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Kinesin and Dynein Superfamily Proteins and the Mechanism of Organelle Transport

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Characterization of a cis-Golgi matrix protein, GM130.

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Altered microtubule organization in small-calibre axons of mice lacking tau protein

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The neuron-specific kinesin superfamily protein KIF1A is a uniqye monomeric motor for anterograde axonal transport of synaptic vesicle precursors

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Microtubules and the endoplasmic reticulum are highly interdependent structures.

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A novel brain ATPase with properties expected for the fast axonal transport motor

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KIF1B, a novel microtubule plus end-directed monomeric motor protein for transport of mitochondria

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Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites.

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The Role of Trim58 in Erythropoiesis

Thom, C. S. (2014) · ScholarlyCommons (University of Pennsylvania)

Vererbung und Positionierung von Mitochondrien: Analyse der Interaktion von Mitochondrien mit Mikrotubuli im filamentösen Pilz Neurospora crassa

Fuchs, F. (2004)

NEURONAL MITOCHONDRIAL TRANSPORT AND TURNOVER VIA MITOPHAGY

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Adenovirus Evasion of Cell-Intrinsic Immunity

Burrage, A. M. (2016) · Loyola eCommons (Loyola University of Chicago)

Effects of oocyte bisphenol A exposure on aspects of oocyte maturation and early embryo development in Bos taurus

Ferris, J. (2015) · The Atrium (University of Guelph)

Characterization of PGAM5

Wilkins, J. M. (2013) · MOspace Institutional Repository (University of Missouri) · doi:10.32469/10355/44044

Asymmetric metabolism by sibling lymphocytes coupling differentiation and self-renewal

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Defective Dynamics Of Mitochondria In Amyotrophic Lateral Sclerosis And Huntington's Disease

Song, W. (2012) · Journal of International Crisis and Risk Communication Research

Mitochondrial Remodeling During Hyperosmotic Stress

Zulys, M. (2009) · TSpace (University of Toronto)

Desvendando as bases moleculares da síndrome SPOAN: deleção em homozigose em região regulatória leva à superexpressão do gene KLC2

Melo, U. S. (2017) · doi:10.11606/t.41.2017.tde-13122016-105746

Unravelling motor protein organization on lysosomal membranes with super-resolution microscopy

Cordier, G. A. (2018) · UPCommons institutional repository (Universitat Politècnica de Catalunya) · doi:10.5821/dissertation-2117-117629

Study of a kinesin adaptor in axonal transport and synapse formation

Dehaghi, T. K. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7310

A Novel Kinesin Adapter Directly Mediates Dendritic mRNA Localization During Synapse Development

Wu, H. (2019) · CUNY Academic Works (City University of New York)

Altered mitochondrial dynamics in a novel cellular model of Leber Hereditary Optic Neuropathy (LHON)

Halangoda, K. (2018) · Summit (Simon Fraser University)

Mitochondria and Neurodegenerative Diseases

Johri, A., & Chandra, A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11474-6

Role of Usp9X in the Regulation of Axon Specification and Growth

Tan, M. C. (2015) · Griffith Research Online · doi:10.25904/1912/379

Mechanisms Regulating Movement and Distribution of Neuronal Mitochondria

Basu, H. (2020) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)

Mitochondrial ATP Synthase Trafficking along Microtubules to Cell Surface Depends on KIF5B and DRP1Preprint

Chang, Y., Yang, T. T., Chen, M., Liaw, Y.-G., Yin, C.-F., Huang, T.-Y., Hou, J.-T., Hung, Y.-H., Hsu, C., Huang, H., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.23.352385

A Review on the Mechanisms of Mitochondrial Dynamics and the Relationship with Neurodegeneration

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Митоптоз, двадцать лет спустя

Лямзаев, К. Г., Кнорре, Д. А., & Черняк, Б. В. (2020) · Biochemistry (Moscow) · doi:10.31857/s0320972520120027

Air plasma-activated medium exerts tumor-specific cytotoxicity via the oxidative stress-induced perinuclear mitochondrial clusteringPreprint

Suzuki‐Karasaki, M., Ando, T., Ochiai, Y., Kawahara, K., Suzuki‐Karasaki, M., Nakayama, H., & Suzuki‐Karasaki, Y. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.31.466636

Mitochondrial Organization and Transport in Neurons

Glater, E. E., & Schwarz, T. L. (2009) · Elsevier eBooks · doi:10.1016/b978-008045046-9.00734-8

Faculty Opinions recommendation of Bicaudal D induces selective dynein-mediated microtubule minus end-directed transport.

