Axonal transport: Driving synaptic function
Open accessAbstract
From trafficking to maintenance: Neurons are remarkably polarized in that proteins made in the cytosol often need to travel many tens or hundreds of cell body lengths along axons to their sites of action in the synapse. Axonal transport of these components is driven by molecular motors along axonal microtubules. Guedes-Dias and Holzbaur review the cell biology of axonal transport and highlight the roles this fundamental process plays in organismal health. Science , this issue p. eaaw9997
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?
It cannot be excluded that the SSRI intervention could have an effect on specific binding in the white matter.
“Further, given that the centrum semiovale had the second highest estimated effect size (Cohen’s d of 0.51) and that we saw an effect of intervention duration for the centrum semiovale, we cannot exclude that the SSRI intervention could have an effect on the specific binding in the white matter, e.g. due to increased axonal transport of newly synthesized synaptic vesicle precursors [56].”
From Effects of escitalopram on synaptic density in the healthy human brain: a randomized controlled trial (2023) · cites this paper as [56]
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
Molecular anatomy of a trafficking organelle
Takamori, S., Holt, M., Stenius, K., Lemke, E. A., Grønborg, M., Riedel, D., Urlaub, H., Schenck, S., Brügger, B., Ringler, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.030 · Cited by 2,373 · see citing works
Kanai, Y., Dohmae, N., & Hirokawa, N. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.022 · Cited by 1,109 · see citing works
Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012 · see citing works
Self-citationQuantitative ultrastructural analysis of hippocampal excitatory synapses
Schikorski, T., & Stevens, C. F. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-15-05858.1997 · Cited by 997 · see citing works
Mutant dynactin in motor neuron disease
Puls, I., Jonnakuty, C., LaMonte, B. H., Holzbaur, E. L. F., Tokito, M. K., MANN, E. A., Floeter, M. K., Bidus, K., Drayna, D. T., Oh, S. J., et al. (2003) · Nature Genetics · doi:10.1038/ng1123 · Cited by 961 · see citing works
Self-citationSaudou, F., & Humbert, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.02.003 · Cited by 945 · see citing works
Control of microtubule organization and dynamics: Two ends in the limelight
Akhmanova, A., & Steinmetz, M. O. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4084 · Cited by 895 · see citing works
The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871 · see citing works
Activity-driven local ATP synthesis is required for synaptic function
Rangaraju, V., Calloway, N., & Ryan, T. A. (2014) · Cell · doi:10.1016/j.cell.2013.12.042 · Cited by 836 · see citing works
Neuropeptide Transmission in Brain Circuits
van den Pol, A. N. (2012) · Neuron · doi:10.1016/j.neuron.2012.09.014 · Cited by 810 · see citing works
Baas, P. W., Deitch, J. S., Black, M. M., & Banker, G. A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.8335 · Cited by 742 · see citing works
Stepanova, T., Slemmer, J., Hoogenraad, C. C., Lansbergen, G. W. A., Dortland, B. R., Zeeuw, C. I. D., Grosveld, F. G., van Cappellen, G. W. A., Akhmanova, A. S., & Galjart, N. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-07-02655.2003 · Cited by 702 · see citing works
Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons
Maday, S., Wallace, K. E., & Holzbaur, E. L. F. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201106120 · Cited by 681 · cited 3× · see citing works
“Autophagosomes initially showbidirectional oscillatory movement before engaging in processive retrograde transport (154).”
BackgroundSelf-citationOkada, Y., Yamazaki, H., Sekine‐Aizawa, Y., & Hirokawa, N. (1995) · Cell · doi:10.1016/0092-8674(95)90538-3 · Cited by 679 · see citing works
Miro1 Is a Calcium Sensor for Glutamate Receptor-Dependent Localization of Mitochondria at Synapses
MacAskill, A. F., Rinholm, J. E., Twelvetrees, A. E., Arancibia‐Cárcamo, I. L., Muir, J., Fransson, Å., Aspenström, P., Attwell, D., & Kittler, J. T. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.030 · Cited by 677 · see citing works
Genome-Wide Analyses Identify KIF5A as a Novel ALS Gene
Nicolas, A., Kenna, K. P., Renton, A. E., Ticozzi, N., Faghri, F., Chia, R., Dominov, J. A., Kenna, B., Nalls, M. A., Keagle, P. J., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.02.027 · Cited by 670 · see citing works
The cytoplasmic dynein transport machinery and its many cargoes
Reck‐Peterson, S. L., Redwine, W. B., Vale, R. D., & Carter, A. P. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0004-3 · Cited by 660 · see citing works
Building the Neuronal Microtubule Cytoskeleton
Kapitein, L. C., & Hoogenraad, C. C. (2015) · Neuron · doi:10.1016/j.neuron.2015.05.046 · Cited by 654 · see citing works
Hirschberg, K., Miller, C. M., Ellenberg, J., Presley, J. F., Siggia, E. D., Phair, R. D., & Lippincott‐Schwartz, J. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.6.1485 · Cited by 610 · see citing works
Microtubule Stabilization Reduces Scarring and Causes Axon Regeneration After Spinal Cord Injury
Hellal, F., Hurtado, A., Ruschel, J., Flynn, K. C., Laskowski, C. J., Umlauf, M., Kapitein, L. C., Strikis, D., Lemmon, V., Bixby, J. L., et al. (2011) · Science · doi:10.1126/science.1201148 · Cited by 592 · see citing works
Activation of cytoplasmic dynein motility by dynactin-cargo adapter complexes
McKenney, R. J., Huynh, W., Tanenbaum, M. E., Bhabha, G., & Vale, R. D. (2014) · Science · doi:10.1126/science.1254198 · Cited by 571 · see citing works
Microtubule dynamics: an interplay of biochemistry and mechanics
Brouhard, G. J., & Rice, L. M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0009-y · Cited by 569 · see citing works
Microtubule stabilization specifies initial neuronal polarization
Witte, H., Neukirchen, D., & Bradke, F. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707042 · Cited by 564 · see citing works
Mitostasis in Neurons: Maintaining Mitochondria in an Extended Cellular Architecture
Misgeld, T., & Schwarz, T. L. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.055 · Cited by 546 · see citing works
Microtubules acquire resistance from mechanical breakage through intralumenal acetylation
Xu, Z., Schaedel, L., Portran, D., Aguilar, A., Gaillard, J., Marinkovich, M. P., Théry, M., & Nachury, M. V. (2017) · Science · doi:10.1126/science.aai8764 · Cited by 513 · see citing works
Johansson, M., Rocha, N., Zwart, W., Jordens, I., Janssen, L., Kuijl, C., Olkkonen, V. M., & Neefjes, J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606077 · Cited by 505 · see citing works
Cytoplasmic dynein functions as a gear in response to load
Mallik, R., Carter, B. C., Lex, S. A., King, S. J., & Gross, S. P. (2004) · Nature · doi:10.1038/nature02293 · Cited by 494 · see citing works
Tubulin acetylation protects long-lived microtubules against mechanical ageing
Portran, D., Schaedel, L., Xu, Z., Théry, M., & Nachury, M. V. (2017) · Nature Cell Biology · doi:10.1038/ncb3481 · Cited by 491 · see citing works
Jung, H., Yoon, B. C., & Holt, C. E. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3210 · Cited by 487 · see citing works
Poirier, K., Lebrun, N., Broix, L., Tian, G., Saillour, Y., Boscheron, C., Parrini, E., Valence, S., Saintpierre, B., Oger, M., et al. (2013) · Nature Genetics · doi:10.1038/ng.2613 · Cited by 479 · see citing works
Dynamic Axonal Translation in Developing and Mature Visual Circuits
Shigeoka, T., Jung, H., Jung, J., Turner-Bridger, B., Ohk, J., Lin, J. Q., Amieux, P. S., & Holt, C. E. (2016) · Cell · doi:10.1016/j.cell.2016.05.029 · Cited by 458 · see citing works
TRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendrites
van Spronsen, M., Mikhaylova, M., Lipka, J., Schlager, M. A., van den Heuvel, D. J., Kuijpers, M., Wulf, P. S., Keijzer, N., Demmers, J., Kapitein, L. C., et al. (2013) · Neuron · doi:10.1016/j.neuron.2012.11.027 · Cited by 450 · see citing works
Late Endosomes Act as mRNA Translation Platforms and Sustain Mitochondria in Axons
Cioni, J.-M., Lin, J. Q., Holtermann, A., Koppers, M., Jakobs, M. A., Azizi, A., Turner-Bridger, B., Shigeoka, T., Franze, K., Harris, W. A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.11.030 · Cited by 445 · see citing works
Systemic administration of epothilone B promotes axon regeneration after spinal cord injury
Ruschel, J., Hellal, F., Flynn, K. C., Dupraz, S., Elliott, D. A., Tedeschi, A., Bates, M., Sliwinski, C., Brook, G. A., Dobrindt, K., et al. (2015) · Science · doi:10.1126/science.aaa2958 · Cited by 433 · see citing works
Motor coordination via a tug-of-war mechanism drives bidirectional vesicle transport
Hendricks, A. G., Perlson, E., Ross, J. L., Schroeder, H. W., Tokito, M., & Holzbaur, E. L. F. (2010) · Current Biology · doi:10.1016/j.cub.2010.02.058 · Cited by 423 · see citing works
The structure of the dynactin complex and its interaction with dynein
