Element Structurally and Kinetically Coordinates Dimers of the Human Kinesin-5, Eg5
Waitzman, J. S., Larson, A. G., Cochran, J. C., Naber, N. I., Cooke, R., Kull, F. J., Pate, E., & Rice, S. E. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.10.032 · Cited by 38
The Second Microtubule-binding Site of Monomeric Kid Enhances the Microtubule Affinity
Shiroguchi, K., Ohsugi, M., Edamatsu, M., Yamamoto, T. S., & Toyoshima, Y. Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212274200 · Cited by 36
A kinesin motor in a force-producing conformation
Heuston, E. F., Bronner, C. E., Kull, F. J., & Endow, S. A. (2010) · BMC Structural Biology · doi:10.1186/1472-6807-10-19 · Cited by 37
Alternating Site ATPase Pathway of Rat Conventional Kinesin
Auerbach, S. D., & Johnson, K. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502984200 · Cited by 35
Kif2C Minimal Functional Domain Has Unusual Nucleotide Binding Properties That Are Adapted to Microtubule Depolymerization
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 35
The stepping motor protein as a feedback control ratchet
Bier, M. (2006) · Biosystems · doi:10.1016/j.biosystems.2006.07.013 · Cited by 33
Only one pRNA hexamer but multiple copies of the DNA-packaging protein gp16 are needed for the motor to package bacterial virus phi29 genomic DNA
Shu, D., & Guo, P. (2003) · Virology · doi:10.1016/s0042-6822(03)00011-4 · Cited by 33
Engineered kinesin motor proteins amenable to small-molecule inhibition
Engelke, M. F., Winding, M., Yue, Y., Shastry, S., Teloni, F., Reddy, S., Blasius, T. L., Soppina, P., Hancock, W. O., Gelfand, V. I., et al. (2016) · Nature Communications · doi:10.1038/ncomms11159 · Cited by 34

Authors: Hackney, D. D.
Affiliations: Carnegie Mellon University (US)
Corresponding author: Hackney, David D.
ORCID: Hackney, David D.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1995-10
Volume: 377
Issue: 6548
Pages: 448-450
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/377448a0
OpenAlex: W2049953608
Cited by: 177
References: 13
Citations by year: 2026: 4 · 2024: 7 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 4 · 2018: 1 · 2017: 4 · 2016: 4 · 2015: 5 · 2014: 2 · 2013: 1 · 2012: 5
FWCI: 4.03
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
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
Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
Keywords: kinesin, microtubule sliding, ATP hydrolysis, processivity, microtubule binding, ADP binding, hand-over-hand mechanism, high-salt conditions, motility assay
MeSH terms: Adenosine Diphosphate, Adenosine Triphosphate, Hydrolysis, Microtubules, Kinesins

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

Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks