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  • 1
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    Helical extension of the neuronal SNARE complex into the membrane (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-07-03
    Description: Neurotransmission relies on synaptic vesicles fusing with the membrane of nerve cells to release their neurotransmitter content into the synaptic cleft, a process requiring the assembly of several members of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family. SNAREs represent an evolutionarily conserved protein family that mediates membrane fusion in the secretory and endocytic pathways of eukaryotic cells. On membrane contact, these proteins assemble in trans between the membranes as a bundle of four alpha-helices, with the energy released during assembly being thought to drive fusion. However, it is unclear how the energy is transferred to the membranes and whether assembly is conformationally linked to fusion. Here, we report the X-ray structure of the neuronal SNARE complex, consisting of rat syntaxin 1A, SNAP-25 and synaptobrevin 2, with the carboxy-terminal linkers and transmembrane regions at 3.4 A resolution. The structure shows that assembly proceeds beyond the already known core SNARE complex, resulting in a continuous helical bundle that is further stabilized by side-chain interactions in the linker region. Our results suggest that the final phase of SNARE assembly is directly coupled to membrane merger.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3108252/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3108252/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stein, Alexander -- Weber, Gert -- Wahl, Markus C -- Jahn, Reinhard -- P01 GM072694/GM/NIGMS NIH HHS/ -- P01 GM072694-01/GM/NIGMS NIH HHS/ -- England -- Nature. 2009 Jul 23;460(7254):525-8. doi: 10.1038/nature08156. Epub 2009 Jul 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19571812" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crystallography, X-Ray ; Membrane Proteins/*chemistry ; Mice ; *Models, Molecular ; Neurons/*metabolism ; Protein Stability ; Protein Structure, Quaternary ; Rats ; SNARE Proteins/*chemistry/*metabolism ; Synapses/metabolism ; Syntaxin 1/chemistry ; Transition Temperature ; Vesicle-Associated Membrane Protein 2/chemistry
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Synaptotagmin: a calcium sensor on the synaptic vesicle surface (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-15
    Description: Neurons release neurotransmitters by calcium-dependent exocytosis of synaptic vesicles. However, the molecular steps transducing the calcium signal into membrane fusion are still an enigma. It is reported here that synaptotagmin, a highly conserved synaptic vesicle protein, binds calcium at physiological concentrations in a complex with negatively charged phospholipids. This binding is specific for calcium and involves the cytoplasmic domain of synaptotagmin. Calcium binding is dependent on the intact oligomeric structure of synaptotagmin (it is abolished by proteolytic cleavage at a single site). These results suggest that synaptotagmin acts as a cooperative calcium receptor in exocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brose, N -- Petrenko, A G -- Sudhof, T C -- Jahn, R -- New York, N.Y. -- Science. 1992 May 15;256(5059):1021-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurochemistry, Max-Planck-Institute for Psychiatry, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589771" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Brain Chemistry ; Calcium/*metabolism/pharmacology ; *Calcium-Binding Proteins ; Cell Membrane/metabolism ; Cytoplasmic Granules/metabolism ; Dansyl Compounds/metabolism ; Energy Transfer ; Exocytosis ; Fluorescent Dyes ; Liposomes/metabolism ; Macromolecular Substances ; Membrane Glycoproteins/chemistry/isolation & purification/*metabolism ; Nerve Tissue Proteins/chemistry/isolation & purification/*metabolism ; Phosphatidylethanolamines/metabolism ; Rats ; Synaptic Vesicles/*metabolism ; Synaptotagmins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Membrane fusion intermediates via directional and full assembly of the SNARE complex (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-06-02
    Description: Cellular membrane fusion is thought to proceed through intermediates including docking of apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and fusion pore opening. A membrane-bridging four-helix complex of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediates fusion. However, how assembly of the SNARE complex generates docking and other fusion intermediates is unknown. Using a cell-free reaction, we identified intermediates visually and then arrested the SNARE fusion machinery when fusion was about to begin. Partial and directional assembly of SNAREs tightly docked bilayers, but efficient fusion and an extended form of hemifusion required assembly beyond the core complex to the membrane-connecting linkers. We propose that straining of lipids at the edges of an extended docking zone initiates fusion.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677693/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3677693/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hernandez, Javier M -- Stein, Alexander -- Behrmann, Elmar -- Riedel, Dietmar -- Cypionka, Anna -- Farsi, Zohreh -- Walla, Peter J -- Raunser, Stefan -- Jahn, Reinhard -- 3P01GM072694-05S1/GM/NIGMS NIH HHS/ -- P01 GM072694/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 22;336(6088):1581-4. doi: 10.1126/science.1221976. Epub 2012 May 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22653732" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Lipid Bilayers/chemistry/*metabolism ; *Liposomes/chemistry/metabolism ; *Membrane Fusion ; Protein Binding ; Protein Conformation ; Rats ; SNARE Proteins/chemistry/*metabolism ; Vesicle-Associated Membrane Protein 2/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Distinct kinetic changes in neurotransmitter release after SNARE protein cleavage (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-07-16