Urnavicius, L., Zhang, K., Diamant, A. G., Motz, C., Schlager, M. A., Yu, M., Patel, N. A., Robinson, C. V., & Carter, A. P. (2015) · Science · doi:10.1126/science.aaa4080 · Cited by 421 · see citing works
Near-atomic model of microtubule-tau interactions
Kellogg, E. H., Hejab, N. M. A., Poepsel, S., Downing, K. H., DiMaio, F., & Nogales, E. (2018) · Science · doi:10.1126/science.aat1780 · Cited by 416 · see citing works
A Family of Protein-Deglutamylating Enzymes Associated with Neurodegeneration
Rogowski, K., van Dijk, J., Magiera, M. M., Bosc, C., Deloulme, J., Bosson, A., Peris, L., Gold, N. D., Lacroix, B., Bosch, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.10.014 · Cited by 397 · see citing works
Wong, Y. C., & Holzbaur, E. L. F. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1870-13.2014 · Cited by 395 · see citing works
Self-citationMicrotubule interaction site of the kinesin motor
Woehlke, G., Ruby, A. K., Hart, C. L., Ly, B., Hom-Booher, N., & Vale, R. D. (1997) · Cell · doi:10.1016/s0092-8674(00)80329-3 · Cited by 386 · see citing works
Autophagosome Biogenesis in Primary Neurons Follows an Ordered and Spatially Regulated Pathway
Maday, S., & Holzbaur, E. L. F. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.001 · Cited by 372 · see citing works
Self-citationFueling thought: Management of glycolysis and oxidative phosphorylation in neuronal metabolism
Yellen, G. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201803152 · Cited by 371 · see citing works
Okada, Y., & Hirokawa, N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.640 · Cited by 353 · see citing works
In vitro reconstitution of a highly processive recombinant human dynein complex
Schlager, M. A., Hoang, H. T., Urnavicius, L., Bullock, S. L., & Carter, A. P. (2014) · The EMBO Journal · doi:10.15252/embj.201488792 · Cited by 351 · see citing works
Fornasiero, E. F., Mandad, S., Wildhagen, H., Alevra, M., Rammner, B., Keihani, S., Opazo, F., Urban, I., Ischebeck, T., Sakib, M. S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06519-0 · Cited by 340 · see citing works
A Targeted Multienzyme Mechanism for Selective Microtubule Polyglutamylation
van Dijk, J., Rogowski, K., Miro, J., Lacroix, B., Eddé, B., & Janke, C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.04.012 · Cited by 320 · see citing works
DCTN1 mutations in Perry syndrome
Farrer, M. J., Hulihan, M., Kachergus, J. M., Dächsel, J. C., Stoessl, A. J., Grantier, L. L., Calne, S. M., Calne, D. B., Lechevalier, B., Chapon, F., et al. (2009) · Nature Genetics · doi:10.1038/ng.293 · Cited by 320 · see citing works
Waterman, C. M., Karki, S., & Holzbaur, E. L. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1634 · Cited by 316 · see citing works
Self-citationCauses and Consequences of Microtubule Acetylation
Janke, C., & Montagnac, G. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.044 · Cited by 312 · see citing works
Differentiation between oppositely oriented microtubules controls polarized neuronal transport
Tas, R. P., Chazeau, A., Cloin, B. M. C., Lambers, M. L. A., Hoogenraad, C. C., & Kapitein, L. C. (2017) · Neuron · doi:10.1016/j.neuron.2017.11.018 · Cited by 306 · see citing works
Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated
Zhang, K., Foster, H. E., Rondelet, A., Lacey, S. E., Bahi‐Buisson, N., Bird, A. W., & Carter, A. P. (2017) · Cell · doi:10.1016/j.cell.2017.05.025 · Cited by 297 · see citing works
Baas, P. W., Black, M. M., & Banker, G. A. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.6.3085 · Cited by 295 · see citing works
A vital role of tubulin-tyrosine-ligase for neuronal organization
Erck, C., Peris, L., Andrieux, A., Meissirel, C., Gruber, A. D., Vernet, M., Schweitzer, A., Saoudi, Y., Pointu, H., Bosc, C., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409626102 · Cited by 295 · see citing works
Microtubules self-repair in response to mechanical stress
Schaedel, L., John, K., Gaillard, J., Nachury, M. V., Blanchoin, L., & Théry, M. (2015) · Nature Materials · doi:10.1038/nmat4396 · Cited by 294 · see citing works
Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation
Aillaud, C., Bosc, C., Peris, L., Bosson, A., Heemeryck, P., Van Dijk, J., Le Friec, J., Boulan, B., Vossier, F., Sanman, L. E., et al. (2017) · Science · doi:10.1126/science.aao4165 · Cited by 293 · see citing works
Super-Resolution Imaging of the Extracellular Space in Living Brain Tissue
Tønnesen, J., Inavalli, V. V. G. K., & Nägerl, U. V. (2018) · Cell · doi:10.1016/j.cell.2018.02.007 · Cited by 293 · see citing works
Axon Extension Occurs Independently of Centrosomal Microtubule Nucleation
Stieß, M., Maghelli, N., Kapitein, L. C., Gomis-Rüth, S., Wilsch‐Bräuninger, M., Hoogenraad, C. C., Tolić, I. M., & Bradke, F. (2010) · Science · doi:10.1126/science.1182179 · Cited by 290 · see citing works
Dynein is required for polarized dendritic transport and uniform microtubule orientation in axons
Zheng, Y., Wildonger, J., Ye, B., Zhang, Y., Kita, A. M., Younger, S. H., Zimmerman, S., Jan, L. Y., & Jan, Y. N. (2008) · Nature Cell Biology · doi:10.1038/ncb1777 · Cited by 290 · see citing works
Molecular Adaptations Allow Dynein to Generate Large Collective Forces inside Cells
Rai, A. K., Rai, A., Ramaiya, A., Jha, R., & Mallik, R. (2013) · Cell · doi:10.1016/j.cell.2012.11.044 · Cited by 284 · see citing works
Microtubule Minus-End Stabilization by Polymerization-Driven CAMSAP Deposition
Jiang, K., Hua, S., Mohan, R., Grigoriev, I., Yau, K. W., Liu, Q., Katrukha, E. A., Altelaar, M. A. F., Heck, A. J. R., Hoogenraad, C. C., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.01.001 · Cited by 282 · see citing works
JIP1 regulates the directionality of APP axonal transport by coordinating kinesin and dynein motors
Fu, M., & Holzbaur, E. L. F. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302078 · Cited by 277 · see citing works
Self-citationDetection of GTP-Tubulin Conformation in Vivo Reveals a Role for GTP Remnants in Microtubule Rescues
Dimitrov, A., Quesnoit, M., Moutel, S., Cantaloube, I., Poüs, C., & Perez, F. (2008) · Science · doi:10.1126/science.1165401 · Cited by 273 · see citing works
Poirier, K., Saillour, Y., Bahi‐Buisson, N., Jaglin, X. H., Fallet‐Bianco, C., Nabbout, R., Castelnau, L., Roubertie, A., Attié‐Bitach, T., Desguerre, I., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq377 · Cited by 273 · see citing works
Hyder, F., Rothman, D. L., & Bennett, M. R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214912110 · Cited by 271 · see citing works
Long-distance retrograde neurotrophic factor signalling in neurons
Harrington, A., & Ginty, D. D. (2013) · Nature reviews. Neuroscience · doi:10.1038/nrn3253 · Cited by 269 · see citing works
Graded Control of Microtubule Severing by Tubulin Glutamylation
Valenstein, M. L., & Roll‐Mecak, A. (2016) · Cell · doi:10.1016/j.cell.2016.01.019 · Cited by 268 · see citing works
Quantitative imaging of energy expenditure in human brain
Zhu, X., Qiao, H., Du, F., Xiong, Q., Liu, X., Zhang, X., Uǧurbil, K., & Chen, W. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.02.013 · Cited by 267 · see citing works
Integrated regulation of motor-driven organelle transport by scaffolding proteins
Fu, M., & Holzbaur, E. L. F. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.002 · Cited by 266 · see citing works
Self-citationCryo-EM shows how dynactin recruits two dyneins for faster movement
Urnavicius, L., Lau, C. K., Elshenawy, M. M., Morales‐Ríos, E., Motz, C., Yıldız, A., & Carter, A. P. (2018) · Nature · doi:10.1038/nature25462 · Cited by 266 · see citing works
Vasohibins encode tubulin detyrosinating activity
Nieuwenhuis, J., Adamopoulos, A., Bleijerveld, O. B., Mazouzi, A., Stickel, E., Celie, P., Altelaar, M., Knipscheer, P., Perrakis, A., Blomen, V. A., et al. (2017) · Science · doi:10.1126/science.aao5676 · Cited by 266 · see citing works
Characterization of LAMP1-labeled nondegradative lysosomal and endocytic compartments in neurons
Cheng, X., Xie, Y., Zhou, B., Huang, N., Farfel‐Becker, T., & Sheng, Z. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201711083 · Cited by 264 · see citing works
Gopal, P. P., Nirschl, J., Klinman, E., & Holzbaur, E. L. F. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614462114 · Cited by 261 · see citing works
Self-citationLewis, T. L., Kwon, S.-K., Lee, A., Shaw, R., & Polleux, F. (2018) · Nature Communications · doi:10.1038/s41467-018-07416-2 · Cited by 260 · see citing works
Drosophila Spastin Regulates Synaptic Microtubule Networks and Is Required for Normal Motor Function
Sherwood, N. T., Sun, Q., Xue, M., Zhang, B., & Zinn, K. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020429 · Cited by 258 · see citing works
The interaction between cytoplasmic dynein and dynactin is required for fast axonal transport
Waterman, C. M., Karki, S., Kuznetsov, S. A., Tabb, J. S., Weiss, D. G., Langford, G. M., & Holzbaur, E. L. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.22.12180 · Cited by 257 · see citing works
Self-citationOrganization of neuronal microtubules in the nematode Caenorhabditis elegans.
