The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
SV2 Renders Primed Synaptic Vesicles Competent for Ca2+-Induced Exocytosis
Open accessAbstract
Synaptic vesicle protein 2 (SV2), one of the first synaptic vesicle proteins identified, is characterized by multiple transmembrane regions that exhibit homology to sugar transporters, and by a highly glycosylated intravesicular sequence. Deletion of SV2 causes postnatal lethality in mice, primarily because of fulminant epilepsy. At the cellular level, deletion of SV2 impairs neurotransmitter release, but its function is unknown, and even the exact point at which release is affected in SV2-deleted synapses remains unclear. Using electrophysiological approaches, we now examine at what step in exocytosis the deletion of SV2 impairs release. Our data demonstrate that deletion of SV2 produces a decrease in evoked synaptic responses without causing changes in mini frequency, mini amplitude, the readily releasable pool of vesicles, or the apparent Ca 2+sensitivity of vesicle fusion. These findings indicate that a previously unidentified step may couple priming of synaptic vesicles to Ca 2+triggering of fusion, and that SV2 acts in this step to render primed synaptic vesicles fully Ca 2+responsive. To investigate the structural requirements for this function of SV2, we used rescue experiments. We demonstrate that conserved charged residues within the transmembrane regions and the intravesicular glycosylation of SV2 are required for its normal folding and trafficking. In contrast, the conserved putative synaptotagmin-binding sequence of SV2 is fully dispensable. Viewed together, these observations suggest that SV2 functions in a maturation step of primed vesicles that converts the vesicles into a Ca 2+- and synaptotagmin-responsive state.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“SV2, a marker for mature synaptic vesicles and regulates presynaptic release (70, 71)”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [71]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
Südhof, T. C. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131412 · Cited by 2,491
Self-citationThe synaptic vesicle protein SV2A is the binding site for the antiepileptic drug levetiracetam
Lynch, B. A., Lambeng, N., Nocka, K., Kensel-Hammes, P., Bajjalieh, S. M., Matagne, A., & Fuks, B. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308208101 · Cited by 1,610
The release of neural transmitter substances
Katz, B. (1969) · Medical Entomology and Zoology · Cited by 1,126
Synaptotagmin I functions as a calcium regulator of release probability
Fernández-Chacón, R., Königstorfer, A., Gerber, S. H., García, J., Matos, M. F., Stevens, C. F., Brose, N., Rizo, J., Rosenmund, C., & Südhof, T. C. (2001) · Nature · doi:10.1038/35065004 · Cited by 961
Self-citationSV2 Is the Protein Receptor for Botulinum Neurotoxin A
Dong, M., Yeh, F. L., Tepp, W. H., Dean, C., Johnson, E. A., Janz, R., & Chapman, E. R. (2006) · Science · doi:10.1126/science.1123654 · Cited by 777
Buckley, K. M., & Kelly, R. B. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.4.1284 · Cited by 713
Differential expression of synaptic vesicle protein 2 (SV2) isoforms
Bajjalieh, S., Frantz, G., Weimann, J., McConnell, S., & Scheller, R. (1994) · The Journal of Neuroscience · doi:10.1523/jneurosci.14-09-05223.1994 · Cited by 440
Abnormal neurotransmission in mice lacking synaptic vesicle protein 2A (SV2A)
Crowder, K. M., Gunther, J. M., Jones, T. A., Hale, B. D., Zhang, H. Z., Peterson, M. R., Scheller, R. H., Chavkin, C., & Bajjalieh, S. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.15268 · Cited by 415 · cited 3×
“…synaptic transmission, the size of the pool of release-ready chromaffin secretory vesicles is decreased, and SNARE-complex assembly in brain may be impaired, suggesting that SV2A may function upstream of Ca 2 triggering in priming synaptic vesicles (Crowder et al., 1999; Xu and Bajjalieh, 2001).”