    Description: Neurotransmitter release is triggered by calcium ions and depends critically on the correct function of three types of SNARE [soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor] proteins. With use of the large calyx of Held presynaptic terminal from rats, we found that cleavage of different SNARE proteins by clostridial neurotoxins caused distinct kinetic changes in neurotransmitter release. When elevating calcium ion concentration directly at the presynaptic terminal with the use of caged calcium, cleavage of SNAP-25 by botulinum toxin A (BoNT/A) produced a strong reduction in the calcium sensitivity for release, whereas cleavage of syntaxin using BoNT/C1 and synaptobrevin using tetanus toxin (TeNT) produced an all-or-nothing block without changing the kinetics of remaining vesicles. When stimulating release by calcium influx through channels, a difference between BoNT/C1 and TeNT emerged, which suggests that cleavage of synaptobrevin modifies the coupling between channels and release-competent vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sakaba, Takeshi -- Stein, Alexander -- Jahn, Reinhard -- Neher, Erwin -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):491-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Department of Membrane Biophysics, Max Planck Institute for Biophysical Chemistry, Gottingen 37077, Germany. tsakaba@gwdg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020741" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Botulinum Toxins/metabolism/pharmacology ; Botulinum Toxins, Type A/metabolism/pharmacology ; Calcium/metabolism ; Calcium Channels/metabolism ; Excitatory Postsynaptic Potentials ; In Vitro Techniques ; Kinetics ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Neurotransmitter Agents/*metabolism ; Patch-Clamp Techniques ; Presynaptic Terminals/*metabolism ; Qa-SNARE Proteins ; R-SNARE Proteins ; Rats ; Synaptic Vesicles/metabolism ; Synaptosomal-Associated Protein 25 ; Tetanus Toxin/metabolism/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Neuroscience. Synaptic vesicles in the fast lane (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-03-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holt, Matthew -- Jahn, Reinhard -- New York, N.Y. -- Science. 2004 Mar 26;303(5666):1986-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15044796" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electric Stimulation ; Endocytosis ; Exocytosis ; Fluorescent Dyes/metabolism ; Models, Neurological ; Movement ; Neuromuscular Junction/*physiology/ultrastructure ; Neurotransmitter Agents/*metabolism ; Presynaptic Terminals/*physiology/ultrastructure ; Pyridinium Compounds/metabolism ; Quaternary Ammonium Compounds/metabolism ; Rana pipiens ; Synaptic Membranes/physiology/ultrastructure ; Synaptic Transmission ; Synaptic Vesicles/*physiology/ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Neuroscience. A neuronal receptor for botulinum toxin (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jahn, Reinhard -- New York, N.Y. -- Science. 2006 Apr 28;312(5773):540-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, 37077 Gottingen, Germany. rjahn@gwdg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16645086" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Botulinum Toxins/chemistry/metabolism ; Botulinum Toxins, Type A/chemistry/*metabolism/toxicity ; Endocytosis ; Evolution, Molecular ; Membrane Glycoproteins/chemistry/genetics/*metabolism ; Mice ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neuromuscular Junction/metabolism ; Neurons/*metabolism ; Neurotransmitter Agents/metabolism ; Presynaptic Terminals/*metabolism ; Protein Isoforms ; R-SNARE Proteins/metabolism ; SNARE Proteins/metabolism ; Synaptic Transmission/drug effects ; Synaptic Vesicles/*metabolism ; Synaptosomal-Associated Protein 25/metabolism ; Synaptotagmins/metabolism ; Tetanus Toxin/metabolism/toxicity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Molecular machines governing exocytosis of synaptic vesicles (2012)
    Nature Publishing Group (NPG)
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    Publication Date: 2012-10-13
    Description: Calcium-dependent exocytosis of synaptic vesicles mediates the release of neurotransmitters. Important proteins in this process have been identified such as the SNAREs, synaptotagmins, complexins, Munc18 and Munc13. Structural and functional studies have yielded a wealth of information about the physiological role of these proteins. However, it has been surprisingly difficult to arrive at a unified picture of the molecular sequence of events from vesicle docking to calcium-triggered membrane fusion. Using mainly a biochemical and biophysical perspective, we briefly survey the molecular mechanisms in an attempt to functionally integrate the key proteins into the emerging picture of the neuronal fusion machine.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4461657/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4461657/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jahn, Reinhard -- Fasshauer, Dirk -- 3P01GM072694-05S1/GM/NIGMS NIH HHS/ -- P01 GM072694/GM/NIGMS NIH HHS/ -- England -- Nature. 2012 Oct 11;490(7419):201-7. doi: 10.1038/nature11320.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, 37077 Gottingen, Germany. rjahn@gwdg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23060190" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Exocytosis/*physiology ; Humans ; Lipid Metabolism ; Models, Biological ; SNARE Proteins/chemistry/metabolism ; Synaptic Vesicles/*physiology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 8
