The DOI matches its Crossref record; 64 of the 65 references it cites were found in a registry or an index.
Molecular Anatomy of a Trafficking Organelle
Open accessAbstract
Membrane traffic in eukaryotic cells involves transport of vesicles that bud from a donor compartment and fuse with an acceptor compartment. Common principles of budding and fusion have emerged, and many of the proteins involved in these events are now known. However, a detailed picture of an entire trafficking organelle is not yet available. Using synaptic vesicles as a model, we have now determined the protein and lipid composition; measured vesicle size, density, and mass; calculated the average protein and lipid mass per vesicle; and determined the copy number of more than a dozen major constituents. A model has been constructed that integrates all quantitative data and includes structural models of abundant proteins. Synaptic vesicles are dominated by proteins, possess a surprising diversity of trafficking proteins, and, with the exception of the V-ATPase that is present in only one to two copies, contain numerous copies of proteins essential for membrane traffic and neurotransmitter uptake.
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
“Competition for Rab6A on the vesicle will be high as the absolute number of Rab GTPases on an individual transport vesicle is likely to be small (∼10 per vesicle; Takamori et al., 2006) and many effectors, including two domains of KIF1C, will be vying to bind to Rabs.”
From The Rab6-regulated KIF1C kinesin motor domain contributes to Golgi organization (2015) · cites this paper as Takamori et al., 2006
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The dendritic membranes on which these receptors reside are, similar to other biological membranes, highly crowded structures (Takamori et al., 2006).”
From Barriers in the brain: resolving dendritic spine morphology and compartmentalization (2014) · cites this paper as Takamori et al., 2006
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
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
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
The Fluid Mosaic Model of the Structure of Cell Membranes
Singer, S. J., & Nicolson, G. L. (1972) · Science · doi:10.1126/science.175.4023.720 · Cited by 9,158
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M. S., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,996
A simplification of the protein assay method of Lowry et al. which is more generally applicable
Peterson, G. L. (1977) · Analytical Biochemistry · doi:10.1016/0003-2697(77)90043-4 · Cited by 8,531
Interaction Models for Water in Relation to Protein Hydration
Berendsen, H. J. C., Postma, J., A, W. F. V. G., & Hermans, J. (1981) · Jerusalem Symposia on Quantum Chemistry and Biochemistry · doi:10.1007/978-94-015-7658-1_21 · Cited by 5,733
Nagle, J. F., & Tristram‐Nagle, S. (2000) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(00)00016-2 · Cited by 2,660
Südhof, T. C. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131412 · Cited by 2,491
The Mechanisms of Vesicle Budding and Fusion
Bonifacino, J. S., & Glick, B. S. (2004) · Cell · doi:10.1016/s0092-8674(03)01079-1 · Cited by 1,908
Buckingham, A. D. (1980) · Springer eBooks · doi:10.1007/978-1-4613-3111-7_1 · Cited by 1,861
Flagged first, then by citations
1 of the 65 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Membrane lipids: where they are and how they behave
van Meer, G., Voelker, D. R., & Feigenson, G. W. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2330 · Cited by 7,157
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
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
Verkhratsky, A., & Nedergaard, M. (2018) · Physiological Reviews · doi:10.1152/physrev.00042.2016 · Cited by 1,678
Urban, C. F., Ermert, D., Schmid, M., Abed, U. A., Goosmann, C., Nacken, W. K. F., Brinkmann, V., Jungblut, P. R., & Zychlinsky, A. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000639 · Cited by 1,720
