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Synaptic vesicle recycling: steps and principles
Open accessAbstract
Synaptic vesicle recycling is one of the best-studied cellular pathways. Many of the proteins involved are known, and their interactions are becoming increasingly clear. However, as for many other pathways, it is still difficult to understand synaptic vesicle recycling as a whole. While it is generally possible to point out how synaptic reactions take place, it is not always easy to understand what triggers or controls them. Also, it is often difficult to understand how the availability of the reaction partners is controlled: how the reaction partners manage to find each other in the right place, at the right time. I present here an overview of synaptic vesicle recycling, discussing the mechanisms that trigger different reactions, and those that ensure the availability of reaction partners. A central argument is that synaptic vesicles bind soluble cofactor proteins, with low affinity, and thus control their availability in the synapse, forming a buffer for cofactor proteins. The availability of cofactor proteins, in turn, regulates the different synaptic reactions. Similar mechanisms, in which one of the reaction partners buffers another, may apply to many other processes, from the biogenesis to the degradation of the synaptic vesicle.
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“The precise mechanisms that govern the number of vesicles undergoing exo- or endocytosis, ensuring efficient resource allocation and preventing membrane imbalances, are still subjects of active investigation [23].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [23]
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Cites
Functional rafts in cell membranes
Simons, K., & Ikonen, E. (1997) · Nature · doi:10.1038/42408 · Cited by 9,757 · cited 1×
“Just as in the ER, the proteins diffuse to proteolipid patches, and may form partially stable protein/lipid assemblies (as described for the plasma membrane (Simons & Ikonen, 1997)).”
Rab GTPases as coordinators of vesicle traffic
Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413
Rab proteins as membrane organizers
Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381
Phosphoinositides in cell regulation and membrane dynamics
Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790
SNAREs — engines for membrane fusion
Jahn, R., & Scheller, R. H. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2002 · Cited by 2,635
Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
Miesenböck, G., Angelis, D. A. D., & Rothman, J. E. (1998) · Nature · doi:10.1038/28190 · Cited by 2,569
Südhof, T. C. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131412 · Cited by 2,491
Wilschut, J. (1990) · Cited by 2,407
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
Molecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223
Flagged first, then by citations
2 of the 387 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Plato (1997) Phaedrus. Transl. by Alexander Nehamas and Paul Woodruff. In Complete Works, Cooper J, Hutchinson D (ed.), pp 507–556. Indianapolis: Hackett Publishing Co
- Virchow R (1862) Die Cellularpathologie, in Ihrer Begründung auf Physiologische und Patologische Gewebelehre. Berlin: Hirschwald, pp 1–25
Cited by
Sorted by citations
Items 101–200 of 317
Molecular architecture of synaptic vesicles
Kravčenko, U., Ruwolt, M., Kroll, J., Yushkevich, A., Zenkner, M., Ruta, J., Lotfy, R., Wanker, E. E., Rosenmund, C., Liu, F., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2407375121 · Cited by 33
Brain‐specific functions of the endocytic machinery
Camblor‐Perujo, S., & Kononenko, N. L. (2021) · FEBS Journal · doi:10.1111/febs.15897 · Cited by 33
Functional Role of ATP Binding to Synapsin I In Synaptic Vesicle Trafficking and Release Dynamics
Orlando, M., Lignani, G., Maragliano, L., Fassio, A., Onofri, F., Baldelli, P., Giovedı̀, S., & Benfenati, F. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1093-14.2014 · Cited by 29
Parthier, D., Kuner, T., & Körber, C. (2017) · The Journal of Physiology · doi:10.1113/jp274885 · Cited by 29
The effects of proteasome on baseline and methamphetamine-dependent dopamine transmission
Limanaqi, F., Biagioni, F., Busceti, C. L., Ryskalin, L., & Fornai, F. (2019) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2019.05.008 · Cited by 29
The HERC proteins and the nervous system
Pérez-Villegas, E. M., Ruiz, R., Bachiller, S., Ventura, F., Armengol, J. A., & Rosa, J. L. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.11.017 · Cited by 32
Wang, C., Zhao, D., Shah, S. Z. A., Yang, W., Li, C., & Yang, L. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0029-6 · Cited by 27
Significance of chromogranin A and synaptophysin in pancreatic neuroendocrine tumors
Tomita, T. (2020) · Bosnian Journal of Basic Medical Sciences · doi:10.17305/bjbms.2020.4632 · Cited by 27
Mechanisms of Synaptic Vesicle Exo- and Endocytosis
Mochida, S. (2022) · Biomedicines · doi:10.3390/biomedicines10071593 · Cited by 31
Brereton, E., Fassi, E., Araujo, G. C., Dodd, J. N., Telegrafi, A. B., Pathak, S., & Shinawi, M. S. (2018) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.362 · Cited by 26
