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  • 1
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    Probing single secretory vesicles with capillary electrophoresis (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-03-21
    Description: Secretory vesicles obtained from the atrial gland of the gastropod mollusk Aplysia californica were chemically analyzed individually with a combination of optical trapping, capillary electrophoresis separation, and a laser-induced fluorescence detection. With the use of optical trapping, a single vesicle that had attoliters (10(-18) liters) of volume was introduced into the tapered inlet of a separation capillary. Once the vesicle was injected, it was lysed, and its components were fluorescently labeled with naphthalene-2, 3-dicarboxaldehyde before separation. The resultant electropherograms indicated distinct variations in the contents of single vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiu, D T -- Lillard, S J -- Scheller, R H -- Zare, R N -- Rodriguez-Cruz, S E -- Williams, E R -- Orwar, O -- Sandberg, M -- Lundqvist, J A -- 1R29GM50336-01A2/GM/NIGMS NIH HHS/ -- DA09873/DA/NIDA NIH HHS/ -- GM18386/GM/NIGMS NIH HHS/ -- R29 GM050336/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 20;279(5354):1190-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9469805" target="_blank"〉PubMed〈/a〉
    Keywords: Amines/*analysis ; Amino Acids/*analysis ; Animals ; Aplysia/chemistry/ultrastructure ; Cytoplasmic Granules/*chemistry ; *Electrophoresis, Capillary ; Mass Spectrometry ; Naphthalenes ; Peptides/analysis ; Potassium Cyanide ; Spectroscopy, Fourier Transform Infrared ; Taurine/*analysis
    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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  • 2
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    Cell biology. Fusion without SNAREs? (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-03
    Description: Highly orchestrated molecular rearrangements are required for two membranes to fuse, as happens, for example, during neurotransmitter release into the synapse. In an elegant Perspective, Scales et al. discuss two studies (Schoch et al., Wang et al.) that shed new light on the protein interactions involved in membrane fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scales, S J -- Finley, M F -- Scheller, R H -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1015-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genentech Inc., South San Francisco, CA 94080, USA. sscales@gene.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691976" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Signaling ; *Calcium-Binding Proteins ; Catecholamines/metabolism ; Cell Membrane/metabolism ; Cells, Cultured ; Electrophysiology ; *Membrane Fusion ; Membrane Glycoproteins/*physiology ; Membrane Proteins/*physiology ; Mice ; Nerve Tissue Proteins/*physiology ; Neurotransmitter Agents/metabolism ; PC12 Cells ; Phospholipids/metabolism ; Protein Isoforms ; R-SNARE Proteins ; Rats ; SNARE Proteins ; Secretory Vesicles/*metabolism ; Synapses/physiology ; Synaptic Transmission ; Synaptic Vesicles/*metabolism ; Synaptotagmins ; *Vesicular Transport Proteins
    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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  • 3
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    Peptide processing and targeting in the neuronal secretory pathway (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-15
    Description: The abdominal ganglion of the marine mollusk Aplysia contains a pair of identified neuronal clusters, the bag cells, which control egg laying by means of a number of unique regulatory mechanisms. Each neuron in the bag cell clusters synthesizes several peptides derived from a single prohormone and packages them into separate vesicles. These vesicles are then differentially localized in specific neuronal processes, thus segregating peptides destined for autocrine and hormonal release sites. Therefore in this system, protein trafficking through the secretory pathway organizes multiple peptide neurochemical messengers to efficiently regulate simple behaviors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jung, L J -- Scheller, R H -- New York, N.Y. -- Science. 1991 Mar 15;251(4999):1330-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Beckman Center, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2003219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aplysia/genetics/*physiology ; Cell Compartmentation ; Cloning, Molecular ; DNA/genetics ; Invertebrate Hormones/genetics/*metabolism ; Neuropeptides/*physiology ; Neurosecretory Systems/*physiology ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Sexual Behavior, Animal/physiology ; Transfection
    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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    Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-10