Neurotransmitter Release: The Last Millisecond in the Life of a Synaptic Vesicle
Südhof, T. C. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.022 · Cited by 1,197
Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry
Ejsing, C. S., Sampaio, J. L., Surendranath, V., Duchoslav, E., Ekroos, K., Klemm, R. W., Simons, K., & Shevchenko, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811700106 · Cited by 1,053
Emerging roles for lipids in shaping membrane-protein function
Phillips, R., Ursell, T. S., Wiggins, P. A., & Sens, P. (2009) · Nature · doi:10.1038/nature08147 · Cited by 988
Brain Glucose Metabolism: Integration of Energetics with Function
Dienel, G. A. (2018) · Physiological Reviews · doi:10.1152/physrev.00062.2017 · Cited by 911
Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins
Wilhelm, B. G., Mandad, S., Truckenbrodt, S., Kröhnert, K., Schäfer, C., Rammner, B., Koo, S. J., Claßen, G. A., Krauss, M., Haucke, V., et al. (2014) · Science · doi:10.1126/science.1252884 · Cited by 770
Self-citationLipidomics: coming to grips with lipid diversity
Shevchenko, A., & Simons, K. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2934 · Cited by 838
Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology
Pirazzini, M., Rossetto, O., Eleopra, R., & Montecucco, C. (2017) · Pharmacological Reviews · doi:10.1124/pr.116.012658 · Cited by 776
Cholesterol metabolism and homeostasis in the brain
Zhang, J., & Liu, Q. (2015) · Protein & Cell · doi:10.1007/s13238-014-0131-3 · Cited by 686
The release and trans-synaptic transmission of Tau via exosomes
Wang, Y., Balaji, V., Kaniyappan, S., Krüger, L., Irsen, S., Tepper, K., Chandupatla, R., Maetzler, W., Schneider, A., Mandelkow, E., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0143-y · Cited by 674
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1750 · Cited by 661
The synapsins: Key actors of synapse function and plasticity
Cesca, F., Baldelli, P., Valtorta, F., & Benfenati, F. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.006 · Cited by 654
Genetic identification of brain cell types underlying schizophrenia
Major Depressive Disorder Working Group of the Psychiatric Genomics Consortium, Skene, N. G., Bryois, J., Bakken, T. E., Breen, G., Crowley, J. J., Gaspar, H. A., Giusti-Rodriguez, P., Hodge, R. D., Miller, J. A., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0129-5 · Cited by 651
Botulinum neurotoxins: genetic, structural and mechanistic insights
Rossetto, O., Pirazzini, M., & Montecucco, C. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3295 · Cited by 637
Spatial proteomics: a powerful discovery tool for cell biology
Lundberg, E., & Borner, G. H. H. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0094-y · Cited by 591
Imaging synaptic density in the living human brain
Finnema, S. J., Nabulsi, N. B., Eid, T., Detyniecki, K., Lin, S.-F., Chen, M.-K., Dhaher, R., Matuskey, D., Baum, E., Holden, D., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf6667 · Cited by 575
A Comprehensive Comparison of Transmembrane Domains Reveals Organelle-Specific Properties
Sharpe, H. J., Stevens, T. J., & Munro, S. (2010) · Cell · doi:10.1016/j.cell.2010.05.037 · Cited by 550
Synaptic Vesicle ExocytosisPreprint
Südhof, T. C., & Rizo, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005637 · Cited by 539
Nanodomain coupling between Ca2+ channels and sensors of exocytosis at fast mammalian synapses
Eggermann, E., Bucurenciu, I., Goswami, S. P., & Jonas, P. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3125 · Cited by 500
Cholesterol metabolism in neurons and astrocytes
Pfrieger, F. W., & Ungerer, N. (2011) · Progress in Lipid Research · doi:10.1016/j.plipres.2011.06.002 · Cited by 500
Membrane lipidome of an epithelial cell line
Sampaio, J. L., Gerl, M. J., Klose, C. D., Ejsing, C. S., Beug, H., Simons, K., & Shevchenko, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019267108 · Cited by 500
A liquid phase of synapsin and lipid vesicles