Yu, S.-C., Jánosi, B., Liewald, J. F., Wabnig, S., & GOTTSCHALK, A. R. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00196 · Cited by 28
Zakyrjanova, G. F., Tsentsevitsky, A. N., Kuznetsova, E. A., & Petrov, A. M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.08.013 · Cited by 26
Rentsch, D., Schneider, M., Goulden, B. D., Dill, H., Liewald, J. F., Zeiler, S., Guldan, J., Ateş, Y. A., Watanabe, S., & GOTTSCHALK, A. R. (2022) · Nature Communications · doi:10.1038/s41467-022-35324-z · Cited by 30
Quantitative analysis of vesicle recycling at the calyx of Held synapse
Qiu, X., Zhu, Q., & Sun, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1424597112 · Cited by 27
Neurotransmitter Release Site Replenishment and Presynaptic Plasticity
Mochida, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010327 · Cited by 26
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Singh, A., Verma, S., Modak, S. B., Chaturvedi, M. M., & Purohit, J. S. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04300-4 · Cited by 23
Latina, V., Caioli, S., Zona, C., Ciotti, M. T., Borreca, A., Calissano, P., & Amadoro, G. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00487 · Cited by 26
Fusion assays for model membranes: a critical review
Lira, R. B., & Dimova, R. (2019) · Advances in biomembranes and lipid self-assembly · doi:10.1016/bs.abl.2019.09.003 · Cited by 24
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Abbott, J., Ye, T., Krenek, K., Gertner, R. S., Wu, W., Jung, H. S., Ham, D., & Park, H. (2020) · Lab on a Chip · doi:10.1039/d0lc00553c · Cited by 25
Brill, S. E., Maraslioglu-Sperber, A., Kurz, C., Kramer, F., Fuhr, M. F., Singh, A., & Friauf, E. (2021) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2020.560008 · Cited by 23
Lange, F., Agüi‐Gonzalez, P., Riedel, D., Phan, N. T. N., Jakobs, S., & Rizzoli, S. O. (2021) · PLoS ONE · doi:10.1371/journal.pone.0240768 · Cited by 23
Self-citationGFP nanobodies reveal recently-exocytosed pHluorin molecules
Seitz, K. J., & Rizzoli, S. O. (2019) · Scientific Reports · doi:10.1038/s41598-019-44262-8 · Cited by 22
Self-citationCyclosporine A (CsA) prevents synaptic impairment caused by truncated tau by caspase-3
Tapia-Monsalves, C., Olesen, M. A., Villavicencio-Tejo, F., & Quintanilla, R. A. (2023) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2023.103861 · Cited by 24
Jantrapirom, S., Piccolo, L. L., Yoshida, H., & Yamaguchi, M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.06.017 · Cited by 23
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Fakhree, M. A. A., Konings, I. B. M., Kole, J., Cambi, A., Blum, C., & Claessens, M. M. A. E. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2021.01.017 · Cited by 22
Spontaneous vesicle recycling in the synaptic bouton
Truckenbrodt, S., & Rizzoli, S. O. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00409 · Cited by 24
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López-Murcia, F. J., Royle, S. J., & Llobet, A. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5081-13.2014 · Cited by 29
Zakirjanova, G. F., Gilmutdinov, A. I., Tsentsevitsky, А. N., & Petrov, A. M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158739 · Cited by 21
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Byczkowicz, N., Ritzau‐Jost, A., Delvendahl, I., & Hallermann, S. (2017) · Neuroscience Research · doi:10.1016/j.neures.2017.10.013 · Cited by 19
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Yamashita, M., Kawaguchi, S., Hori, T., & Takahashi, T. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.02.080 · Cited by 24
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Suresh, S., Verma, V., Sateesh, S., Clement, J. P., & Manjithaya, R. R. (2018) · Journal of Genetics · doi:10.1007/s12041-018-0955-3 · Cited by 22
Richter, K. N., Wildhagen, H., Helm, M. S., Ußling, J., Schikorski, T., & Rizzoli, S. O. (2018) · Scientific Reports · doi:10.1038/s41598-018-33130-6 · Cited by 22
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Imler, E., Pyon, J. S., Kindelay, S. M., Torvund, M., Zhang, Y.-Q., Chandra, S. S., & Zinsmaier, K. E. (2019) · eLife · doi:10.7554/elife.46607 · Cited by 17
Endosomal phosphatidylinositol 3-phosphate controls synaptic vesicle cycling and neurotransmission
Liu, G., Kochlamazashvili, G., Puchkov, D., Müller, R., Schultz, C., Mackintosh, A. I., Vollweiter, D., Haucke, V., & Soykan, T. (2022) · The EMBO Journal · doi:10.15252/embj.2021109352 · Cited by 19
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Yagensky, O., Dehaghi, T. K., & Chua, J. J. E. (2016) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2016.00003 · Cited by 20
Wihan, J., Grosch, J., Kalinichenko, L. S., Müller, C. P., Winkler, J., & Kohl, Z. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.03.014 · Cited by 19
Kang, C., & Sun, R. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c08620 · Cited by 20
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Peng, Y.-J., Geng, J., Wu, Y. T., Pinales, C., Langen, J., Chang, Y.-C., Buser, C., & Chang, K. T. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202011028 · Cited by 15
Mondal, D., Ghosh, A. K., Paul, I., & Schmittel, M. (2021) · Organic Letters · doi:10.1021/acs.orglett.1c03654 · Cited by 15
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Perego, E., Reshetniak, S., Lorenz, C., Hoffmann, C., Milovanović, D., Rizzoli, S. O., & Köster, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-77887-1 · Cited by 16
