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  • 1
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    Specific covalent labeling of recombinant protein molecules inside live cells (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-10
    Description: Recombinant proteins containing four cysteines at the i, i + 1, i + 4, and i + 5 positions of an alpha helix were fluorescently labeled in living cells by extracellular administration of 4',5'-bis(1,3, 2-dithioarsolan-2-yl)fluorescein. This designed small ligand is membrane-permeant and nonfluorescent until it binds with high affinity and specificity to the tetracysteine domain. Such in situ labeling adds much less mass than does green fluorescent protein and offers greater versatility in attachment sites as well as potential spectroscopic and chemical properties. This system provides a recipe for slightly modifying a target protein so that it can be singled out from the many other proteins inside live cells and fluorescently stained by small nonfluorescent dye molecules added from outside the cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Griffin, B A -- Adams, S R -- Tsien, R Y -- NS27177/NS/NINDS NIH HHS/ -- T32 CA09523/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Jul 10;281(5374):269-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, CA 92093-0647, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9657724" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calmodulin/chemistry/genetics/metabolism ; Cell Membrane Permeability ; Cell Survival ; Cysteine/*chemistry ; Energy Transfer ; Ethylene Glycol ; Fluoresceins/chemical synthesis/chemistry/*metabolism ; Fluorescence ; *Fluorescent Dyes ; Green Fluorescent Proteins ; HeLa Cells ; Humans ; Jurkat Cells ; Ligands ; Luminescent Proteins/chemistry/genetics/metabolism ; Molecular Sequence Data ; Organometallic Compounds/chemical synthesis/chemistry/*metabolism ; Peptides/chemistry/*metabolism ; Protein Structure, Secondary ; Recombinant Proteins/chemistry/*metabolism ; Spectrometry, Fluorescence ; 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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  • 2
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    Quantitation of transcription and clonal selection of single living cells with beta-lactamase as reporter (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-24
    Description: Gene expression was visualized in single living mammalian cells with beta-lactamase as a reporter that hydrolyzes a substrate loaded intracellularly as a membrane-permeant ester. Each enzyme molecule changed the fluorescence of many substrate molecules from green to blue by disrupting resonance energy transfer. This wavelength shift was detectable by eye or color film in individual cells containing less than 100 beta-lactamase molecules. The robust change in emission ratio reveals quantitative heterogeneity in real-time gene expression, enables clonal selection by flow cytometry, and forms a basis for high-throughput screening of pharmaceutical candidate drugs in living mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zlokarnik, G -- Negulescu, P A -- Knapp, T E -- Mere, L -- Burres, N -- Feng, L -- Whitney, M -- Roemer, K -- Tsien, R Y -- NS27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jan 2;279(5347):84-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aurora Biosciences, 11010 Torreyana Road, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9417030" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Separation/methods ; Clone Cells/*metabolism ; DNA-Binding Proteins/genetics/metabolism ; Drug Evaluation, Preclinical ; Energy Transfer ; Flow Cytometry ; Fluoresceins/metabolism ; Fluorescent Dyes/metabolism ; *Gene Expression ; *Genes, Reporter ; Half-Life ; Humans ; *Lactams ; Muscarinic Agonists/pharmacology ; Muscarinic Antagonists/pharmacology ; NFATC Transcription Factors ; *Nuclear Proteins ; Sensitivity and Specificity ; Spectrometry, Fluorescence ; Transcription Factors/genetics/metabolism ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; Umbelliferones/metabolism ; beta-Lactamases/*genetics/metabolism ; beta-Lactams/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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  • 3
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    Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-07-06