Milovanović, D., Wu, Y., Bian, X., & Camilli, P. V. D. (2018) · Science · doi:10.1126/science.aat5671 · Cited by 494
Mass spectrometry in high-throughput proteomics: ready for the big time
Nilsson, T., Mann, M., Aebersold, R., Yates, J. R., Bairoch, A., & Bergeron, J. J. M. (2010) · Nature Methods · doi:10.1038/nmeth0910-681 · Cited by 470
The mechanisms and functions of spontaneous neurotransmitter release
Kavalali, E. T. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3875 · Cited by 486
Selective Activation of Cognate SNAREpins by Sec1/Munc18 Proteins
Shen, J., Tareste, D. C., Paumet, F., Rothman, J. E., & Melia, T. J. (2007) · Cell · doi:10.1016/j.cell.2006.12.016 · Cited by 487
Inhibition of mitochondrial fusion by α‐synuclein is rescued by PINK1, Parkin and DJ‐1
Kamp, F., Exner, N., Lutz, A. K., Wender, N., Hegermann, J., Brunner, B., Nuscher, B., Bartels, T., Giese, A., Beyer, K., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.223 · Cited by 504
Synaptophysin Regulates the Kinetics of Synaptic Vesicle Endocytosis in Central Neurons
Kwon, S. E., & Chapman, E. R. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.001 · Cited by 470
Rab family of small GTPases: an updated view on their regulation and functions
Homma, Y., Hiragi, S., & Fukuda, M. (2020) · FEBS Journal · doi:10.1111/febs.15453 · Cited by 482
Saheki, Y., & De Camilli, P. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005645 · Cited by 457
CLC Chloride Channels and Transporters: Structure, Function, Physiology, and Disease
Jentsch, T. J., & Pusch, M. (2018) · Physiological Reviews · doi:10.1152/physrev.00047.2017 · Cited by 462
Molecular Mechanisms for Synchronous, Asynchronous, and Spontaneous Neurotransmitter Release
Kaeser, P. S., & Regehr, W. G. (2014) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170338 · Cited by 447
Exocytosis and Endocytosis: Modes, Functions, and Coupling Mechanisms
Wu, L., Hamid, E., Shin, W., & Chiang, H. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170305 · Cited by 462
Lipids on the move: Simulations of membrane pores, domains, stalks and curves
Marrink, S. J., de Vries, A. H., & Tieleman, D. P. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.006 · Cited by 440
Mechanisms of Membrane Curvature Sensing
Antonny, B. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052809-155121 · Cited by 442
Botulinum Neurotoxin: A Marvel of Protein Design
Montal, M. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.051908.125345 · Cited by 425
Single-Molecule Localization Microscopy in Eukaryotes
Sauer, M., & Heilemann, M. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00667 · Cited by 400
Proteomic Analysis of Unbounded Cellular Compartments: Synaptic Clefts
Loh, K. H., Stawski, P. S., Draycott, A. S., Udeshi, N. D., Lehrman, E. K., Wilton, D. K., Svinkina, T., Deerinck, T. J., Ellisman, M. H., Stevens, B., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.041 · Cited by 399
Astrocytes as secretory cells of the central nervous system: idiosyncrasies of vesicular secretion
Verkhratsky, A., Matteoli, M., Parpura, V., Mothet, J., & Zorec, R. (2016) · The EMBO Journal · doi:10.15252/embj.201592705 · Cited by 397
Membrane traffic in the secretory pathway
Fukuda, M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8351-4 · Cited by 403
The Morphological and Molecular Nature of Synaptic Vesicle Priming at Presynaptic Active Zones
Imig, C., Min, S.-W., Krinner, S., Arancillo, M., Rosenmund, C., Südhof, T. C., Rhee, J., Brose, N., & Cooper, B. H. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.009 · Cited by 389
Phosphatidylserine in the brain: Metabolism and function
Kim, H.-Y., Huang, B. X., & Spector, A. A. (2014) · Progress in Lipid Research · doi:10.1016/j.plipres.2014.06.002 · Cited by 389
Polyunsaturated phospholipids facilitate membrane deformation and fission by endocytic proteins
Pinot, M., Vanni, S., Pagnotta, S., Lacas‐Gervais, S., Payet, L.-A., Ferreira, T., Gautier, R., Goud, B., Antonny, B., & Barelli, H. (2014) · Science · doi:10.1126/science.1255288 · Cited by 388