Background
Cited by
Sorted by citations
Items 101–175 of 175
Fronczak, K. M., Li, Y., Henchir, J., Dixon, C. E., & Carlson, S. W. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02534-3 · Cited by 18
Naujock, M., Speidel, A., Fischer, S. E., Kizner, V., Dorner‐Ciossek, C., & Gillardon, F. (2020) · Stem Cells and Development · doi:10.1089/scd.2020.0082 · Cited by 18
Bradberry, M. M., & Chapman, E. R. (2022) · The Journal of Physiology · doi:10.1113/jp282601 · Cited by 16
PET imaging of synaptic density in Parkinsonian disorders
Martin, S. L., Uribe, C., & Strafella, A. P. (2023) · Journal of Neuroscience Research · doi:10.1002/jnr.25253 · Cited by 19
Small, C., Harper, C., Jiang, A., Kontaxi, C., Pronot, M., Yak, N., Malapaka, A., Davenport, E. C., Wallis, T. P., Gormal, R. S., et al. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16186 · Cited by 14
Zhang, Y., Heylen, L., Partoens, M., Mills, J. D., Kaminski, R. M., Godard, P., Gillard, M. R., de Witte, P. A. M., & Siekierska, A. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.881933 · Cited by 14
Bucher, M. L., Dunn, A. R., Bradner, J. M., Egerton, K. S., Burkett, J. P., Johnson, M. A., & Miller, G. W. (2024) · European Journal of Neuroscience · doi:10.1111/ejn.16311 · Cited by 14
Anxiety-like features and spatial memory problems as a consequence of hippocampal SV2A expression
Navacerrada, M. E. S., Bartholomé, O., den Ackerveken, P. V., Ferrara, A., Rogister, B., Plenevaux, A., & Tirelli, E. (2019) · PLoS ONE · doi:10.1371/journal.pone.0217882 · Cited by 15
Li, Y., Li, S., Liu, J., Huo, Y., & Luo, X. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01261-4 · Cited by 13
Asch, R. H., Abdallah, C. G., Carson, R. E., & Esterlis, I. (2025) · Neuropsychopharmacology · doi:10.1038/s41386-024-01913-3 · Cited by 13
Benarroch, E. E. (2013) · Neurology · doi:10.1212/wnl.0b013e318293e3cd · Cited by 12
Levetiracetam Has Opposite Effects on Alcohol- and Cocaine-Related Behaviors in C57BL/6J Mice
Robinson, J. E., Chen, M., Stamatakis, A. M., Krouse, M. C., Howard, E. C., Faccidomo, S., Hodge, C. W., Fish, E. W., & Malanga, C. J. (2013) · Neuropsychopharmacology · doi:10.1038/npp.2013.30 · Cited by 13
The synaptic vesicle cluster as a controller of pre‐ and postsynaptic structure and function
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
Botermans, W., Koole, M. J. B., Laere, K. V., Savidge, J. R., Kemp, J. A., Sunaert, S. G., Duffy, M. M., Ramael, S., Cesura, A. M., D’Ostilio, K., et al. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1066447 · Cited by 13
Liebl, F. L. W., McKeown, C. L., Yao, Y., & Hing, H. K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012778 · Cited by 13
The Molecular Mechanisms Underlying Synaptic Transmission
Ashery, U., Bielopolski, N., Lavi, A., Barak, B., Michaeli, L., Ben‐Simon, Y., Sheinin, A., Bar-On, D., Shapira, Z., & Gottfried, I. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-418675-0.00002-x · Cited by 13
Non-VMAT2 inhibitor treatments for the treatment of tardive dyskinesia
Lin, C.-C., & Ondo, W. G. (2018) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2018.02.014 · Cited by 12
Mechanisms of Antiepileptic Drug Action
Walker, M. C., & Fisher, A. (2004) · doi:10.1002/9780470752463.ch9 · Cited by 12
SV2B defines a subpopulation of synaptic vesicles
Paulußen, I., Beckert, H., Musial, T. F., Gschossmann, L. J., Wolf, J., Schmitt, M., Clasadonte, J., Mairet‐Coello, G., Wolff, C., Schoch, S., et al. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad054 · Cited by 13
Harada, S., Tanaka, S., Takahashi, Y., Matsumura, H., Shimamoto, C., Nakano, T., Kuwabara, H., Sawabe, Y., & Nakahari, T. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.09.037 · Cited by 11