    Description: Heterozygous mutations encoding abnormal forms of the death receptor Fas dominantly interfere with Fas-induced lymphocyte apoptosis in human autoimmune lymphoproliferative syndrome. This effect, rather than depending on ligand-induced receptor oligomerization, was found to stem from ligand- independent interaction of wild-type and mutant Fas receptors through a specific region in the extracellular domain. Preassociated Fas complexes were found in living cells by means of fluorescence resonance energy transfer between variants of green fluorescent protein. These results show that formation of preassociated receptor complexes is necessary for Fas signaling and dominant interference in human disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siegel, R M -- Frederiksen, J K -- Zacharias, D A -- Chan, F K -- Johnson, M -- Lynch, D -- Tsien, R Y -- Lenardo, M J -- NS27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2354-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875918" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD95/*chemistry/genetics/*metabolism ; *Apoptosis ; Autoimmune Diseases/physiopathology ; Cell Line ; Cell Membrane/metabolism ; Cross-Linking Reagents ; Fas Ligand Protein ; Humans ; Ligands ; Lymphocytes/cytology ; Lymphoproliferative Disorders/physiopathology ; Macromolecular Substances ; Membrane Glycoproteins/*metabolism ; Mice ; Mutation ; Point Mutation ; Recombinant Fusion Proteins/chemistry/metabolism ; *Signal Transduction ; Succinimides ; Tumor Cells, Cultured
    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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    Alteration of stimulus-specific guard cell calcium oscillations and stomatal closing in Arabidopsis det3 mutant (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-29
    Description: Cytosolic calcium oscillations control signaling in animal cells, whereas in plants their importance remains largely unknown. In wild-type Arabidopsis guard cells abscisic acid, oxidative stress, cold, and external calcium elicited cytosolic calcium oscillations of differing amplitudes and frequencies and induced stomatal closure. In guard cells of the V-ATPase mutant det3, external calcium and oxidative stress elicited prolonged calcium increases, which did not oscillate, and stomatal closure was abolished. Conversely, cold and abscisic acid elicited calcium oscillations in det3, and stomatal closure occurred normally. Moreover, in det3 guard cells, experimentally imposing external calcium-induced oscillations rescued stomatal closure. These data provide genetic evidence that stimulus-specific calcium oscillations are necessary for stomatal closure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allen, G J -- Chu, S P -- Schumacher, K -- Shimazaki, C T -- Vafeados, D -- Kemper, A -- Hawke, S D -- Tallman, G -- Tsien, R Y -- Harper, J F -- Chory, J -- Schroeder, J I -- R01 GM60396-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 29;289(5488):2338-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell and Developmental Biology Section, Division of Biology and Center for Molecular Genetics, University of California, San Diego, La Jolla, CA 92093-0116, USA. gallen@biomail.ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11009417" target="_blank"〉PubMed〈/a〉
    Keywords: Abscisic Acid/pharmacology ; Arabidopsis/cytology/genetics/*physiology ; Calcium/metabolism ; *Calcium Signaling ; Cell Membrane/metabolism ; Cold Temperature ; Endoplasmic Reticulum/metabolism ; Genes, Plant ; Hydrogen Peroxide/pharmacology ; Membrane Potentials ; Mutation ; Oxidative Stress ; Plant Leaves/cytology/*physiology ; Potassium/metabolism ; Proton-Translocating ATPases/genetics/metabolism ; *Vacuolar Proton-Translocating ATPases ; Vacuoles/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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  • 5
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    Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: Many proteins associated with the plasma membrane are known to partition into submicroscopic sphingolipid- and cholesterol-rich domains called lipid rafts, but the determinants dictating this segregation of proteins in the membrane are poorly understood. We suppressed the tendency of Aequorea fluorescent proteins to dimerize and targeted these variants to the plasma membrane using several different types of lipid anchors. Fluorescence resonance energy transfer measurements in living cells revealed that acyl but not prenyl modifications promote clustering in lipid rafts. Thus the nature of the lipid anchor on a protein is sufficient to determine submicroscopic localization within the plasma membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zacharias, David A -- Violin, Jonathan D -- Newton, Alexandra C -- Tsien, Roger Y -- 2T32 GM07752/GM/NIGMS NIH HHS/ -- DK54441/DK/NIDDK NIH HHS/ -- NS27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):913-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Biomedical Sciences Graduate Program, and, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093-0647, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988576" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Animals ; Bacterial Proteins/chemistry/*metabolism ; Caveolin 1 ; Caveolins/metabolism ; Cell Line ; Detergents ; Dimerization ; Dogs ; Energy Transfer ; Fluorescence ; Green Fluorescent Proteins ; Luminescent Proteins/chemistry/*metabolism ; Membrane Microdomains/*metabolism ; Myristic Acid/metabolism ; Oligopeptides/chemistry/*metabolism ; Palmitic Acid/metabolism ; Protein Prenylation ; Recombinant Fusion Proteins/metabolism ; Solubility ; Spectrometry, Fluorescence ; 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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    Generation of calcium oscillations in fibroblasts by positive feedback between calcium and IP3 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-01-04