Axonal transport: Driving synaptic function
Guedes-Dias, P., & Holzbaur, E. L. F. (2019) · Science · doi:10.1126/science.aaw9997 · Cited by 355
From glutamate co-release to vesicular synergy: vesicular glutamate transporters
El Mestikawy, S., Wallén-Mackenzie, Å., Fortin, G. M., Descarries, L., & Trudeau, L.-E. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2969 · Cited by 385
Mechanisms of α-Synuclein Induced Synaptopathy in Parkinson's Disease
Bridi, J. C., & Hirth, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00080 · Cited by 396
Effects of Curvature and Composition on α-Synuclein Binding to Lipid Vesicles
Middleton, E. R., & Rhoades, E. R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.07.056 · Cited by 392
Multiple Tight Phospholipid-Binding Modes of α-Synuclein Revealed by Solution NMR Spectroscopy
Bodner, C. R., Dobson, C. M., & Bax, A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.05.066 · Cited by 378
The complexity of tau in Alzheimer’s disease
Naseri, N. N., Wang, H., Guo, J. D., Sharma, M., & Luo, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.022 · Cited by 393
Nanovehicular Intracellular Delivery Systems
Prokop, A., & Davidson, J. M. (2008) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21270 · Cited by 374
Hepatocellular carcinoma: signaling pathways and therapeutic advances
Zheng, J., Wang, S., Xia, L., Sun, Z., Chan, K. M., Bernards, R., Qin, W., Chen, J., Xia, Q., & Jin, H. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02075-w · Cited by 421
Autophagy in Parkinson's Disease
Hou, X., Watzlawik, J. O., Fiesel, F. C., & Springer, W. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.037 · Cited by 361
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 356
Self-citationGracià, R. S., Bezlyepkina, N., Knorr, R. L., Lipowsky, R., & Dimova, R. (2010) · Soft Matter · doi:10.1039/b920629a · Cited by 350
Exorcising the Exocyst Complex
Heider, M. R., & Munson, M. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01353.x · Cited by 344
C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction
Lautenschläger, J., Stephens, A. D., Fusco, G., Ströhl, F., Curry, N., Zacharopoulou, M., Michel, C. H., Laine, R. F., Nespovitaya, N., Fantham, M., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03111-4 · Cited by 339
Clathrin regenerates synaptic vesicles from endosomes
Watanabe, S., Trimbuch, T., Camacho-Pérez, M., Rost, B. R., Brokowski, B., Söhl-Kielczynski, B., Felies, A., Davis, M. W., Rosenmund, C., & Jorgensen, E. M. (2014) · Nature · doi:10.1038/nature13846 · Cited by 333
Myelin Proteomics: Molecular Anatomy of an Insulating Sheath
Jahn, O., Tenzer, S., & Werner, H. B. (2009) · Molecular Neurobiology · doi:10.1007/s12035-009-8071-2 · Cited by 355
Gliotransmission: Beyond Black-and-White
Savtchouk, I., & Volterra, A. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.0017-17.2017 · Cited by 325
Cargo Recognition in Clathrin-Mediated EndocytosisPreprint
Traub, L. M., & Bonifacino, J. S. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016790 · Cited by 328
Synaptic vesicle recycling: steps and principles
Rizzoli, S. O. (2014) · The EMBO Journal · doi:10.1002/embj.201386357 · Cited by 317
Dynamic Activity of Lipid Droplets: Protein Phosphorylation and GTP-Mediated Protein Translocation
Bartz, R., Zehmer, J. K., Zhu, M., Chen, Y., Serrero, G., Zhao, Y., & Liu, P. (2007) · Journal of Proteome Research · doi:10.1021/pr070158j · Cited by 316
Systematic resequencing of X-chromosome synaptic genes in autism spectrum disorder and schizophrenia
Piton, A., Gauthier, J., Hamdan, F. F., Lafrenière, R. G., Yang, Y., Henrion, É., Laurent, S. B., Noreau, A., Thibodeau, P., Karemera, L., et al. (2010) · Molecular Psychiatry · doi:10.1038/mp.2010.54 · Cited by 318
G Protein-Coupled Receptors Self-Assemble in Dynamics Simulations of Model Bilayers
Périole, X., Huber, T., Marrink, . J., & Sakmar, T. P. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0706246 · Cited by 314