Chalfie, M., & Thomson, J. N. (1979) · The Journal of Cell Biology · doi:10.1083/jcb.82.1.278 · Cited by 257 · see citing works
Taxol Facilitates Axon Regeneration in the Mature CNS
Sengottuvel, V., Leibinger, M., Pfreimer, M., Andreadaki, A., & Fischer, D. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4885-10.2011 · Cited by 254 · see citing works
The Axon Initial Segment: An Updated Viewpoint
Leterrier, C. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1922-17.2018 · Cited by 251 · see citing works
Chen, Y., & Sheng, Z.-H. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201302040 · Cited by 250 · see citing works
Niwa, S., Tanaka, Y., & Hirokawa, N. (2008) · Nature Cell Biology · doi:10.1038/ncb1785 · Cited by 232 · see citing works
Tyrosination of α‐tubulin controls the initiation of processive dynein–dynactin motility
McKenney, R. J., Huynh, W., Vale, R. D., & Sirajuddin, M. (2016) · The EMBO Journal · doi:10.15252/embj.201593071 · Cited by 232 · see citing works
BORC/kinesin-1 ensemble drives polarized transport of lysosomes into the axon
Farías, G. G., Guardia, C. M., De Pace, R., Britt, D. J., & Bonifacino, J. S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616363114 · Cited by 228 · see citing works
van Beuningen, S. F. B., Will, L., Harterink, M., Chazeau, A., van Battum, E. Y., Frias, C. P., Franker, M. A. M., Katrukha, E. A., Stucchi, R., Vocking, K., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.11.012 · Cited by 225 · see citing works
Microtubule Minus-End Binding Protein CAMSAP2 Controls Axon Specification and Dendrite Development
Yau, K. W., van Beuningen, S. F. B., Cunha‐Ferreira, I., Cloin, B. M. C., van Battum, E. Y., Will, L., Schätzle, P., Tas, R. P., van Krugten, J., Katrukha, E. A., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.019 · Cited by 218 · see citing works
Dynein activators and adaptors at a glance
Olenick, M. A., & Holzbaur, E. L. F. (2019) · Journal of Cell Science · doi:10.1242/jcs.227132 · Cited by 218 · see citing works
Self-citationCohen, L. D., Zuchman, R., Sorokina, O., Müller, A., Dieterich, D. C., Armstrong, J. D., Ziv, T., & Ziv, N. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063191 · Cited by 215 · see citing works
Changes in microtubule number and length during axon differentiation
Yu, W., & Baas, P. (1994) · The Journal of Neuroscience · doi:10.1523/jneurosci.14-05-02818.1994 · Cited by 213 · see citing works
Competition between microtubule-associated proteins directs motor transport
Monroy, B. Y., Sawyer, D. L., Ackermann, B. E., Borden, M. M., Tan, T. C., & Ori-McKenney, K. M. (2018) · Nature Communications · doi:10.1038/s41467-018-03909-2 · Cited by 213 · see citing works
Severing enzymes amplify microtubule arrays through lattice GTP-tubulin incorporation
Vemu, A., Szczesna, E., Zehr, E. A., Spector, J. O., Grigorieff, N., Deaconescu, A. M., & Roll-Mecak, A. (2018) · Science · doi:10.1126/science.aau1504 · Cited by 210 · see citing works
Resolving bundled microtubules using anti-tubulin nanobodies
Mikhaylova, M., Cloin, B. M. C., Finan, K., van den Berg, R., Teeuw, J., Kijanka, M. M., Sokołowski, M., Katrukha, E. A., Maidorn, M., Opazo, F., et al. (2015) · Nature Communications · doi:10.1038/ncomms8933 · Cited by 206 · see citing works
Stable kinesin and dynein assemblies drive the axonal transport of mammalian prion protein vesicles
Encalada, S. E., Szpankowski, L., Xia, C.-H., & Goldstein, L. S. B. (2011) · Cell · doi:10.1016/j.cell.2011.01.021 · Cited by 206 · see citing works
Fu, M., Nirschl, J., & Holzbaur, E. L. F. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.04.015 · Cited by 205 · see citing works
Self-citationSerial analysis of microtubules in cultured rat sensory axons
Bray, D., & Bunge, M. B. (1981) · Journal of Neurocytology · doi:10.1007/bf01262592 · Cited by 203 · see citing works
Dynactin Is Required for Transport Initiation from the Distal Axon
Moughamian, A. J., & Holzbaur, E. L. F. (2012) · Neuron · doi:10.1016/j.neuron.2012.02.025 · Cited by 198 · see citing works
Self-citationSánchez-Huertas, C., Freixo, F., Viais, R., Lacasa, C., Soriano, E., & Lüders, J. (2016) · Nature Communications · doi:10.1038/ncomms12187 · Cited by 195 · see citing works
Nirschl, J., Magiera, M. M., Lazarus, J. E., Janke, C., & Holzbaur, E. L. F. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.046 · Cited by 192 · see citing works
Self-citationCytoskeleton dynamics in axon regeneration
Blanquie, O., & Bradke, F. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.02.024 · Cited by 189 · see citing works
Evidence That Myosin Activity Opposes Microtubule-Based Axonal Transport of Mitochondria
Pathak, D., Sepp, K. J., & Hollenbeck, P. J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1621-10.2010 · Cited by 188 · see citing works
Oates, E. C., Rossor, A. M., Hafezparast, M., Gonzalez, M., Speziani, F., MacArthur, D. G., Lek, M., Cottenie, E., Scoto, M., Foley, A. R., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.04.018 · Cited by 186 · see citing works
Self-repair promotes microtubule rescue
Aumeier, C., Schaedel, L., Gaillard, J., John, K., Blanchoin, L., & Théry, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3406 · Cited by 181 · see citing works
Autoinhibition and cooperative activation mechanisms of cytoplasmic dynein
Torisawa, T., Ichikawa, M., Furuta, A., Saito, K., Oiwa, K., Kojima, H., Toyoshima, Y. Y., & Furuta, K. (2014) · Nature Cell Biology · doi:10.1038/ncb3048 · Cited by 177 · see citing works
Neveling, K., Martinez-Carrera, L. A., Hölker, I., Heister, A. J. G. M., Verrips, A., Hosseinibarkooie, S., Gilissen, C., Vermeer, S., Pennings, M., Meijer, R. P. P., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.04.011 · Cited by 175 · see citing works
A microtubule bestiary: structural diversity in tubulin polymers
Chaaban, S., & Brouhard, G. J. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-05-0271 · Cited by 174 · see citing works
A dynamic formin-dependent deep F-actin network in axons
Ganguly, A., Tang, Y., Wang, L., Ladt, K. C., Loi, J., Dargent, B., Leterrier, C., & Roy, S. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201506110 · Cited by 173 · see citing works
Complete morphologies of basal forebrain cholinergic neurons in the mouse
Wu, H., Williams, J., & Nathans, J. (2014) · eLife · doi:10.7554/elife.02444 · Cited by 167 · see citing works
Lewis, T. L., Turi, G. F., Kwon, S., Losonczy, A., & Polleux, F. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.064 · Cited by 167 · see citing works
Autophagy in the presynaptic compartment in health and disease
Vijayan, V., & Verstreken, P. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611113 · Cited by 167 · see citing works
The nano-architecture of the axonal cytoskeleton
Leterrier, C., Dubey, P., & Roy, S. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.129 · Cited by 167 · see citing works
MAP7 family proteins regulate kinesin-1 recruitment and activation
Hooikaas, P. J., Martin, M., Mühlethaler, T., Kuijntjes, G.-J., Peeters, C. A. E., Katrukha, E. A., Ferrari, L., Stucchi, R., Verhagen, D. G. F., van Riel, W. E., et al. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201808065 · Cited by 166 · see citing works
Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin
Hendershott, M. C., & Vale, R. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404133111 · Cited by 165 · see citing works
Neuropeptide Delivery to Synapses by Long-Range Vesicle Circulation and Sporadic Capture
Wong, M. Y., Zhou, C., Shakiryanova, D. M., Lloyd, T. E., Deitcher, D. L., & Levitan, E. S. (2012) · Cell · doi:10.1016/j.cell.2011.12.036 · Cited by 164 · see citing works
End-binding proteins EB3 and EB1 link microtubules to ankyrin G in the axon initial segment
Leterrier, C., Vacher, H., Fache, M., d'Ortoli, S. A., Castets, F., Autillo‐Touati, A., & Dargent, B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018671108 · Cited by 164 · see citing works
Lee, J.-R., Srour, M., Kim, D., Hamdan, F. F., Lim, S.-H., Brunel‐Guitton, C., Décarie, J., Rossignol, E., Mitchell, G. A., Schreiber, A., et al. (2014) · Human Mutation · doi:10.1002/humu.22709 · Cited by 160 · see citing works
Separating the effects of nucleotide and EB binding on microtubule structure
Zhang, R., LaFrance, B., & Nogales, E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1802637115 · Cited by 160 · see citing works