    Description: A wide variety of nonexcitable cells generate repetitive transient increases in cytosolic calcium ion concentration ([Ca2+]i) when stimulated with agonists that engage the phosphoinositide signalling pathway. Current theories regarding the mechanisms of oscillation disagree on whether Ca2+ inhibits or stimulates its own release from internal stores and whether inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DG) also undergo oscillations linked to the Ca2+ spikes. In this study, Ca2+ was found to stimulate its own release in REF52 fibroblasts primed by mitogens plus depolarization. However, unlike Ca2+ release in muscle and nerve cells, this amplification was insensitive to caffeine or ryanodine and required hormone receptor occupancy and functional IP3 receptors. Oscillations in [Ca2+]i were accompanied by oscillations in IP3 concentration but did not require functional protein kinase C. Therefore, the dominant feedback mechanism in this cell type appears to be Ca2+ stimulation of phospholipase C once this enzyme has been activated by hormone receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harootunian, A T -- Kao, J P -- Paranjape, S -- Tsien, R Y -- GM 31004/GM/NIGMS NIH HHS/ -- NS 27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1991 Jan 4;251(4989):75-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute M-047, University of California San Diego, La Jolla 92093-0647.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1986413" target="_blank"〉PubMed〈/a〉
    Keywords: Caffeine/pharmacology ; Calcium/*metabolism/pharmacology ; Cell Line ; Cytosol/metabolism ; Feedback ; Fibroblasts/drug effects/*metabolism ; Heparin/pharmacology ; Inositol 1,4,5-Trisphosphate/*metabolism ; Ionomycin/pharmacology ; *Periodicity ; Phorbol 12,13-Dibutyrate/pharmacology ; Protein Kinase C/antagonists & inhibitors/metabolism ; Ryanodine/pharmacology ; Type C Phospholipases/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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  • 7
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    The fluorescent toolbox for assessing protein location and function (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-15
    Description: Advances in molecular biology, organic chemistry, and materials science have recently created several new classes of fluorescent probes for imaging in cell biology. Here we review the characteristic benefits and limitations of fluorescent probes to study proteins. The focus is on protein detection in live versus fixed cells: determination of protein expression, localization, activity state, and the possibility for combination of fluorescent light microscopy with electron microscopy. Small organic fluorescent dyes, nanocrystals ("quantum dots"), autofluorescent proteins, small genetic encoded tags that can be complexed with fluorochromes, and combinations of these probes are highlighted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giepmans, Ben N G -- Adams, Stephen R -- Ellisman, Mark H -- Tsien, Roger Y -- GM 72033/GM/NIGMS NIH HHS/ -- NS27177/NS/NINDS NIH HHS/ -- RR04050/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):217-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Microscopy and Imaging Research, Center for Research in Biological Systems, Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614209" target="_blank"〉PubMed〈/a〉
    Keywords: Diffusion ; Enzymes/metabolism ; Fluorescence ; Fluorescence Resonance Energy Transfer ; Fluorescent Antibody Technique ; *Fluorescent Dyes/chemistry ; Genetic Techniques ; Immunohistochemistry ; *Luminescent Proteins/chemistry/genetics ; Microscopy, Electron ; *Molecular Probe Techniques ; Protein Conformation ; Protein Transport ; Proteins/*analysis/chemistry/metabolism/*physiology ; *Quantum Dots
    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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  • 8
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    Multicolor and electron microscopic imaging of connexin trafficking (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: Recombinant proteins containing tetracysteine tags can be successively labeled in living cells with different colors of biarsenical fluorophores so that older and younger protein molecules can be sharply distinguished by both fluorescence and electron microscopy. Here we used this approach to show that newly synthesized connexin43 was transported predominantly in 100- to 150-nanometer vesicles to the plasma membrane and incorporated at the periphery of existing gap junctions, whereas older connexins were removed from the center of the plaques into pleiomorphic vesicles of widely varying sizes. Selective imaging by correlated optical and electron microscopy of protein molecules of known ages will clarify fundamental processes of protein trafficking in situ.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaietta, Guido -- Deerinck, Thomas J -- Adams, Stephen R -- Bouwer, James -- Tour, Oded -- Laird, Dale W -- Sosinsky, Gina E -- Tsien, Roger Y -- Ellisman, Mark H -- DC03192/DC/NIDCD NIH HHS/ -- NS14718/NS/NINDS NIH HHS/ -- NS27177/NS/NINDS NIH HHS/ -- P01 DK54441/DK/NIDDK NIH HHS/ -- R01 GM065937/GM/NIGMS NIH HHS/ -- RR04050/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):503-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Microscopy and Imaging Research, Department of Neurosciences, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964472" target="_blank"〉PubMed〈/a〉