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    Membrane protein sequestering by ionic protein-lipid interactions (2011)
    Nature Publishing Group (NPG)
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    Publication Date: 2011-10-25
    Description: Neuronal exocytosis is catalysed by the SNAP receptor protein syntaxin-1A, which is clustered in the plasma membrane at sites where synaptic vesicles undergo exocytosis. However, how syntaxin-1A is sequestered is unknown. Here we show that syntaxin clustering is mediated by electrostatic interactions with the strongly anionic lipid phosphatidylinositol-4,5-bisphosphate (PIP2). Using super-resolution stimulated-emission depletion microscopy on the plasma membranes of PC12 cells, we found that PIP2 is the dominant inner-leaflet lipid in microdomains about 73 nanometres in size. This high accumulation of PIP2 was required for syntaxin-1A sequestering, as destruction of PIP2 by the phosphatase synaptojanin-1 reduced syntaxin-1A clustering. Furthermore, co-reconstitution of PIP2 and the carboxy-terminal part of syntaxin-1A in artificial giant unilamellar vesicles resulted in segregation of PIP2 and syntaxin-1A into distinct domains even when cholesterol was absent. Our results demonstrate that electrostatic protein-lipid interactions can result in the formation of microdomains independently of cholesterol or lipid phases.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3409895/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3409895/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van den Bogaart, Geert -- Meyenberg, Karsten -- Risselada, H Jelger -- Amin, Hayder -- Willig, Katrin I -- Hubrich, Barbara E -- Dier, Markus -- Hell, Stefan W -- Grubmuller, Helmut -- Diederichsen, Ulf -- Jahn, Reinhard -- P01 GM072694/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Oct 23;479(7374):552-5. doi: 10.1038/nature10545.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22020284" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cholesterol ; Membrane Microdomains/*chemistry/metabolism ; Microscopy, Confocal ; Molecular Dynamics Simulation ; Nerve Tissue Proteins/metabolism ; PC12 Cells ; Phosphatidylinositol 4,5-Diphosphate/*chemistry/*metabolism ; Phosphoric Monoester Hydrolases/metabolism ; *Protein Binding ; Rats ; *Static Electricity ; Syntaxin 1/*chemistry/*metabolism ; Unilamellar Liposomes/chemistry/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 9
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    Lioness leadership (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jahn, G C -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1215-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638093" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; Cooperative Behavior ; Female ; Lions/*psychology ; Territoriality
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Video-rate far-field optical nanoscopy dissects synaptic vesicle movement (2008)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2008-02-23
    Description: We present video-rate (28 frames per second) far-field optical imaging with a focal spot size of 62 nanometers in living cells. Fluorescently labeled synaptic vesicles inside the axons of cultured neurons were recorded with stimulated emission depletion (STED) microscopy in a 2.5-micrometer by 1.8-micrometer field of view. By reducing the cross-sectional area of the focal spot by about a factor of 18 below the diffraction limit (260 nanometers), STED allowed us to map and describe the vesicle mobility within the highly confined space of synaptic boutons. Although restricted within boutons, the vesicle movement was substantially faster in nonbouton areas, consistent with the observation that a sizable vesicle pool continuously transits through the axons. Our study demonstrates the emerging ability of optical microscopy to investigate intracellular physiological processes on the nanoscale in real time.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Westphal, Volker -- Rizzoli, Silvio O -- Lauterbach, Marcel A -- Kamin, Dirk -- Jahn, Reinhard -- Hell, Stefan W -- New York, N.Y. -- Science. 2008 Apr 11;320(5873):246-9. doi: 10.1126/science.1154228. Epub 2008 Feb 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of NanoBiophotonics, Max-Planck-Institute for Biophysical Chemistry, Gottingen 37077, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18292304" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Axons/physiology/*ultrastructure ; Cells, Cultured ; Fluorescent Dyes ; Hippocampus/physiology/ultrastructure ; Kinetics ; Microscopy, Fluorescence/*methods ; Movement ; *Nanotechnology ; Optics and Photonics ; Rats ; Synaptic Vesicles/*physiology/*ultrastructure ; Video Recording
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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