Propagation of Protein Aggregation in Neurodegenerative Diseases
Vaquer‐Alicea, J., & Diamond, M. I. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045049 · Cited by 316
Bacaj, T., Wu, D., Yang, X., Morishita, W., Zhou, P., Xu, W., Malenka, R. C., & Südhof, T. C. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.026 · Cited by 308
Galvagnion, C., Brown, J. W. P., Ouberai, M. M., Flagmeier, P., Vendruscolo, M., Buell, A. K., Sparr, E., & Dobson, C. M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601899113 · Cited by 306
Structure and Organization of Coat Proteins in the COPII Cage
Fath, S., Mancias, J. D., Bi, X., & Goldberg, J. D. (2007) · Cell · doi:10.1016/j.cell.2007.05.036 · Cited by 304
Rak, J. W. (2010) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-0030-1267043 · Cited by 311
Klassen, T., Davis, C., Goldman, A. M., Burgess, D., Chen, T. F., Wheeler, D. A., McPherson, J. D., Bourquin, T., Lewis, L. R., Villasana, D., et al. (2011) · Cell · doi:10.1016/j.cell.2011.05.025 · Cited by 305
Syntaxin-4 defines a domain for activity-dependent exocytosis in dendritic spines
Kennedy, M. J., Davison, I. G., Robinson, C. G., & Ehlers, M. D. (2010) · Cell · doi:10.1016/j.cell.2010.02.042 · Cited by 294
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity
Perni, M., Galvagnion, C., Maltsev, A. S., Meisl, G., Müller, M. B. D., Challa, P. K., Kirkegaard, J. B., Flagmeier, P., Cohen, S. I. A., Cascella, R., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610586114 · Cited by 300
Bartels, T., Ahlstrom, L. S., Leftin, A., Kamp, F., Haass, C., Brown, M. F., & Beyer, K. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.06.035 · Cited by 300
Enkavi, G., Javanainen, M., Kulig, W., Róg, T., & Vattulainen, I. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00538 · Cited by 293
One SNARE complex is sufficient for membrane fusion
van den Bogaart, G., Holt, M. G., Bunt, G., Riedel, D., Wouters, F. S., & Jahn, R. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1748 · Cited by 289
Self-citationThe Multifaceted Role of SNARE Proteins in Membrane Fusion
Han, J., Pluháčková, K., & Böckmann, R. A. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00005 · Cited by 286
Synaptic Vesicle Pools and Dynamics
Alabi, A. A., & Tsien, R. W. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013680 · Cited by 284
Protein scaffolds in the coupling of synaptic exocytosis and endocytosis
Haucke, V., Neher, E., & Sigrist, S. J. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn2948 · Cited by 298
A role for lipid droplets in inter‐membrane lipid traffic
Zehmer, J. K., Huang, Y., Gong, P., Pu, J., Anderson, R. G. W., & Liu, P. (2009) · PROTEOMICS · doi:10.1002/pmic.200800584 · Cited by 282
Balaji, J., & Ryan, T. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707574105 · Cited by 279
Energetics and dynamics of SNAREpin folding across lipid bilayers
Li, F., Pincet, F., Perez, É., Eng, W. S., Melia, T. J., Rothman, J. E., & Tareste, D. C. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1310 · Cited by 290
Fernández, E., Collins, M. O., Uren, R. T., Kopanitsa, M. V., Komiyama, N. H., Croning, M. D. R., Zografos, L., Armstrong, J. D., Choudhary, J. S., & Grant, S. G. N. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.27 · Cited by 270
Architecture and biogenesis of plus-strand RNA virus replication factories
Paul, D. (2013) · World Journal of Virology · doi:10.5501/wjv.v2.i2.32 · Cited by 274
Proteases for Processing Proneuropeptides into Peptide Neurotransmitters and Hormones
HOOK, V. Y. H., Funkelstein, L., Lu, D., Bark, S. J., Wegrzyn, J., & Hwang, S. (2008) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.113006.094812 · Cited by 274
The Lateral Organization and Mobility of Plasma Membrane Components
Jacobson, K., Liu, P., & Lagerholm, B. C. (2019) · Cell · doi:10.1016/j.cell.2019.04.018 · Cited by 276
Another Piece of the Membrane Puzzle: Extending Slipids Further
Jämbeck, J. P. M., & Lyubartsev, A. P. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct300777p · Cited by 276