Hu, J., Bai, X., Bowen, J. R., Dolat, L., Korobova, F. V., Yu, W., Baas, P. W., Svitkina, T., Gallo, G., & Spiliotis, E. T. (2012) · Current Biology · doi:10.1016/j.cub.2012.04.019 · Cited by 157 · see citing works
Nakata, T., Niwa, S., Okada, Y., Perez, F., & Hirokawa, N. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201104034 · Cited by 156 · see citing works
Lo, K. Y., Kuzmin, A., Unger, S. M., Petersen, J. D., & Silverman, M. A. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.01.018 · Cited by 155 · see citing works
Excessive tubulin polyglutamylation causes neurodegeneration and perturbs neuronal transport
Magiera, M. M., Bodakuntla, S., Žiak, J., Lacomme, S., Sousa, P. M., Leboucher, S., Hausrat, T. J., Bosc, C., Andrieux, A., Kneussel, M., et al. (2018) · The EMBO Journal · doi:10.15252/embj.2018100440 · Cited by 155 · see citing works
Kinesin-3 responds to local microtubule dynamics to target synaptic cargo delivery to the presynapse
Guedes-Dias, P., Nirschl, J. J., Abreu, N., Tokito, M. K., Janke, C., Magiera, M. M., & Holzbaur, E. L. F. (2019) · Current Biology · doi:10.1016/j.cub.2018.11.065 · Cited by 153 · see citing works
Self-citationMicrotubule Organization Determines Axonal Transport Dynamics
Yogev, S., Cooper, R. C., Fetter, R. D., Horowitz, M., & Shen, K. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.036 · Cited by 152 · see citing works
Cai, Q., Pan, P., & Sheng, Z. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0731-07.2007 · Cited by 150 · see citing works
Wu, Y., Huo, L., Maeder, C. I., Feng, W., & Shen, K. (2013) · Neuron · doi:10.1016/j.neuron.2013.04.035 · Cited by 144 · see citing works
An assay to image neuronal microtubule dynamics in mice
Kleele, T., Marinković, P., Williams, P. R., Stern, S., Weigand, E. E., Engerer, P., Naumann, R., Hartmann, J., Karl, R. M., Bradke, F., et al. (2014) · Nature Communications · doi:10.1038/ncomms5827 · Cited by 142 · see citing works
Kim, G.-W., Li, L., Gorbani, M., You, L., & Yang, X.-J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.464792 · Cited by 141 · see citing works
Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility
Grotjahn, D. A., Chowdhury, S., Xu, Y., McKenney, R. J., Schroer, T. A., & Lander, G. C. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0027-7 · Cited by 136 · see citing works
Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin
Szyk, A., Deaconescu, A. M., Piszczek, G., & Roll‐Mecak, A. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2148 · Cited by 135 · see citing works
Degradation of dendritic cargos requires Rab7-dependent transport to somatic lysosomes
Yap, C. C., Digilio, L. C., McMahon, L. P., Garcia, A. D. R., & Winckler, B. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201711039 · Cited by 135 · see citing works
Tubulin genes and malformations of cortical development
Romaniello, R., Arrigoni, F., Fry, A. E., Bassi, M. T., Rees, M. I., Borgatti, R., Pilz, D. T., & Cushion, T. D. (2018) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2018.07.012 · Cited by 132 · see citing works
Dynein Regulator NDEL1 Controls Polarized Cargo Transport at the Axon Initial Segment
Kuijpers, M., van de Willige, D., Freal, A., Chazeau, A., Franker, M. A. M., Hofenk, J., Rodrigues, R. J. C., Kapitein, L. C., Akhmanova, A. S., Jaarsma, D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.022 · Cited by 131 · see citing works
Vaccaro, V., Devine, M. J., Higgs, N., & Kittler, J. T. (2016) · EMBO Reports · doi:10.15252/embr.201642710 · Cited by 131 · see citing works
Peeters, K., Litvinenko, I., Asselbergh, B., Almeida-Souza, L., Chamova, T., Geuens, T., Ydens, E., Zimoń, M., Irobi, J., Vriendt, E. D., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.04.013 · Cited by 129 · see citing works
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 · see citing works
Loss of tubulin deglutamylase CCP1 causes infantile‐onset neurodegeneration
Shashi, V., Magiera, M. M., Klein, D., Zaki, M. S., Schoch, K., Rudnik‐Schöneborn, S., Norman, A. M., Neto, O. L. A., Dusl, M., Yuan, X., et al. (2018) · The EMBO Journal · doi:10.15252/embj.2018100540 · Cited by 127 · see citing works
Regulation of Axonal Transport by Protein Kinases
Gibbs, K. L., Greensmith, L., & Schiavo, G. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.08.003 · Cited by 126 · see citing works
Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport
Shima, T., Morikawa, M., Kaneshiro, J., Kambara, T., Kamimura, S., Yagi, T., Iwamoto, H., Uemura, S., Shigematsu, H., Shirouzu, M., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201711178 · Cited by 125 · see citing works
De novo mutations in KIF1A cause progressive encephalopathy and brain atrophy
Nieh, S. E., Madou, M. R. Z., Sirajuddin, M., Fregeau, B., McKnight, D., Lexa, K. W., Strober, J. B., Spaeth, C. G., Hallinan, B. E., Smaoui, N., et al. (2015) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.198 · Cited by 124 · see citing works
Myosin II Activity Facilitates Microtubule Bundling in the Neuronal Growth Cone Neck
Burnette, D. T., Ji, L., Schaefer, A. W., Medeiros, N. A., Danuser, G. M., & Forscher, P. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.05.016 · Cited by 123 · see citing works
Impaired JIP3-dependent axonal lysosome transport promotes amyloid plaque pathology
Gowrishankar, S., Wu, Y., & Ferguson, S. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201612148 · Cited by 123 · see citing works
Newly produced synaptic vesicle proteins are preferentially used in synaptic transmission
Truckenbrodt, S., Viplav, A., Jähne, S., Vogts, A., Denker, A., Wildhagen, H., Fornasiero, E. F., & Rizzoli, S. O. (2018) · The EMBO Journal · doi:10.15252/embj.201798044 · Cited by 123 · see citing works
The Dynamic Localization of Cytoplasmic Dynein in Neurons Is Driven by Kinesin-1
Twelvetrees, A. E., Pernigo, S., Sanger, A., Guedes-Dias, P., Schiavo, G., Steiner, R. A., Dodding, M. P., & Holzbaur, E. L. F. (2016) · Neuron · doi:10.1016/j.neuron.2016.04.046 · Cited by 122 · see citing works
Self-citationTortosa, E., Adolfs, Y., Fukata, M., Pasterkamp, R. J., Kapitein, L. C., & Hoogenraad, C. C. (2017) · Neuron · doi:10.1016/j.neuron.2017.04.042 · Cited by 120 · see citing works
Mitochondrial dynamics and quality control in Huntington's disease
Guedes-Dias, P., Pinho, B. R., Soares, T. R., de Proença, J., Duchen, M. R., & Oliveira, J. M. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.09.008 · Cited by 119 · see citing works
Self-citationMechanistic Logic Underlying the Axonal Transport of Cytosolic Proteins
Scott, D. A., Das, U., Tang, Y., & Roy, S. (2011) · Neuron · doi:10.1016/j.neuron.2011.03.022 · Cited by 119 · see citing works
Biswas, S., & Kalil, K. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2281-17.2017 · Cited by 119 · see citing works
Deacetylation of Miro1 by HDAC6 blocks mitochondrial transport and mediates axon growth inhibition
Kalinski, A. L., Kar, A. N., Craver, J., Tosolini, A. P., Sleigh, J. N., Lee, S. J., Hawthorne, A. L., Brito‐Vargas, P., Miller-Randolph, S., Passino, R., et al. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201702187 · Cited by 119 · see citing works
Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams
Chaudhary, A. R., Berger, F., Berger, C. L., & Hendricks, A. G. (2018) · Traffic · doi:10.1111/tra.12537 · Cited by 118 · see citing works
Structural basis for kinesin-1:cargo recognition
Pernigo, S., Lamprecht, A., Steiner, R. A., & Dodding, M. P. (2013) · Science · doi:10.1126/science.1234264 · Cited by 117 · see citing works
Atherton, J., Farabella, I., Yu, I.-M., Rosenfeld, S. S., Houdusse, A., Topf, M., & Moores, C. A. (2014) · eLife · doi:10.2210/pdb4uxr/pdb · Cited by 110 · see citing works
Kevenaar, J. T., Bianchi, S., van Spronsen, M., Olieric, N., Lipka, J., Frias, C. P., Mikhaylova, M., Harterink, M., Keijzer, N., Wulf, P. S., et al. (2016) · Current Biology · doi:10.1016/j.cub.2016.01.048 · Cited by 110 · 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
Kuo, Y., Trottier, O., Mahamdeh, M., & Howard, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818824116 · Cited by 106 · see citing works
Tubulins and brain development – The origins of functional specification
Breuss, M. W., Leca, I., Gstrein, T., Hansen, A. H., & Keays, D. A. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.03.002 · Cited by 102 · see citing works
Defective Axonal Transport of Rab7 GTPase Results in Dysregulated Trophic Signaling