    Description: Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Two 35-kilodalton proteins (p35 or syntaxins) were identified that interact with the synaptic vesicle protein p65 (synaptotagmin). The p35 proteins are expressed only in the nervous system, are 84 percent identical, include carboxyl-terminal membrane anchors, and are concentrated on the plasma membrane at synaptic sites. An antibody to p35 immunoprecipitated solubilized N-type calcium channels. The p35 proteins may function in docking synaptic vesicles near calcium channels at presynaptic active zones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, M K -- Calakos, N -- Scheller, R H -- 2T32G07365/PHS HHS/ -- New York, N.Y. -- Science. 1992 Jul 10;257(5067):255-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University Medical Center, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1321498" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens, Surface ; *Calcium-Binding Proteins ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Membrane Glycoproteins/physiology ; Molecular Sequence Data ; Nerve Tissue Proteins/isolation & purification/*physiology ; Oligonucleotide Probes ; Rats ; Sequence Homology, Nucleic Acid ; Synaptic Transmission/physiology ; Synaptic Vesicles/*physiology ; Synaptotagmin I ; Synaptotagmins ; Syntaxin 1
    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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    SV2, a brain synaptic vesicle protein homologous to bacterial transporters (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-28
    Description: Synaptic vesicle protein 2 (SV2) is a membrane glycoprotein specifically localized to secretory vesicles in neurons and endocrine cells. As a first step toward understanding the function of SV2 in neural secretion, a rat brain complementary DNA (cDNA) that encodes SV2 was isolated and characterized. Analyses of this cDNA predict that SV2 contains 12 transmembrane domains. The NH2-terminal half of the protein shows significant amino acid sequence identity to a family of bacterial proteins that transport sugars, citrate, and drugs. Expression of the SV2 cDNA in COS cells yielded a high level of SV2-like immunoreactivity distributed in a reticular and punctate pattern, which suggests localization to intracellular membranes. Its localization to vesicles, predicted membrane topology, and sequence identity to known transporters suggest that SV2 is a synaptic vesicle-specific transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bajjalieh, S M -- Peterson, K -- Shinghal, R -- Scheller, R H -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1271-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519064" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/genetics ; Brain/*metabolism ; Carrier Proteins/genetics ; DNA/isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/genetics ; Membrane Glycoproteins/*genetics ; Molecular Sequence Data ; Nerve Tissue Proteins/*genetics ; Polymerase Chain Reaction ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
    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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    Presynaptic component of long-term potentiation visualized at individual hippocampal synapses (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-16
    Description: Long-term potentiation has previously been studied with electrophysiological techniques that do not readily separate presynaptic and postsynaptic contributions. Changes in exocytotic-endocytotic cycling have now been monitored at synapses between cultured rat hippocampal neurons by measuring the differential uptake of antibodies that recognize the intraluminal domain of the synaptic vesicle protein synaptotagmin. Vesicular cycling increased markedly during glutamate-induced long-term potentiation. The degree of potentiation was heterogeneous, appearing greater at synapses at which the initial extent of vesicular turnover was low. Thus, changes in presynaptic activity were visualized directly and the spatial distribution of potentiation could be determined at the level of single synaptic boutons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malgaroli, A -- Ting, A E -- Wendland, B -- Bergamaschi, A -- Villa, A -- Tsien, R W -- Scheller, R H -- D.016/Telethon/Italy -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1624-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scientific Institute San Raffaele, Milan, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7777862" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Calcium-Binding Proteins ; Cells, Cultured ; Glutamic Acid/pharmacology ; Hippocampus/*cytology/physiology ; Long-Term Potentiation/drug effects/*physiology ; Membrane Glycoproteins/analysis/immunology ; Molecular Sequence Data ; Nerve Tissue Proteins/analysis/immunology ; Neurons/*physiology ; Patch-Clamp Techniques ; Potassium/pharmacology ; Presynaptic Terminals/drug effects/*physiology ; Pyrroles/pharmacology ; Rats ; Receptors, N-Methyl-D-Aspartate/physiology ; *Synaptic Transmission/drug effects ; Synaptic Vesicles/chemistry/metabolism ; Synaptotagmins
    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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    Single cells as biosensors for chemical separations (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-06