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Touahri, Y., Hanna, J., Tachibana, N., Okawa, S., Liu, H., David, L. A., Olender, T., Vasan, L., Pak, A., Mehta, D. N., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114005 · Cited by 14
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Dong, B., Liu, L., & Hu, C. (2018) · Biomacromolecules · doi:10.1021/acs.biomac.8b00769 · Cited by 14
Vitet, H., Bruyère, J., Xu, H., Séris, C., Brocard, J., Abada, Y.-S., Delatour, B., Scaramuzzino, C., Venance, L., & Saudou, F. (2023) · eLife · doi:10.7554/elife.81011 · Cited by 13
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Gormal, R. S., Valmas, N., Fath, T., & Meunier, F. A. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.04.003 · Cited by 11
Hu, Z., Liu, Z., Li, X., & Deng, X. (2017) · Scientific Reports · doi:10.1038/s41598-017-13764-8 · Cited by 13
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Faritovich, N. L., Khuzakhmetova, V. F., Khaziev, E. F., Samigullin, D. V., Tsentsevitsky, A. N., Skorinkin, A. I., Bukharaeva, E. A., & Vagin, O. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.01.060 · Cited by 13
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Reshetniak, S., Bogaciu, C. A., Bonn, S., Brose, N., Cooper, B. H., D’Este, E., Fauth, M. J., Fernández‐Busnadiego, R., Fiošins, M., Fischer, A., et al. (2024) · The Journal of Physiology · doi:10.1113/jp286400 · Cited by 15
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David, S., Pinter, K. L., Nguyen, K., Lee, D. S., Lei, Z., Sokolova, Y., Sheets, L., & Kindt, K. S. (2024) · The Journal of Physiology · doi:10.1113/jp286263 · Cited by 11
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Fassio, A., Fadda, M., & Benfenati, F. (2016) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2016.00010 · Cited by 11
Terni, B., Pacciolla, P., Masanas, H., Gorostiza, P., & Llobet, A. (2017) · The Journal of Comparative Neurology · doi:10.1002/cne.24303 · Cited by 11
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Nunes, P. T., Gómez‐Mendoza, D. P., Rezende, C. P., Figueiredo, H. C. P., & Ribeiro, A. M. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.06.003 · Cited by 11
Jin, W., Dai, Y., Li, F., Zhu, L., Huang, Z., Liu, W., Li, J., Zhang, M., Du, J., Zhang, W., et al. (2019) · iScience · doi:10.1016/j.isci.2019.02.031 · Cited by 10
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Chakraborty, K., Anees, P., Surana, S., Martin, S., Aburas, J., Moutel, S., Perez, F., Koushika, S. P., Kratsios, P., & Krishnan, Y. (2021) · eLife · doi:10.7554/elife.67830 · Cited by 11
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Sharma, A., Sah, N., Sharma, R. B., Vyas, P., Liyanage, W., Kannan, S., & Kannan, R. M. (2024) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10655 · Cited by 10
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Tomita, T. (2020) · Bosnian Journal of Basic Medical Sciences · doi:10.17305/bjbms.2020.5407 · Cited by 10
Heredia, D. J., Feng, C.-Y., Agarwal, A. B., Nennecker, K., Hennig, G. W., & Gould, T. W. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0956-18.2018 · Cited by 12
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Ganzella, M., Ninov, M., Riedel, D., & Jahn, R. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1916-2_11 · Cited by 9
Eich, M., Dembla, E., Wahl, S., Dembla, M., Schwarz, K., & Schmitz, F. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00230 · Cited by 10
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Sabeva, N. S., Cho, R. W., Vasin, A., Gonzalez, A., Littleton, J. T., & Bykhovskaia, M. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1854-16.2016 · Cited by 9
Akula, A. K., Zhang, X., Viotti, J., Nestvogel, D., Rhee, J., Ebrecht, R., Reim, K., Wouters, F. S., Liepold, T., Jahn, O., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00249 · Cited by 9
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Self-citationOuyang, X., Wu, B., Yu, H., & Dong, B. (2023) · Biological Research · doi:10.1186/s40659-023-00422-9 · Cited by 8
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Huang, M., Darvas, M., Keene, C. D., & Wang, Y. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b02485 · Cited by 8
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Jiang, Z., & Gong, L. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1494-22.2023 · Cited by 8
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Ríos, H., Paganelli, A. R., & Fosser, N. S. (2020) · The Journal of Comparative Neurology · doi:10.1002/cne.24855 · Cited by 8
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Spencer, R. K. W., Smirnova, Y. G., Soleimani, A., & Müller, M. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.06.009 · Cited by 7
Bohler, S., Krauskopf, J., Espín-Pérez, A., Gebel, S., Palli, D., Rantakokko, P., Kiviranta, H., Kyrtopoulos, S. Α., Balling, R., & Kleinjans, J. C. S. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.04.005 · Cited by 7
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“The precise mechanisms that govern the number of vesicles undergoing exo-or endocytosis, ensuring the efficient allocation of cellular resources, are still subjects of active investigation [23].”