Zhang, K., Kenan, R. F. B., Osakada, Y., Xu, W. L., Sinit, R. S., Chen, L., Zhao, X., Chen, J.-Y., Cui, B., & Wu, C. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.4322-12.2013 · Cited by 99 · see citing works
Brill, M. S., Kleele, T., Ruschkies, L., Wang, M., Marahori, N. A., Reuter, M. S., Hausrat, T. J., Weigand, E. E., Fisher, M., Ahles, A., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.049 · Cited by 99 · see citing works
Kwinter, D. M., Lo, K. Y., Mafi, P., & Silverman, M. A. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.05.038 · Cited by 98 · see citing works
Farı́as, G. G., Freal, A., Tortosa, E., Stucchi, R., Pan, X., Portegies, S., Will, L., Altelaar, M. A. F., & Hoogenraad, C. C. (2019) · Neuron · doi:10.1016/j.neuron.2019.01.030 · Cited by 96 · see citing works
The structured core of human β tubulin confers isotype-specific polymerization properties
Pamula, M. C., Ti, S.-C., & Kapoor, T. M. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201603050 · Cited by 95 · see citing works
The impact of cytoskeletal organization on the local regulation of neuronal transport
Nirschl, J., Ghiretti, A. E., & Holzbaur, E. L. F. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.100 · Cited by 95 · see citing works
Self-citationMicrotubule plus-end tracking proteins in neuronal development
van de Willige, D., Hoogenraad, C. C., & Akhmanova, A. S. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2168-3 · Cited by 93 · see citing works
Smit‐Rigter, L. A., Rajendran, R., Silva, C. A., Spierenburg, L., Groeneweg, F. L., Ruimschotel, E., van Versendaal, D., van der Togt, C., Eysel, U. T., Heimel, J. A., et al. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.033 · Cited by 88 · see citing works
Dynein activator Hook1 is required for trafficking of BDNF-signaling endosomes in neurons
Olenick, M. A., Domínguez, R., & Holzbaur, E. L. F. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201805016 · Cited by 87 · see citing works
Self-citationTHE CYTOSKELETON IN MYELINATED AXONS: SERIAL SECTION STUDY
Tsukita, S., & Ishikawa, H. (1981) · Biomedical Research · doi:10.2220/biomedres.2.424 · Cited by 86 · see citing works
Roy, S. (2013) · The Neuroscientist · doi:10.1177/1073858413498306 · Cited by 85 · see citing works
Lessard, D. V., Zinder, O. J., Hotta, T., Verhey, K. J., Ohi, R., & Berger, C. L. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005765 · Cited by 85 · see citing works
Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles
Prezel, E., Elie, A., Delaroche, J., Stoppin-Mellet, V., Bosc, C., Serre, L., Fourest-Lieuvin, A., Andrieux, A., Vantard, M., & Arnal, I. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0429 · Cited by 83 · see citing works
Sambri, I., D’Alessio, R., Ezhova, Y., Giuliano, T., Sorrentino, N. C., Cacace, V., Risi, M. D., Cataldi, M., Annunziato, L., Leonibus, E. D., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606965 · Cited by 81 · see citing works
CAMSAP3 maintains neuronal polarity through regulation of microtubule stability
Pongrakhananon, V., Saito, H., Hiver, S., Abe, T., Shioi, G., Meng, W., & Takeichi, M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803875115 · Cited by 81 · see citing works
Soppina, V., & Verhey, K. J. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-01-0696 · Cited by 80 · see citing works
MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules
Chaudhary, A. R., Lu, H., Krementsova, E. B., Bookwalter, C. S., Trybus, K. M., & Hendricks, A. G. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008052 · Cited by 80 · see citing works
Motor reattachment kinetics play a dominant role in multimotor-driven cargo transport
Feng, Q., Mickolajczyk, K. J., Chen, G.-Y., & Hancock, W. O. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.016 · Cited by 76 · see citing works
Wei, D., Gao, N., Li, L., Zhu, J.-X., Diao, L., Huang, J., Han, Q., Wang, S., Xue, H., Wang, Q., et al. (2017) · Cerebral Cortex · doi:10.1093/cercor/bhx225 · Cited by 75 · see citing works
TRIM46 Organizes Microtubule Fasciculation in the Axon Initial Segment
Harterink, M., Vocking, K., Pan, X., Soriano, E., Slenders, L., Freal, A., Tas, R. P., van de Wetering, W. J., Timmer, K., Motshagen, J., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.3105-18.2019 · Cited by 75 · see citing works
Direct induction of microtubule branching by microtubule nucleation factor SSNA1
Basnet, N., Nedozrálová, H., Crevenna, Á. H., Bodakuntla, S., Schlichthaerle, T., Taschner, M. J., Giovanni Cardone, A., Janke, C., Jungmann, R., Magiera, M. M., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0199-8 · Cited by 70 · see citing works
Cogli, L., Piro, F., & Bucci, C. (2009) · Biochemical Society Transactions · doi:10.1042/bst0371027 · Cited by 65 · see citing works
Chung, P. J., Song, C., Deek, J., Miller, H. P., Li, Y., Choi, M. C., Wilson, L., Feinstein, S. C., & Safinya, C. R. (2016) · Nature Communications · doi:10.1038/ncomms12278 · Cited by 65 · see citing works
Multivesicular bodies mediate long-range retrograde NGF-TrkA signaling
Ye, M., Lehigh, K. M., & Ginty, D. D. (2018) · eLife · doi:10.7554/elife.33012 · Cited by 65 · see citing works
The tubulin code in neuronal polarity
Park, J. H., & Roll‐Mecak, A. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.03.001 · Cited by 61 · see citing works
Romaniello, R., Tonelli, A., Arrigoni, F., Baschirotto, C., Triulzi, F. M., Bresolin, N., Bassi, M. T., & Borgatti, R. (2012) · Developmental Medicine & Child Neurology · doi:10.1111/j.1469-8749.2012.04316.x · Cited by 58 · see citing works
Islands Containing Slowly Hydrolyzable GTP Analogs Promote Microtubule Rescues
Tropini, C., Roth, E. A., Žanić, M., Gardner, M. K., & Howard, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030103 · Cited by 57 · see citing works
Intracellular Ca 2+ Release and Synaptic Plasticity: A Tale of Many Stores
Padamsey, Z., Foster, W. J., & Emptage, N. J. (2018) · The Neuroscientist · doi:10.1177/1073858418785334 · Cited by 56 · see citing works
Pan, X., Cao, Y., Stucchi, R., Hooikaas, P. J., Portegies, S., Will, L., Martin, M., Akhmanova, A. S., Harterink, M., & Hoogenraad, C. C. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.084 · Cited by 55 · see citing works
The many disguises of the signalling endosome
Villarroel‐Campos, D., Schiavo, G., & Lazo, O. M. (2018) · FEBS Letters · doi:10.1002/1873-3468.13235 · Cited by 54 · see citing works
MTCL1 plays an essential role in maintaining Purkinje neuron axon initial segment
Satake, T., Yamashita, K., Hayashi, K., Miyatake, S., Tamura‐Nakano, M., Doi, H., Furuta, Y., Shioi, G., Miura, E., Takeo, Y. H., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201695630 · Cited by 53 · see citing works
Aiken, J., Moore, J. K., & Bates, E. A. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy416 · Cited by 53 · see citing works
Klinman, E., Tokito, M. K., & Holzbaur, E. L. F. (2017) · Traffic · doi:10.1111/tra.12529 · Cited by 50 · see citing works
Self-citationTwo kinesins drive anterograde neuropeptide transport
Lim, A. P. C., Rechtsteiner, A., & Saxton, W. M. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-12-0820 · Cited by 47 · see citing works
Ketschek, A., Spillane, M., Dun, X., Hardy, H., Chilton, J. K., & Gallo, G. (2016) · Developmental Neurobiology · doi:10.1002/dneu.22377 · Cited by 46 · see citing works
Expression of kinesin superfamily genes in cultured hippocampal neurons
Silverman, M. A., Kaech, S., Ramser, E. M., Lu, X., Lasarev, M. R., Nagalla, S. R., & Banker, G. A. (2010) · Cytoskeleton · doi:10.1002/cm.20487 · Cited by 37 · see citing works
Microtubules of frog olfactory axons: their length and number/axon
Burton, P. R. (1987) · Brain Research · doi:10.1016/0006-8993(87)90742-6 · Cited by 35 · see citing works
Quantifying Protein Copy Number in Super Resolution Using an Imaging-Invariant Calibration
Zanacchi, F. C., Manzo, C., Magrassi, R., Derr, N. D., & Lakadamyali, M. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.04.026 · Cited by 34 · see citing works
Goldberg–Shprintzen megacolon syndrome with associated sensory motor axonal neuropathy
Dafsari, H. S., Byrne, S., Lin, J., Pitt, M. C., Jongbloed, J. D. H., Flinter, F. A., & Jungbluth, H. (2015) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.36873 · Cited by 29 · see citing works
Understanding mRNA trafficking: Are we there yet?