Davis, I. (2003) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1016534.200900

Conformational state of monomeric kinesin UNC-104

Henschel, V. C. (2012) · doi:10.53846/goediss-3523

Dynein and Kinesin

Bowman, A. B., & Goldstein, L. S. B. (2001) · Encyclopedia of Life Sciences · doi:10.1038/npg.els.0000677

Mitochondrial Dynamics: The Control of Mitochondrial Shape, Size, Number, Motility, and Cellular Inheritance

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Transient transfection permits analysis of mismatch repair genes

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Faculty Opinions recommendation of Miro1-mediated mitochondrial positioning shapes intracellular energy gradients required for cell migration.

Insall, R. H. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727719956.793567183

Faculty Opinions recommendation of Kinesin-1 and Dynein are the primary motors for fast transport of mitochondria in Drosophila motor axons.

Akhmanova, A. S. (2006) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1031329.368707

Further Reading | Kinesin Superfamily Proteins

Hirokawa, N., Tanaka, Y., & Takemura, R. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00301-7

Kinesins, Human

Rogers, K. R., & Cross, R. A. (2002) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm0009

The Expanding Universe of Kinesin Superfamily Molecular Motors (KIFs) – The Postmen Who Govern the Country

Tanaka, Y. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00177-2

Neurons

Dehorter, N., & Hammond, C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-98811-7.00001-1

Molecular Motors, Micro-Transporters in the Cell are Fundamental for the Life

Hirokawa, N. (2024) · Transactions of the Japan Academy · doi:10.2183/tja.78.3_235

Motor protein KIF5B inhibition as a novel strategy of controlled reperfusion against myocardial ischemia/reperfusion injury

Gao, F., Zhang, Y., Jin, L., Gong, H., Zhang, X., Zheng, Q., Chen, Z., & Qin, X. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167785

High level dynein impairs mitochondrial distribution and differentiation of rhabdomyosarcoma cells

Ke, T.-L., & Chen, L. (2026) · iScience · doi:10.1016/j.isci.2026.116057

The molecular control of cell movements during early vertebrate development

Ewald, A. J. (2003) · doi:10.7907/67z0-h535

Additional file 1 of Normal levels of KIF5 but reduced KLC1 levels in both Alzheimer disease and Alzheimer disease in Down syndrome: evidence suggesting defects in anterograde transport

Chen, X.-Q., Das, U., Park, G., & Mobley, W. C. (2021) · Figshare · doi:10.6084/m9.figshare.14196547

Additional file 1 of Static magnetic field-modulated mesenchymal stem cell-derived mitochondria-containing microvesicles for enhanced intervertebral disc degeneration therapy

Shi, P., Gao, H., Cheng, Z., Zhao, K., Chen, Y., Chen, X., Gan, W., Zhang, A., Yang, C., & Zhang, Y. (2024) · Figshare · doi:10.6084/m9.figshare.26420361

Liver Disease Reveals KIF12 as a Critical Regulator of Mitochondria, Lysosome and Cilia LocalizationPreprint

Seth, A., Brancale, J., Dashti-Gibson, N. M., Florentino, R. M., Faccioli, L. A. P., Liu, Z., Konkwo, C., Hong, H., Soto–Gutiérrez, A., & Vilarinho, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.24.707575

Importance du contrôle qualité des mitochondries dans les maladies neurodégénératives : analyse cellulaire et génétique dans des modèles drosophile de la maladie de Huntington et de la sclérose latérale amyotrophique

Khalil, B. (2016) · theses.fr (ABES) · doi:10.70675/4446111fz4182z4737zae76z7f117887a893

Pince optique et microscopie à contraste de phase pour l'étude de la mécanique cellulaire : développement, modélisation et calibration en réflexion.