InfluentialA role for synapsin tetramerization in synaptic vesicle clustering
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Wilson, P., Kim, N., Cotter, R., Parkes, M., Cmelak, L., Reed, M. N., & Gramlich, M. W. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115410 · Cited by 7
Atwa, A., Alhadidy, M. M., Lamp, J. A., Combs, B., & Kanaan, N. M. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00473 · Cited by 6
Parkes, M., Landers, N., & Gramlich, M. W. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1286915 · Cited by 4
Vahdat, Z., Gambrell, O., Fisch, J. O., Friauf, E., & Singh, A. (2025) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1013067 · Cited by 7
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Saal, K. A., Arias, C. C. W. P., Roser, A., Koch, J. C., Bähr, M., Rizzoli, S. O., & Lingor, P. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15274 · Cited by 6
Self-citationIntracellular Acidification Suppresses Synaptic Vesicle Mobilization in the Motor Nerve Terminals
Zefirov, A. L., Mukhametzyanov, R. D., Zakharov, A., Mukhutdinova, K. A., Odnoshivkina, Y. G., & Petrov, A. M. (2020) · Acta Naturae · doi:10.32607/actanaturae.11054 · Cited by 6
Atomistic Insight into the Lipid Nanodomains of Synaptic Vesicles
Kang, C., Fujioka, K., & Sun, R. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c07982 · Cited by 6
Huang, L., Wickramasekara, S. I., Akinyeke, T. O., Stewart, B., Jiang, Y., Raber, J., & Maier, C. S. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.03.032 · Cited by 6
Lam, C. S., Tipoe, G. L., Wong, J. K.-C., Youdim, M. B. H., & Fung, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166966 · Cited by 6
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Self-citationSpastin locally amplifies microtubule dynamics to pattern the axon for presynaptic cargo deliveryPreprint
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Wal, P., Dutta, A., Jawaid, T., Rahman, M. U., Gowri, K., Jyothi, S. R., Kaur, I., Al-Hasnaawei, S., Sinha, A., Maharana, L., et al. (2026) · Biogerontology · doi:10.1007/s10522-026-10394-4 · Cited by 4
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Metadata
- Authors
- Rizzoli, S. O.
- Affiliations
- Universitätsmedizin Göttingen (DE)
- Corresponding author
- Rizzoli, Silvio O
- ORCID
- Rizzoli, Silvio O
- Venue
- The EMBO Journal
- Published
- 2014-03-04
- Volume
- 33
- Issue
- 8
- Pages
- 788-822
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC4194108
- OpenAlex
- W2011652925
- Cited by
- 317
- References
- 387
- Citations by year
- 2026: 22 · 2025: 29 · 2024: 28 · 2023: 20 · 2022: 21 · 2021: 23 · 2020: 24 · 2019: 34 · 2018: 28 · 2017: 34 · 2016: 25 · 2015: 18 · 2014: 10
- FWCI
- 2.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- The EMBO Journal (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- GRO (submittedVersion, cc-by)
- Funders
- European Research Council (FP7)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- synaptic vesicle recycling, synaptic vesicle exocytosis, protein availability, synaptic vesicle biogenesis, synaptic vesicle fusion, protein-protein interaction
- MeSH terms
- Animals, Endocytosis, Exocytosis, Humans, Nerve Tissue Proteins, Neurons, Synaptic Vesicles, Metabolic Networks and Pathways
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