Czaplinski, K. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.04.025 · Cited by 29 · see citing works
Activity Induces Fmr1-Sensitive Synaptic Capture of Anterograde Circulating Neuropeptide Vesicles
Cavolo, S. L., Bulgari, D., Deitcher, D. L., & Levitan, E. S. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2212-16.2016 · Cited by 29 · see citing works
Hayashi, K., Hasegawa, S., Sagawa, T., Tasaki, S., & Niwa, S. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp05890j · Cited by 28 · see citing works
An Essential Postdevelopmental Role for Lis1 in Mice
Hines, T. J., Gao, X., Sahu, S., Lange, M. M., Turner, J. R., Twiss, J. L., & Smith, D. S. (2018) · eNeuro · doi:10.1523/eneuro.0350-17.2018 · Cited by 16 · see citing works
Occurrence of fasciculated microtubules at nodes of Ranvier in rat spinal roots
Nakazawa, E., & Ishikawa, H. (1995) · Journal of Neurocytology · doi:10.1007/bf01189066 · Cited by 12 · see citing works
Differential effect of multiple kinesin motors on run length, force and microtubule binding rate
Gutiérrez–Medina, B., Buendía-Padilla, M., Gutiérrez-Esparza, A. J., & Camacho, A. R. O. (2018) · Biophysical Chemistry · doi:10.1016/j.bpc.2018.08.007 · Cited by 10 · see citing works
Native kinesin‐1 does not bind preferentially to GTP‐tubulin‐rich microtubules in vitro
Li, Q., King, S. J., & Xu, J. (2017) · Cytoskeleton · doi:10.1002/cm.21386 · Cited by 9 · see citing works
Cytoplasmic dynein dysfunction and neurodegenerative disease
Moughamian, A. J., & Holzbaur, E. L. F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809470-9.00013-8 · Cited by 7 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
The tubulin code and its role in controlling microtubule properties and functions
Janke, C., & Magiera, M. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0214-3 · Cited by 956 · see citing works
Mechanisms of microtubule organization in differentiated animal cells
Akhmanova, A., & Kapitein, L. C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00473-y · Cited by 233 · see citing works
Mechanism of STMN2 cryptic splice-polyadenylation and its correction for TDP-43 proteinopathies
Baughn, M. W., Melamed, Z., López‐Erauskin, J., Beccari, M. S., Ling, K., Zuberi, A. R., Presa, M. F., Gonzalo-Gil, E., Maimon, R., Vazquez‐Sanchez, S., et al. (2023) · Science · doi:10.1126/science.abq5622 · Cited by 236 · see citing works
Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction
Deniston, C. K., Salogiannis, J., Mathea, S., Snead, D., Lahiri, I., Matyszewski, M., Donosa, O., Watanabe, R., Böhning, J., Shiau, A. K., et al. (2020) · Nature · doi:10.1038/s41586-020-2673-2 · Cited by 243 · see citing works
Oligodendrocytes support axonal transport and maintenance via exosome secretion
Frühbeis, C., Kuo, W. P., Müller, C., Barth, K., Peris, L., Tenzer, S., Möbius, W., Werner, H. B., Nave, K., Fröhlich, D., et al. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000621 · Cited by 193 · see citing works
Kuijpers, M., Kochlamazashvili, G., Stumpf, A., Puchkov, D., Swaminathan, A., Lucht, M. T., Krause, E., Maritzen, T., Schmitz, D., & Haucke, V. (2021) · Neuron · doi:10.1016/j.neuron.2020.10.005 · Cited by 170 · see citing works
Boecker, C. A., Goldsmith, J., Dou, D., Cajka, G. G., & Holzbaur, E. L. F. (2021) · Current Biology · doi:10.1016/j.cub.2021.02.061 · Cited by 166 · see citing works
Self-citationStructure and Mechanics of Dynein Motors
Canty, J. T., Tan, R., Kusakci, E., Fernandes, J., & Yıldız, A. (2021) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111020-101511 · Cited by 129 · see citing works
Molecular Pathophysiological Mechanisms in Huntington’s Disease
Jurcău, A. (2022) · Biomedicines · doi:10.3390/biomedicines10061432 · Cited by 111 · see citing works
Cramer, A., Prasad, V., Eftestøl, E., Song, T., Hansson, K., Dugdale, H. F., Sadayappan, S., Ochala, J., Gundersen, K., & Millay, D. P. (2020) · Nature Communications · doi:10.1038/s41467-020-20058-7 · Cited by 109 · see citing works
Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport
Leonzino, M., Reinisch, K. M., & Camilli, P. V. D. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.159003 · Cited by 103 · see citing works
The Cell Biology of LRRK2 in Parkinson's Disease
Usmani, A., Shavarebi, F., & Hiniker, A. (2021) · Molecular and Cellular Biology · doi:10.1128/mcb.00660-20 · Cited by 97 · see citing works
Anterograde Axonal Transport in Neuronal Homeostasis and Disease
Guillaud, L., El-Agamy, S. E., Otsuki, M., & Terenzio, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.556175 · Cited by 95 · see citing works
Axonal energy metabolism, and the effects in aging and neurodegenerative diseases
Yang, S., Park, J. H., & Lu, H.-C. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00634-3 · Cited by 94 · see citing works
Mitochondrial Behavior in Axon Degeneration and Regeneration
Wang, B., Huang, M., Shang, D., Yan, X., Zhao, B., & Zhang, X. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.650038 · Cited by 90 · see citing works
Mechanism and regulation of kinesin motors.