Gillant, F. (2016) · doi:10.70675/aaebbb95zd9f2z461az9eecz08cbb747c2bf

The role of lysosome alterations in bladder cancer progression

Santos, C. D. B. (2017) · theses.fr (ABES) · doi:10.70675/db736cc6z1bdaz49caza113z778f80e168ba

The role of PKD in mitochondrial fission during mitosis

Bielska, O. (2018) · theses.fr (ABES) · doi:10.70675/2dbab59fze200z4e37z9770zea1c8f1345ea

Rôle de la dérégulation neuronale de la protéine kinase activée par l’AMP (AMPK) dans la pathologie tau, l’intégrité des synapses et le métabolisme énergétique : relevance pour la maladie d’Alzheimer

Domise, M. (2018) · theses.fr (ABES) · doi:10.70675/43c1f12fze623z41e8z970fz64a5de94a299

Développement d’une méthode de mesure et d’analyse du transport intraneuronal dans le cerveau de larve de poissons-zèbre par suivi de nanocristaux non-linéaires en microscopie de second-harmonique : application à l’étude d’anomalies de transport chez des poissons portant une mutation retrouvée dans des neuropathies humaines.

Terras, F. (2020) · doi:10.70675/872df6d1ze1b9z4a8dzb02dzad4656ff10f0

Importance of host molecular motors in Salmonella enterica virulence

Fang, Z. (2021) · theses.fr (ABES) · doi:10.70675/e12d5606z0b45z4eadzb9bcz19139d305022

Targeting AVEN Liquid‐Liquid Phase Separation in Colorectal Cancer: Insights From a Raddeanin A‐Based Chemical Probe

Yu, X., Wu, H., Guo, K., Liu, Z., Zhou, L., Wu, H., Wang, S., Fu, J., Cui, X., Fu, Z., et al. (2026) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.70257

Traffic Jams in the Brain: How Kinesin Dysfunction Shapes Neurodevelopmental Disorders

Nosrati, M. S. S., Doustmohammadi, M., Dostmohammadi, A., Hamidi, A. K., Boogari, M., Tavassol, Z. H., Khosravinejat, S., Asgari, M., Shafiei, M., Nemati, A. H., et al. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48080837

KIF24 depletion induces Fe–S-dependent mitochondrial dysfunction and AMPK/p53/SLC7A11 mediated ferroptosis in gastric cancerPreprint

Liu, J.-B., Zhu, H.-X., Gu, C.-Y., Yu, Q. Y., Shao, J.-J., Song, L., & Wu, Y. (2026) · Research Square · doi:10.21203/rs.3.rs-10011659/v1

A systems-level proteomic analysis identifies kinesin targets of KIFBP during neuronal developmentPreprint

Paschall, S., Blasius, T. L., Missman, A., Rodriguez, P., Cianfrocco, M. A., Verhey, K. J., & Stumpff, J. K. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.17.739260

Mitochondrial molecular diversity in the brain

Sainz, A. G., & Wang, X. (2026) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2026.103270

Liver disease reveals KIF12 as a regulator of mitochondria, lysosome and cilia localisation in human cholangiocytes

Seth, A., Brancale, J., Dashti-Gibson, N. M., Florentino, R. M., Faccioli, L. A. P., Liu, Z., Konkwo, C., Hong, H., Soto–Gutiérrez, A., & Vilarinho, S. (2026) · EBioMedicine · doi:10.1016/j.ebiom.2026.106474 · Cited by 1

Serum Response Factor and Actin Treadmilling Influence Neuronal Mitochondrial Dynamics

Beck, H. (2012)

A) Mitochondrial perinuclear clustering (a consequence of defective trafficking) results from siRNA-mediated knockdown of KIF5B, but not of KIF11

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Functional Analysis Of Mouse Conventional Kinesin Heavy Chain,KIF5B,Using Gene Targeting

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Tangled yet in tune: Orchestrating the dynamics of microtubules, vimentin and endoplasmic reticulum

Pasolli, M. (2025) · doi:10.33540/3164

Defective kinesin heavy chain behavior in mouse kinesin light chain mutants

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Defective Kinesin Heavy Chain Behavior in Mouse Kinesin Light

Mutants, C., & Kamal, A. R. A. (2013)