Pozdnyakova, N., Dudarenko, M., & Borisova, Т. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00676-6 · Cited by 11
Kaltwaßer, B., Schulenborg, T., Beck, F., Klotz, M., Schäfer, K., Schmitt, M., Sickmann, A., & Friauf, E. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.11.018 · Cited by 11
Song, S.-Y., Chae, M., Yu, J. H., Lee, M. Y., Pyo, S., Shin, Y., Baek, A., Park, J., Park, E. S., Choi, J. Y., et al. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00465 · Cited by 11
Zhou, J., Liang, W., Wang, J., Chen, J., Liu, D., Wang, X., Wu, Y., Zhang, Q., & Shen, D. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab338 · Cited by 11
Vega, A., Cancino-Rodezno, A., Valle‐Leija, P., Sánchez-Tafolla, B. M., Elinos, D., Cifuentes, F., & Morales, M. A. (2015) · Developmental Neurobiology · doi:10.1002/dneu.22362 · Cited by 11
Pichardo‐Macías, L. A., Contreras‐García, I. J., Zamudio, S., Mixcoha, E., & Mendoza‐Torreblanca, J. G. (2016) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-6355-3_4 · Cited by 11
A presynaptic congenital myasthenic syndrome attributed to a homozygous sequence variant in LAMA5
Maselli, R. A., Arredondo, J., Vázquez, J., Chong, J. X., Bamshad, M. J., Nickerson, D. A., Lara, M., Ng, F., Lo, V. L., Pytel, P., et al. (2018) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13585 · Cited by 11
Benner, O., Cast, T. P., Minamide, L. S., Lenninger, Z., Bamburg, J. R., & Chanda, S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105361 · Cited by 12
Loss of the SV2-like Protein SVOP Produces No Apparent Deficits in Laboratory Mice
Yao, J., de la Iglesia, H. O., & Bajjalieh, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068215 · Cited by 9
Antiepileptogenesis, Plasticity of AED Targets, Drug Resistance, and Targeting the Immature Brain
Beck, H., & Yaari, Y. (2012) · Oxford University Press eBooks · doi:10.1093/med/9780199746545.003.0083 · Cited by 9
Levetiracetam Affects Differentially Presynaptic Proteins in Rat Cerebral Cortex
Marcotulli, D., Fattorini, G., Bragina, L., Perugini, J., & Conti, F. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00389 · Cited by 9
Ma, Y., Gao, K., Sun, X., Wang, J., Yang, Y., Wu, J., Chai, A., Li, Y., Liu, N., Yu, H., et al. (2024) · 中国科学通报：英文版 · doi:10.1016/j.scib.2024.02.013 · Cited by 9
MacLeod, K. M., & Horiuchi, T. K. (2011) · Biological Cybernetics · doi:10.1007/s00422-011-0428-8 · Cited by 8
Mechanisms of Antiepileptic Drug Action
Walker, M. C., Surges, R., & Fisher, A. (2009) · doi:10.1002/9781118936979.ch6 · Cited by 8
Synaptic Vesicle Glycoprotein 2C: a role in Parkinson’s disease
Chang, C. H., Lim, K. L., & Foo, J. N. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1437144 · Cited by 7
Axon glycoprotein routing in nerve polarity, function, and repair
ez-Revuelta, N. D. ́. (2015) · Cited by 7
Sugaya, Y., Jinde, S., Kato, N., & Maru, E. (2009) · Neuroscience Research · doi:10.1016/j.neures.2009.10.014 · Cited by 7
A role for endosomal proteins in alphavirus dissemination in mosquitoes
Campbell, C. L., Lehmann, C. J., Gill, S. S., Dunn, W. A., James, A. A., & Foy, B. D. (2011) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2011.01078.x · Cited by 6
Differentiation of two human neuroblastoma cell lines alters SV2 expression patterns
Lekholm, E., Ceder, M. M., Forsberg, E. C., Schiöth, H. B., & Fredriksson, R. (2021) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-020-00243-8 · Cited by 6
Hogg, J. A., & Cousin, M. A. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.16308 · Cited by 5
Belmont, L., Contreras, M., Cartwright-Acar, C. H., Marceau, C. D., Agrawal, A., Levoir, L. M., Lubow, J., & Goo, L. (2024) · Journal of Virology · doi:10.1128/jvi.01582-24 · Cited by 5