Yildiz, A. (2025) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-024-00780-6 · Cited by 88 · see citing works
Barron, J. C., Hurley, E. P., & Parsons, M. P. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.689332 · Cited by 85 · see citing works
Short-distance vesicle transport via phase separation
Qiu, H., Wu, X., Ma, X., Li, S., Cai, Q., Ganzella, M., Ge, L., Zhang, H., & Zhang, M. (2024) · Cell · doi:10.1016/j.cell.2024.03.003 · Cited by 86 · see citing works
Tesco, G., & Lomoio, S. (2022) · Seminars in Immunology · doi:10.1016/j.smim.2022.101628 · Cited by 91 · see citing works
Neuronal maturation and axon regeneration: unfixing circuitry to enable repair
Hilton, B. J., Griffin, J. M., Fawcett, J. W., & Bradke, F. (2024) · Nature reviews. Neuroscience · doi:10.1038/s41583-024-00849-3 · Cited by 77 · see citing works
Li, Y., Sang, S., Ren, W., Pei, Y., Bian, Y., Chen, Y., & Sun, H. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113874 · Cited by 77 · see citing works
Azizi, S. A. (2020) · The Neuroscientist · doi:10.1177/1073858420974336 · Cited by 76 · see citing works
Tubulin polyglutamylation is a general traffic-control mechanism in hippocampal neurons
Bodakuntla, S., Schnitzler, A., Villablanca, C., González-Billault, C. E., Bièche, I., Janke, C., & Magiera, M. M. (2020) · Journal of Cell Science · doi:10.1242/jcs.241802 · Cited by 73 · see citing works
RNA Modifications and RNA Metabolism in Neurological Disease Pathogenesis
Chatterjee, B., Shen, C.-K. J., & Majumder, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111870 · Cited by 67 · see citing works
A Presynaptic Perspective on Transport and Assembly Mechanisms for Synapse Formation
Rizalar, F. S., Roosen, D. A., & Haucke, V. (2020) · Neuron · doi:10.1016/j.neuron.2020.09.038 · Cited by 63 · see citing works
Microtubule Organization Is Essential for Maintaining Cellular Morphology and Function
Huang, L., Peng, Y., Tao, X., Ding, X., Li, R., Jiang, Y., & Zuo, W. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1623181 · Cited by 64 · see citing works
Mitochondria in Alzheimer’s Disease Pathogenesis
Reiss, A. B., Gulkarov, S., Jacob, B., Srivastava, A., Pinkhasov, A., Gomolin, I. H., Stecker, M. M., Wısnıewskı, T., & Leon, J. D. (2024) · Life · doi:10.3390/life14020196 · Cited by 62 · see citing works
Fernandez-Valenzuela, J. J., Sanchez-Varo, R. M., Muñoz‐Castro, C., Castro, V. D., Sánchez‐Mejías, E., Navarro, V., Jiménez, S., Nuñez‐Diaz, C., Gómez-Arboledas, Á., Moreno‐González, I., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71767-4 · Cited by 60 · see citing works
Fang, C., Hernandez, P., Liow, K. K., Damiano, E., Zetterberg, H., Blennow, K., Feng, D., Chen, M., & Maccecchini, M. L. (2022) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2022.84 · Cited by 62 · see citing works
Metabolic and Cellular Compartments of Acetyl-CoA in the Healthy and Diseased Brain
Jankowska-Kulawy, A., Klimaszewska-Łata, J., Gul-Hinc, S., Ronowska, A., & Szutowicz, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710073 · Cited by 49 · see citing works
Bodakuntla, S., Yuan, X., Genova, M., Gadadhar, S., Leboucher, S., Birling, M., Klein, D., Martini, R., Janke, C., & Magiera, M. M. (2021) · The EMBO Journal · doi:10.15252/embj.2021108498 · Cited by 56 · see citing works
Synaptic Vesicle Recycling and the Endolysosomal System: A Reappraisal of Form and Function
Ivanova, D., & Cousin, M. A. (2022) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2022.826098 · Cited by 56 · see citing works
Braun, N. J., Yao, K. R., Alford, P. W., & Liao, D. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008306117 · Cited by 53 · see citing works
Synaptic Damage and Its Clinical Correlates in People With Early Huntington Disease
Delva, A., Michiels, L., Koole, M. J. B., Laere, K. V., & Vandenberghe, W. (2021) · Neurology · doi:10.1212/wnl.0000000000012969 · Cited by 53 · see citing works
Radwitz, J., Hausrat, T. J., Heisler, F. F., Janiesch, P. C., Pechmann, Y., Rübhausen, M., & Kneussel, M. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04607-5 · Cited by 53 · see citing works
LC3B phosphorylation regulates FYCO1 binding and directional transport of autophagosomes
Nieto-Torres, J. L., Shanahan, S.-L., Chassefeyre, R., Chaiamarit, T., Zaretski, S., Landeras-Bueno, S., Verhelle, A., Encalada, S. E., & Hansen, M. (2021) · Current Biology · doi:10.1016/j.cub.2021.05.052 · Cited by 52 · see citing works
AP-4-mediated axonal transport controls endocannabinoid production in neurons
Davies, A. K., Alecu, J. E., Ziegler, M., Vasilopoulou, C. G., Merciai, F., Jumo, H., Saber, W. A., Şahin, M., Ebrahimi‐Fakhari, D., & Borner, G. H. H. (2022) · Nature Communications · doi:10.1038/s41467-022-28609-w · Cited by 51 · see citing works
JIP3 interacts with dynein and kinesin-1 to regulate bidirectional organelle transport
Celestino, R., Gama, J. B., Castro-Rodrigues, A. F., Barbosa, D. J., Rocha, H., d’Amico, E. A., Musacchio, A., Carvalho, A. X., Morais-Cabral, J. H., & Gassmann, R. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202110057 · Cited by 48 · see citing works
Johansen, A., Armand, S., Plavén-Sigray, P., Nasser, A., Ozenne, B., Petersen, I. N., Keller, S. H., Madsen, J., Beliveau, V., Møller, K., et al. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02285-8 · Cited by 53 · see citing works
Cheng, X., & Sheng, Z. (2020) · Developmental Neurobiology · doi:10.1002/dneu.22748 · Cited by 50 · see citing works
Mechanisms of Neuroinvasion and Neuropathogenesis by Pathologic Flaviviruses
de Vries, L., & Harding, A. T. (2023) · Viruses · doi:10.3390/v15020261 · Cited by 48 · see citing works
The synaptic life of microtubules
Waites, C. L., Qu, X., & Bartolini, F. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.03.004 · Cited by 48 · see citing works
Saroja, S. R., Sharma, A., Hof, P. R., & Pereira, A. C. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12518 · Cited by 45 · see citing works
Dynamic microtubules at the synapse
Dent, E. W. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2020.01.003 · Cited by 47 · see citing works
Liang, X., Sun, L., Liao, X., Lei, T., Xia, M., Duan, D., Zeng, Z., Li, Q., Xu, Z., Men, W., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-44863-6 · Cited by 42 · see citing works
The Role of Axonal Transport in Glaucoma
Dias, M. S., Luo, X., Ribas, V. T., Petrs‐Silva, H., & Koch, J. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073935 · Cited by 45 · see citing works
Huang, K., Upadhyay, G. K., Ahn, Y., Sakakura, M., Pagan‐Diaz, G. J., Cho, Y., Weiss, A. C., Huang, C., Mitchell, J. W., Li, J., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313590121 · Cited by 42 · see citing works
Rab2 Drives Axonal Transport of Dense Core Vesicles and Lysosomal Organelles
Lund, V. K., Lycas, M. D., Schack, A. E., Andersen, R. C., Gether, U., & Kjærulff, O. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.108973 · Cited by 42 · see citing works
Ding, C., Wu, Y., Dabas, H., & Hammarlund, M. (2022) · eLife · doi:10.7554/elife.73557 · Cited by 41 · see citing works
Tubulin polyglutamylation, a regulator of microtubule functions, can cause neurodegeneration
Bodakuntla, S., Janke, C., & Magiera, M. M. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135656 · Cited by 40 · see citing works
Molecular and cellular mechanisms of spastin in neural development and disease (Review)
Liu, Q., Zhang, G., Ji, Z., & Lin, H. (2021) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2021.5051 · Cited by 40 · see citing works
The Role of Spastin in Axon Biology
Costa, A. C., & Sousa, M. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.934522 · Cited by 40 · see citing works
DNA damage response in neurodevelopment and neuromaintenance
Qing, X., Zhang, G., & Wang, Z. (2022) · FEBS Journal · doi:10.1111/febs.16535 · Cited by 38 · see citing works
Mann, J. R., McKenna, E. D., Mawrie, D., Papakis, V., Alessandrini, F., Anderson, E. N., Mayers, R., Ball, H. E., Kaspi, E., Lubinski, K., et al. (2023) · Science Advances · doi:10.1126/sciadv.adi5548 · Cited by 39 · see citing works
Collura, K. M., Niu, J., Sanders, S. S., Montersino, A., Holland, S. M., & Thomas, G. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013815 · Cited by 39 · see citing works
Presynaptic protein synthesis and brain plasticity: From physiology to neuropathology
Perrone‐Capano, C., Volpicelli, F., Penna, E., Chun, J. T., & Crispino, M. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102051 · Cited by 36 · see citing works
The role of RGC degeneration in the pathogenesis of glaucoma
Si, Z., Fan, Y., Wang, M., Zhao, J., Zhang, Y., Liu, D., & Zheng, Y. (2024) · International Journal of Biological Sciences · doi:10.7150/ijbs.103222 · Cited by 45 · see citing works
Perez, J. D., Fusco, C. M., & Schuman, E. M. (2021) · Annual Review of Genetics · doi:10.1146/annurev-genet-030321-054851 · Cited by 36 · see citing works
Axonal plasticity in response to active forces generated through magnetic nano-pulling
Falconieri, A., Vincentiis, S. D., Cappello, V., Convertino, D., Das, R., Ghignoli, S., Figoli, S., Luin, S., Català-Castro, F., Marchetti, L., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111912 · Cited by 34 · see citing works
Saez, T. M. M., Bessone, I. F., Rodriguez, M. S., Alloatti, M., Otero, M. G., Cromberg, L. E., Devoto, V. M. P., Oubiña, G., Sosa, L. J., Buffone, M. G., et al. (2020) · Development · doi:10.1242/dev.184069 · Cited by 32 · see citing works