LRRK2 Controls Synaptic Vesicle Storage and Mobilization within the Recycling Pool
Piccoli, G., Condliffe, S. B., Bauer, M., Giesert, F., Boldt, K., Astis, S. D., Meixner, A., Sarioglu, H., Weisenhorn, D. M. V., Wurst, W., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3730-10.2011 · Cited by 282
Meng, J., Wang, J., Lawrence, G. W., & Dolly, J. O. (2007) · Journal of Cell Science · doi:10.1242/jcs.012211 · Cited by 267
Brügger, B. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035324 · Cited by 265
Self-citationThe Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson’s Disease
Galvagnion, C. (2017) · Journal of Parkinson s Disease · doi:10.3233/jpd-171103 · Cited by 275
SNARE Proteins: One to Fuse and Three to Keep the Nascent Fusion Pore Open
Shi, L., Shen, Q.-T., Kiel, A., Wang, J., Wang, H., Melia, T. J., Rothman, J. E., & Pincet, F. (2012) · Science · doi:10.1126/science.1214984 · Cited by 278
Protein area occupancy at the center of the red blood cell membrane
Dupuy, A. D., & Engelman, D. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712379105 · Cited by 262
Structural basis of synaptic vesicle assembly promoted by α-synuclein
Fusco, G., Pape, T., Stephens, A. D., Mahou, P., Costa, A. R., Kaminski, C. F., Schierle, G. S. K., Vendruscolo, M., Veglia, G., Dobson, C. M., et al. (2016) · Nature Communications · doi:10.1038/ncomms12563 · Cited by 261
The Synaptic Vesicle Cycle Revisited: New Insights into the Modes and Mechanisms
Chanaday, N. L., Cousin, M. A., Milosevic, I., Watanabe, S., & Morgan, J. R. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.1158-19.2019 · Cited by 255
Measuring synaptic vesicles using cellular electrochemistry and nanoscale molecular imaging
Phan, N. T. N., Li, X., & Ewing, A. G. (2017) · Nature Reviews Chemistry · doi:10.1038/s41570-017-0048 · Cited by 252
Ca2+-Activated K+Channels: From Protein Complexes to Function
Berkefeld, H., Fakler, B., & Schulte, U. (2010) · Physiological Reviews · doi:10.1152/physrev.00049.2009 · Cited by 274
Synaptic vesicle pools: an update
Denker (2010) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2010.00135 · Cited by 248
Metadata
- Authors
- Takamori, S., Holt, M., Stenius, K., Lemke, E. A., Grønborg, M., Riedel, D., Urlaub, H., Schenck, S., Brügger, B., Ringler, P., Müller, S. A., Rammner, B., Gräter, F., Hub, J. S., De Groot, B. L., Mieskes, G., Moriyama, Y., Klingauf, J., Grubmüller, H., Heuser, J., Wieland, F., & Jahn, R.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Yale University (US)
- Heidelberg University (DE)
- University of Basel (CH)
- Okayama University (JP)
- Washington University in St. Louis (US)
- Corresponding author
- Jahn, Reinhard
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-11
- Volume
- 127
- Issue
- 4
- Pages
- 831-846
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2144447780
- Cited by
- 2,373
- References
- 65
- Citations by year
- 2026: 65 · 2025: 94 · 2024: 124 · 2023: 103 · 2022: 136 · 2021: 131 · 2020: 132 · 2019: 106 · 2018: 134 · 2017: 126 · 2016: 121 · 2015: 127 · 2014: 131 · 2013: 119 · 2012: 124
- FWCI
- 47.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Lirias (submittedVersion, other-oa)
- Max Planck Institute for Plasma Physics (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- VUBIR (Vrije Universiteit Brussel) (submittedVersion)
- Funders
- University of Cambridge
- Deutsche Forschungsgemeinschaft
- Forsknings- og Innovationsstyrelsen
- Leibniz-Gemeinschaft
- Japan Society for the Promotion of Science
- Danish Agency for Science and Higher Education
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- synaptic vesicles, membrane trafficking, vesicle budding, vesicle fusion, protein composition, lipid composition, protein copy number, V-ATPase, neurotransmitter uptake
- MeSH terms
- Animals, Lipids, Models, Molecular, Proteins, Spectrometry, Fluorescence, Synaptic Vesicles, Protein Transport, Rats
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