Midorikawa, R., Takakura, D., Morise, J., Wakazono, Y., Kawasaki, N., Oka, S., & Takamiya, K. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14964 · Cited by 5
iTRAQ-based proteomic analysis after mesenchymal stem cell line transplantation for ischemic stroke
Mitaki, S., Nagai, A., Wada, Y., Onoda, K., Sheikh, A. M., Adachi, E., Matsumoto, K., & Yamaguchi, S. (2020) · Brain Research · doi:10.1016/j.brainres.2020.146900 · Cited by 5
Small, C., Harper, C., Jiang, A., Kontaxi, C., Yak, N., Malapaka, A., Davenport, E. C., Wallis, T. P., Gormal, R. S., Joensuu, M., et al. (2022) · doi:10.1101/2022.12.12.520075 · Cited by 4
Pharmacological treatment strategies targeting cognitive impairment associated with aging
Koh, M. T. (2012) · Folia Pharmacologica Japonica · doi:10.1254/fpj.139.157 · Cited by 4
SV2A-Syt1 interaction controls surface nanoclustering and access to recycling synaptic vesiclesPreprint
Small, C., Harper, C. B., Kontaxi, C., Davenport, E. C., Wallis, T. P., Malapaka, A., Yak, N., Joensuu, M., Martínez‐Mármol, R., Cousin, M. A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.08.471864 · Cited by 4
Levetiracetam: An antiseizure drug with unique neuroprotective properties
Ewens, A. N., & Thayer, S. A. (2025) · ASPET Discovery · doi:10.1016/j.aspetd.2025.100006 · Cited by 4
Whitt, J. D., Hong, W. S., Telange, R., Lin, C. P., Bibb, J. A., Beebe, D. J., Chen, H. R., & Jaskula‐Sztul, R. (2020) · Cancer Gene Therapy · doi:10.1038/s41417-020-0167-x · Cited by 3
Gumenyuk, V. P., & Trikash, I. O. (2014) · Neurophysiology · doi:10.1007/s11062-014-9416-7 · Cited by 3
Computational Analyses of the Mechanism of Action of Antiepileptic Agents
Sinha, S., Dubey, M., Misal, S., Alavala, R. R., & Ramaa, C. S. (2025) · Springer eBooks · doi:10.1007/978-981-96-4154-3_24 · Cited by 2
Kil, H. K., Kim, K. W., Lee, D.-H., Lee, S. M., Lee, C. H., & Kim, S. Y. (2021) · Biochemical Genetics · doi:10.1007/s10528-021-10034-1 · Cited by 2
Glutamate and Epilepsy: An Insight from Temporal Lobe Epilepsy
Musto, A. E. (2022) · Springer eBooks · doi:10.1007/978-3-030-87480-3_18 · Cited by 2
Neuroimmune cortical organoids overexpressing C4A exhibit multiple schizophrenia endophenotypesPreprint
Stanton, M. M., Modan, S., Taylor, P. M., Hariani, H. N., Sorokin, J. M., Rash, B. G., Rao, S. B., Tobon, A., Enriquez, L., Dang, B., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.20.524955 · Cited by 2
Kang, S., Na, Y. H., Kwon, Y., Joo, K., An, H. J., Kim, H. J., Kim, S., & Oh, M. J. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.153685 · Cited by 1
Maturation and heterogeneity of vertebrate motor synapses
Tejero, R., López-Manzaneda, M., Franco-Espín, J., & Tabares, L. (2018) · Current Opinion in Physiology · doi:10.1016/j.cophys.2018.02.009 · Cited by 1
Synaptisches Vesikelprotein 2A
Surges, R., Schoch, S., & Elger, C. E. (2012) · Clinical Epileptology · doi:10.1007/s10309-012-0249-3 · Cited by 1
The Dual-Receptor Recognition of Botulinum Neurotoxins
Rummel, A. (2014) · Springer eBooks · doi:10.1007/978-1-4614-9454-6_6
Synaptic Vesicle Protein 2 (SV2) does not hydrolyze ATP
Yao, J., & Bajjalieh, S. (2013) · F1000Research · doi:10.12688/f1000research.2-209.v1
Meehan, A. L. (2011) · University of Minnesota Digital Conservancy (University of Minnesota)
Glutamatergic Synapse Formation in Developing Zebrafish Embryos
Fierro, J. (2015) · Scholars' Bank (University of Oregon)
Evidence for Synaptic Vesicle Binding by the C-terminal of a Short Splice CaV2.1 Calcium Channel
Snidal, C. A. (2018) · TSpace (University of Toronto)
Vavoulis, D. V., Pagnamenta, A. T., Knight, S., Pentony, M. M., Armstrong, M., Galizia, E. C., Balestrini, S., Sisodiya, S. M., & Taylor, J. C. (2019) · arXiv (Cornell University) · doi:10.48550/arxiv.1909.10580 · Cited by 1