    Description: A biosensor system based on the response of living cells was demonstrated that can detect specific components of a complex mixture fractionated by a microcolumn separation technique. This system uses ligand-receptor binding and signal-transduction pathways to biochemically amplify the presence of an analyte after electrophoretic separation. The transduced signal was measured by means of two approaches: (i) fluorescence determination of intracellular calcium concentrations in one or more rat PC-12 cells and (ii) measurement of transmembrane current in a Xenopus laevis oocyte microinjected with messenger RNA that encodes a specific receptor. This analysis system has the potential to identify biologically active ligands present in a complex mixture with exceptional sensitivity and selectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shear, J B -- Fishman, H A -- Allbritton, N L -- Garigan, D -- Zare, R N -- Scheller, R H -- MH45324-05/MH/NIMH NIH HHS/ -- MH45423-03/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):74-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809609" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/analysis/isolation & purification ; Adenosine Triphosphate/analysis/isolation & purification ; Animals ; *Biosensing Techniques ; Bradykinin/analysis/isolation & purification ; Calcium/analysis ; Chemistry Techniques, Analytical/*methods ; Electrophoresis ; Ligands ; Microscopy, Fluorescence ; Oocytes ; PC12 Cells ; Patch-Clamp Techniques ; Rats ; Reproducibility of Results ; Sensitivity and Specificity ; Serotonin/analysis/isolation & purification ; Signal Transduction ; Xenopus laevis
    Print ISSN: 0036-8075
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  • 8
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    Patch-clamp detection of neurotransmitters in capillary electrophoresis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-21
    Description: Gamma-aminobutyrate acid, L-glutamate, and N-methyl-D-aspartate were separated by capillary electrophoresis and detected by the use of whole-cell and outside-out patch-clamp techniques on freshly dissociated rat olfactory interneurons. These neuroactive compounds could be identified from their electrophoretic migration times, unitary channel conductances, and power spectra that yielded corner frequencies and mean single-channel conductances characteristic for each of the different agonist-receptor interactions. This technique has the sensitivity to observe the opening of a single ion channel for agonists separated by capillary electrophoresis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orwar, O -- Jardemark, K -- Jacobson, I -- Moscho, A -- Fishman, H A -- Scheller, R H -- Zare, R N -- DA 09873-01/DA/NIDA NIH HHS/ -- MH 45423-06/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1779-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Stanford University, California 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650575" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biosensing Techniques ; Electrophoresis, Capillary ; Glutamic Acid/*analysis/isolation & purification ; Interneurons/*chemistry ; Ion Channels/physiology ; N-Methylaspartate/*analysis/isolation & purification ; Olfactory Bulb/cytology ; Patch-Clamp Techniques ; Rats ; Receptors, GABA/physiology ; Receptors, Glutamate/physiology ; Receptors, N-Methyl-D-Aspartate/physiology ; Sensitivity and Specificity ; gamma-Aminobutyric Acid/*analysis/isolation & purification
    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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  • 9
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    Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-25
    Description: Intracellular vesicles destined to fuse with the plasma membrane and secrete their contents must have a mechanism for specifically interacting with the appropriate target membrane. Such a mechanism is now suggested by the demonstration of specific interaction between vesicular proteins and plasma membrane proteins. The vesicle-associated membrane proteins (VAMPs) 1 and 2 specifically bind the acceptor membrane proteins syntaxin 1A and 4 but not syntaxin 2 or 3. The binding site is within amino acids 194 to 267 of syntaxin 1A, and the approximate equilibrium dissociation constants is 4.7 x 10(-6) molar. These data suggest a physical basis for the specificity of intracellular vesicular transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Calakos, N -- Bennett, M K -- Peterson, K E -- Scheller, R H -- New York, N.Y. -- Science. 1994 Feb 25;263(5150):1146-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University Medical Center, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8108733" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/*metabolism ; Binding Sites ; Cell Line ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Haplorhini ; Kinetics ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Nerve Tissue Proteins/*metabolism ; R-SNARE Proteins ; Recombinant Fusion Proteins/metabolism ; Synaptic Vesicles/*metabolism ; Syntaxin 1
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Molecular neurobiology--a conference sponsored by the NIMH (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scheller, R H -- Barchas, J D -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):13-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2902686" target="_blank"〉PubMed〈/a〉
    Keywords: Congresses as Topic ; *National Institute of Mental Health (U.S.) ; *Neurobiology ; United States ; *United States Substance Abuse and Mental Health Services Administration
    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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