    Keywords: 3,3'-Diaminobenzidine/chemistry ; Amino Acid Motifs ; Animals ; Arsenicals/metabolism ; Cell Line ; Cell Membrane/metabolism/ultrastructure ; Connexin 43/biosynthesis/*metabolism ; Cysteine/chemistry ; Endocytosis ; Exocytosis ; Fluoresceins/metabolism ; Fluorescence ; Fluorescent Dyes/metabolism ; Gap Junctions/*metabolism/ultrastructure ; HeLa Cells ; Humans ; Microscopy, Confocal ; Microscopy, Electron ; Microscopy, Immunoelectron ; Organometallic Compounds/metabolism ; Oxazines/metabolism ; Patch-Clamp Techniques ; Protein Transport ; Recombinant Proteins/metabolism ; Transport Vesicles/*metabolism/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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  • 9
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    Seeing the machinery of live cells (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsien, R Y -- Miyawaki, A -- NS27177/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1954-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093-0647, USA. rtsien@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9669950" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biochemistry/*methods ; *Cell Physiological Phenomena ; Flow Cytometry ; *Fluorescent Dyes ; Gene Expression ; Green Fluorescent Proteins ; *Indicators and Reagents ; *Luminescent Proteins ; Proteins/analysis ; Recombinant Fusion 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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  • 10
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    Engineering a memory with LTD and LTP (2014)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2014-06-05
    Description: It has been proposed that memories are encoded by modification of synaptic strengths through cellular mechanisms such as long-term potentiation (LTP) and long-term depression (LTD). However, the causal link between these synaptic processes and memory has been difficult to demonstrate. Here we show that fear conditioning, a type of associative memory, can be inactivated and reactivated by LTD and LTP, respectively. We began by conditioning an animal to associate a foot shock with optogenetic stimulation of auditory inputs targeting the amygdala, a brain region known to be essential for fear conditioning. Subsequent optogenetic delivery of LTD conditioning to the auditory input inactivates memory of the shock. Then subsequent optogenetic delivery of LTP conditioning to the auditory input reactivates memory of the shock. Thus, we have engineered inactivation and reactivation of a memory using LTD and LTP, supporting a causal link between these synaptic processes and memory.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4210354/" 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/PMC4210354/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nabavi, Sadegh -- Fox, Rocky -- Proulx, Christophe D -- Lin, John Y -- Tsien, Roger Y -- Malinow, Roberto -- MH049159/MH/NIMH NIH HHS/ -- NS27177/NS/NINDS NIH HHS/ -- R01 AG032132/AG/NIA NIH HHS/ -- R01 MH049159/MH/NIMH NIH HHS/ -- R01 MH091119/MH/NIMH NIH HHS/ -- R01 NS027177/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2014 Jul 17;511(7509):348-52. doi: 10.1038/nature13294. Epub 2014 Jun 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Center for Neural Circuits and Behavior, Department of Neuroscience and Section of Neurobiology, University of California at San Diego, California 92093, USA [2]. ; Center for Neural Circuits and Behavior, Department of Neuroscience and Section of Neurobiology, University of California at San Diego, California 92093, USA. ; Department of Pharmacology, University of California at San Diego, California 92093, USA. ; 1] Department of Pharmacology, University of California at San Diego, California 92093, USA [2] Howard Hughes Medical Institute, University of California at San Diego, California 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24896183" target="_blank"〉PubMed〈/a〉
    Keywords: Amygdala/physiology ; Animals ; Conditioning (Psychology)/physiology ; Electric Stimulation ; Electrophysiology ; Fear/physiology/psychology ; Long-Term Potentiation/*physiology ; Long-Term Synaptic Depression/*physiology ; Male ; Memory/*physiology ; Optogenetics ; Rats ; Rats, Sprague-Dawley ; Synapses/*physiology ; Synaptic Transmission
    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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