Vavoulis, D. V., Pagnamenta, A. T., Sjl., K., Pentony, M. M., Armstrong, M., Galizia, E. C., Balestrini, S., Sisodiya, S. M., & Taylor, J. C. (2019) · medRxiv · doi:10.1101/19007674
Biology of Proteoglycans and Associated Glycosaminoglycans
Salinas-Marín, R., Villanueva-Cabello, T. M., & Martínez-Duncker, I. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819475-1.00065-1
Presynaptic Dysfunction in Parkinson’s Disease
Kar, K. (2024) · Springer eBooks · doi:10.1007/978-981-99-9404-5_12
Application of SV2A PET in neurodegenerative disorders
Chen, D., & JIANG, H. (2024) · Scientia Sinica Vitae · doi:10.1360/ssv-2024-0086
The role of the synaptic vesicle protein SV2A in regulating mitochondrial morphology and autophagyPreprint
Jörg, M., Reichert, J., Pauly, K., Distler, U., Tenzer, S., Bartholomé, O., Rogister, B., Kern, A., Behl, C., Gellérie, M., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.30.605753 · Cited by 1
The role of the synaptic vesicle protein SV2A in regulating mitochondrial morphology and autophagyPreprint
Friedland, K., Jörg, M., Reichert, J., Pauly, K., Distler, U., Tenzer, S., Bartholomé, O., Rogister, B., Kern, A., Behl, C., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4538326/v1
Mapping Dural and Periosteal SV2C, a Botulinum Toxin A Receptor, in the Mouse
Dehghani, A., Melo‐Carrillo, A., Strassman, A. M., Broide, R. S., Adams, A. M., Dabruzzo, B., Brin, M. F., & Burstein, R. (2025) · Toxins · doi:10.3390/toxins17100509
Immaturity of the neuromuscular junction in spinal muscular atrophy mouse models
Tabares, L., Fuentes, A., Cano, R., Ruiz, R., & Arumugam, S. (2026) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2026.1795130
McDonough, M. C., Kuralay, A., Butler, T. C., Alysia, B., Madelin, S., Gasparini, S., Geerling, J. C., & Resch, J. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.21.759848
Effects of environmental pollutants on SH-SY5Y in vitro neurodevelopmental model
Lopez-Suarez, L. (2022) · theses.fr (ABES) · doi:10.70675/1e791dd5z5848z4ee2zb26ez089a2f5c505e
Singh, S., Nayak, R., Gangachannaiah, S., Bhosale, A., Parveen, R. S., G, V. K. S., & Sundar, G. (2026) · PLoS ONE · doi:10.1371/journal.pone.0350585
Ma, J., Braun, A., Oskamp, A., Kricsfalussy-Hrabár, L., Hermes, N., Djakkani, S., Holz, U., Jakobs, S., Klein, S., Stüsgen, S., et al. (2026) · iScience · doi:10.1016/j.isci.2026.116676
Metadata
- Authors
- Chang, W.-P., & Südhof, T. C.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Howard Hughes Medical Institute (US)
- ORCID
- Südhof, Thomas C.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-01-28
- Volume
- 29
- Issue
- 4
- Pages
- 883-897
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2693337
- OpenAlex
- W2039108005
- Cited by
- 176
- References
- 30
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 14 · 2023: 8 · 2022: 9 · 2021: 10 · 2020: 7 · 2019: 12 · 2018: 7 · 2017: 8 · 2016: 8 · 2015: 10 · 2014: 10 · 2013: 15 · 2012: 19
- FWCI
- 6.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- 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 protein 2, SV2, synaptic vesicle priming, neurotransmitter release, vesicle fusion, readily releasable pool, vesicle maturation, epilepsy
- MeSH terms
- Action Potentials, Analysis of Variance, Animals, Animals, Newborn, Calcium, Cells, Cultured, Cerebral Cortex, Egtazic Acid, Electric Stimulation, Exocytosis, Glycosylation, Ionophores, Lysine, Membrane Glycoproteins, Models, Molecular, Mutation, Nerve Tissue Proteins, Synaptic Transmission, Neurons, Picrotoxin, Synaptic Vesicles, Ionomycin, Mice, Knockout, Excitatory Amino Acid Antagonists, 6-Cyano-7-nitroquinoxaline-2,3-dione, GABA Antagonists, Green Fluorescent Proteins, Synaptotagmins, 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