Moya‐Alvarado, G., Guerra, M. V., Tiburcio, R., Bravo, E., & Bronfman, F. C. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105796 · Cited by 31 · see citing works
Mechanism and prospects of mitochondrial transplantation for spinal cord injury treatment
Wang, Q., Wang, X., Shang, Z., & Zhao, L. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-04077-5 · Cited by 32 · see citing works
Cargo-Mediated Activation of Cytoplasmic Dynein in vivo
Xiang, X., & Qiu, R. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.598952 · Cited by 32 · see citing works
Understanding how kinesin motor proteins regulate postsynaptic function in neuron
Fan, R., & Lai, K. (2021) · FEBS Journal · doi:10.1111/febs.16285 · Cited by 32 · see citing works
Hou, M., Shao, Z., Zhang, S., Liu, X., Fan, P., Jiang, M., Zhao, Y., Xiao, R., & Yuan, H. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04836-3 · Cited by 32 · see citing works
Spastin locally amplifies microtubule dynamics to pattern the axon for presynaptic cargo delivery
Aiken, J., & Holzbaur, E. L. F. (2024) · Current Biology · doi:10.1016/j.cub.2024.03.010 · Cited by 31 · see citing works
Self-citationEpigenetic treatment of behavioral and physiological deficits in a tauopathy mouse model
Wang, W., Cao, Q., Tan, T., Yang, F., Williams, J. B., & Yan, Z. (2021) · Aging Cell · doi:10.1111/acel.13456 · Cited by 29 · see citing works
Adult Mouse Retina Explants: From ex vivo to in vivo Model of Central Nervous System Injuries
Schaeffer, J., Delpech, C., Albert, F., Belin, S., & Nawabi, H. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.599948 · Cited by 30 · see citing works
Smart motors and cargo steering drive kinesin-mediated selective transport
Nabb, A. T., Frank, M., & Bentley, M. (2020) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103464 · Cited by 29 · see citing works
NMNAT2 supports vesicular glycolysis via NAD homeostasis to fuel fast axonal transport
Yang, S., Niou, Z., Enriquez, A., LaMar, J., Huang, J.-Y., Ling, K., Jafar‐Nejad, P., Gilley, J., Coleman, M. P., Tennessen, J. M., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00690-9 · Cited by 29 · see citing works
Espadas, I., Wingfield, J. L., Nakahata, Y., Chanda, K., Grinman, E., Ghosh, I., Bauer, K. E., Raveendra, B., Kiebler, M. A., Yasuda, R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-46972-8 · Cited by 28 · see citing works
Presynaptic perspective: Axonal transport defects in neurodevelopmental disorders
Xiong, G.-J., & Sheng, Z. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202401145 · Cited by 26 · see citing works
Scaramuzzino, C., Cuoc, E. C., Pla, P., Humbert, S., & Saudou, F. (2022) · Science Advances · doi:10.1126/sciadv.abj8812 · Cited by 27 · see citing works
How neurons maintain their axons long-term: an integrated view of axon biology and pathology
Smith, G. A., Sweeney, S. T., O’Kane, C. J., & Prokop, A. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1236815 · Cited by 26 · see citing works
Boosting peripheral BDNF rescues impaired in vivo axonal transport in CMT2D mice
Sleigh, J. N., Villarroel‐Campos, D., Surana, S., Wickenden, T., Tong, Y., Simkin, R. L., Vargas, J. N. S., Rhymes, E. R., Tosolini, A. P., West, S. J., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.157191 · Cited by 26 · see citing works
Anterograde transport of α-herpesviruses in neuronal axons
DuRaine, G. D., & Johnson, D. C. (2021) · Virology · doi:10.1016/j.virol.2021.02.011 · Cited by 24 · see citing works
Yıldız, A., & Zhao, Y. (2023) · Current Biology · doi:10.1016/j.cub.2023.10.064 · Cited by 22 · see citing works
Cross-talk between α-synuclein and the microtubule cytoskeleton in neurodegeneration
Mazzetti, S., Calogero, A. M., Pezzoli, G., & Cappelletti, G. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114251 · Cited by 22 · see citing works
Bayliak, M. M., Gospodaryov, D. V., & Lushchak, V. I. (2023) · BBA Advances · doi:10.1016/j.bbadva.2023.100077 · Cited by 22 · see citing works
Peripheral neuropathy in mitochondrial disease
Horváth, R., Medina, J. M., Reilly, M. M., Shy, M. E., & Zuchner, S. L. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-12-821751-1.00014-2 · Cited by 22 · see citing works
Genetic risk factors underlying white matter hyperintensities and cortical atrophy
Patel, Y., Shin, J., Sliz, E., Tang, A., Mishra, A., Xia, R., Hofer, E., Rajula, H., Wang, R.-Q., Beyer, F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53689-1 · Cited by 17 · see citing works
Molecular Motors in Blood–Brain Barrier Maintenance by Astrocytes
Sobral, A. F., Costa, I. D., Teixeira, V., Silva, R., & Barbosa, D. J. (2025) · Brain Sciences · doi:10.3390/brainsci15030279 · Cited by 21 · see citing works
Ataxin-2 is essential for cytoskeletal dynamics and neurodevelopment in Drosophila
del Castillo, U., Norkett, R., Lü, W., Serpinskaya, A. S., & Gelfand, V. I. (2021) · iScience · doi:10.1016/j.isci.2021.103536 · Cited by 21 · see citing works
Phosphoregulation of Kinesins Involved in Long-Range Intracellular Transport
Kumari, D., & Ray, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.873164 · Cited by 21 · see citing works
The role of the endolysosomal pathway in α-synuclein pathogenesis in Parkinson’s disease
Smith, J. K., Mellick, G. D., & Sykes, A. M. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1081426 · Cited by 20 · see citing works
MINFLUX reveals dynein stepping in live neurons
Schleske, J. M., Hubrich, J., Wirth, J. O., D’Este, E., Engelhardt, J., & Hell, S. W. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2412241121 · Cited by 17 · see citing works
Coordination between Transport and Local Translation in Neurons
Broix, L., Turchetto, S., & Nguyen, L. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.01.001 · Cited by 19 · see citing works
Optimizing mitochondrial maintenance in extended neuronal projections
Agrawal, A., & Koslover, E. F. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009073 · Cited by 20 · see citing works
Health Policies and Black Americans
Willis, D. P. (1988) · DigitalGeorgetown (Georgetown University Library) · Cited by 20 · see citing works
Sleigh, J. N., Mech, A. M., Aktar, T., Zhang, Y., & Schiavo, G. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00232 · Cited by 19 · see citing works
An adult-stage transcriptional program for survival of serotonergic connectivity
Kitt, M. M., Tabuchi, N., Spencer, W. C., Robinson, H. L., Zhang, X. L., Eastman, B., Lobur, K. J., Silver, J., Mei, L., & Deneris, E. S. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110711 · Cited by 19 · see citing works
Suh, B. K., Lee, S., Park, C., Suh, Y., Kim, S. J., Woo, Y. S., Nhung, T. T. M., Lee, S. B., Mun, D. J., Goo, B. S., et al. (2021) · Molecular Brain · doi:10.1186/s13041-020-00720-3 · Cited by 18 · see citing works
Song, N., Fang, Y., Zhu, H. Y., Liu, J., Jiang, S., Sun, S., Xu, R. H., Ding, J., Hu, G., & Lu, M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102168 · Cited by 18 · see citing works
Taguchi, S., Nakano, J., Imasaki, T., Kita, T., Saijo‐Hamano, Y., Sakai, N., Shigematsu, H., Okuma, H., Shimizu, T., Nitta, E., et al. (2022) · eLife · doi:10.7554/elife.77877 · Cited by 18 · see citing works
Alzheimer’s disease: an axonal injury disease?
Liang, D., & Zhang, Z. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1264448 · Cited by 18 · see citing works
Yang, X., Ma, Z., Lian, P., Wu, Y., Liu, K., Zhang, Z., Tang, Z., Xu, Y. C., & Cao, X. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-00926-z · Cited by 17 · see citing works
Structural Insights and Development of LRRK2 Inhibitors for Parkinson’s Disease in the Last Decade
Thakur, G., Kumar, V., Lee, K. W., & Won, C. (2022) · Genes · doi:10.3390/genes13081426 · Cited by 17 · see citing works
Lin, S., Leitao, A. D. G., Fang, S., Gu, Y., Barber, S., Gilliard-Telefoni, R., Castro, A., Sung, K., Shen, R., Florio, J. B., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106010 · Cited by 17 · see citing works
Low Forces Push the Maturation of Neural Precursors into Neurons
Vincentiis, S. D., Baggiani, M., Merighi, F., Cappello, V., Lopane, J., Caprio, M. D., Costa, M., Mainardi, M., Onorati, M., & Raffa, V. (2023) · Small · doi:10.1002/smll.202205871 · Cited by 17 · see citing works
Presynaptic Precursor Vesicles—Cargo, Biogenesis, and Kinesin-Based Transport across Species
Petzoldt, A. (2023) · Cells · doi:10.3390/cells12182248 · Cited by 11 · see citing works
- Authors
- Guedes-Dias, P., & Holzbaur, E. L. F.
- Affiliations
- Technical University of Munich (DE)
- University of Pennsylvania (US)
- Corresponding author
- Holzbaur, Erika L. F.
- Venue
- Science
- Published
- 2019-10-11
- Volume
- 366
- Issue
- 6462
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC6996143
- OpenAlex
- W2979904465
- Cited by
- 355
- References
- 199
- Citations by year
- 2026: 43 · 2025: 65 · 2024: 61 · 2023: 43 · 2022: 63 · 2021: 44 · 2020: 31 · 2019: 3
- FWCI
- 4.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (R35 GM126950)
- Alexander von Humboldt-Stiftung
- Deutsche Forschungsgemeinschaft (EXC 2145 SyNergy)
- Elite Network Bavaria
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- axonal transport, kinesin motors, dynein motor, microtubules, vesicle trafficking, presynaptic terminals, synaptic function, synaptic transmission, growth factor transport, protein aggregation, learning and memory
- MeSH terms
- Animals, Axonal Transport, Humans, Microtubules, Protein Processing, Post-Translational, Synapses, Tubulin, Protein Isoforms, Mice
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
