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  • 1
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    Interaction of RAFT1 with gephyrin required for rapamycin-sensitive signaling (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-15
    Description: RAFT1 (rapamycin and FKBP12 target 1; also called FRAP or mTOR) is a member of the ATM (ataxia telangiectasia mutated)-related family of proteins and functions as the in vivo mediator of the effects of the immunosuppressant rapamycin and as an important regulator of messenger RNA translation. In mammalian cells RAFT1 interacted with gephyrin, a widely expressed protein necessary for the clustering of glycine receptors at the cell membrane of neurons. RAFT1 mutants that could not associate with gephyrin failed to signal to downstream molecules, including the p70 ribosomal S6 kinase and the eIF-4E binding protein, 4E-BP1. The interaction with gephyrin ascribes a function to the large amino-terminal region of an ATM-related protein and reveals a role in signal transduction for the clustering protein gephyrin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sabatini, D M -- Barrow, R K -- Blackshaw, S -- Burnett, P E -- Lai, M M -- Field, M E -- Bahr, B A -- Kirsch, J -- Betz, H -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- DA-00266/DA/NIDA NIH HHS/ -- GM-07309/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 May 14;284(5417):1161-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Johns Hopkins University School of Medicine, Department of Neuroscience, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10325225" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Gene Expression ; HeLa Cells ; Humans ; Membrane Proteins/*metabolism ; Molecular Sequence Data ; Mutation ; Phosphoproteins/*metabolism ; Phosphorylation ; *Phosphotransferases (Alcohol Group Acceptor) ; Rats ; Receptors, Glycine/metabolism ; Repressor Proteins/metabolism ; Ribosomal Protein S6 Kinases/*metabolism ; *Signal Transduction ; Sirolimus/*pharmacology ; TOR Serine-Threonine Kinases
    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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    Nitric oxide: first in a new class of neurotransmitters (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Snyder, S H -- DA-00266/DA/NIDA NIH HHS/ -- DA-271-90-7408/DA/NIDA NIH HHS/ -- MH-18501/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Jul 24;257(5069):494-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1353273" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*physiology ; Models, Neurological ; Muscle, Smooth, Vascular/physiology ; Neurons/*physiology ; Neurotransmitter Agents/*metabolism ; Nitric Oxide/*metabolism ; Second Messenger Systems ; Vasodilation
    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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    Schizophrenia: diverse approaches to a complex disease (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-27
    Description: Schizophrenia is a debilitating mental illness that affects 1% of the population. Despite intensive study, its molecular etiology remains enigmatic. Like many common diseases, schizophrenia is multifactorial in origin, with both genetic and environmental contributions likely playing an important role in the manifestation of symptoms. Recent advances based on pharmacological studies, brain imaging analyses, and genetic research are now converging on tantalizing leads that point to a central role for several neurotransmitters, including dopamine, glutamate, and serotonin, that may interface with neurodevelopmental defects reflecting disease-related genetic aberrations. Here, we provide a brief overview of the parallel approaches being used to identify the molecular causes of schizophrenia and discuss possible directions for future research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sawa, Akira -- Snyder, Solomon H -- DA-00074/DA/NIDA NIH HHS/ -- DA-00266/DA/NIDA NIH HHS/ -- MH-18501/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 26;296(5568):692-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976442" target="_blank"〉PubMed〈/a〉
    Keywords: Antipsychotic Agents/pharmacology/therapeutic use ; Brain/metabolism/pathology ; Chromosome Mapping ; Disease Susceptibility ; Genetic Predisposition to Disease ; Humans ; Mutation ; Neurotransmitter Agents/metabolism ; Polymorphism, Genetic ; Receptors, Neurotransmitter/metabolism ; Risk Factors ; Schizophrenia/*etiology/genetics/metabolism/pathology
    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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    Genetics. Two genes link two distinct psychoses (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sawa, Akira -- Snyder, Solomon H -- New York, N.Y. -- Science. 2005 Nov 18;310(5751):1128-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA. asawa1@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293746" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/*genetics/physiology ; Affective Disorders, Psychotic/enzymology/*genetics ; Carrier Proteins/physiology ; Cyclic AMP/metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 4 ; Enzyme Activation ; Humans ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Protein Binding ; Schizophrenia/*genetics ; Signal Transduction ; Translocation, Genetic
    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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    Phosphorylation of proteins by inositol pyrophosphates (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: The inositol pyrophosphates IP7 and IP8 contain highly energetic pyrophosphate bonds. Although implicated in various biologic functions, their molecular sites of action have not been clarified. Using radiolabeled IP7, we detected phosphorylation of multiple eukaryotic proteins. We also observed phosphorylation of endogenous proteins by endogenous IP7 in yeast. Phosphorylation by IP7 is nonenzymatic and may represent a novel intracellular signaling mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saiardi, Adolfo -- Bhandari, Rashna -- Resnick, Adam C -- Snowman, Adele M -- Snyder, Solomon H -- DA00074/DA/NIDA NIH HHS/ -- MH068830-02/MH/NIMH NIH HHS/ -- MH18501/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2101-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604408" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Escherichia coli Proteins/metabolism ; Humans ; Inositol Phosphates/*metabolism ; Kinetics ; Magnesium/metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/chemistry/*metabolism ; Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Phosphate Group Acceptor)/metabolism ; Protein Kinases/genetics/metabolism ; Proteins/*metabolism ; RNA-Binding Proteins/chemistry/*metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Serine/metabolism ; Signal Transduction ; Temperature
    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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    Endothelial NOS and the blockade of LTP by NOS inhibitors in mice lacking neuronal NOS (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-22
    Description: Long-term potentiation (LTP) is a persistent increase in synaptic strength implicated in certain forms of learning and memory. In the CA1 region of the hippocampus, LTP is thought to involve the release of one or more retrograde messengers from the postsynaptic cell that act on the presynaptic terminal to enhance transmitter release. One candidate retrograde messenger is the membrane-permeant gas nitric oxide (NO), which in the brain is released after activation of the neuronal-specific NO synthase isoform (nNOS). To assess the importance of NO in hippocampal synaptic plasticity, LTP was examined in mice where the gene encoding nNOS was disrupted by gene targeting. In nNOS- mice, LTP induced by weak intensity tetanic stimulation was normal except for a slight reduction in comparison to that in wild-type mice and was blocked by NOS inhibitors, just as it was in wild-type mice. Immunocytochemical studies indicate that in the nNOS- mice as in wild-type mice, the endothelial form of NOS (eNOS) is expressed in CA1 neurons. These findings suggest that eNOS, rather than nNOS, generates NO within the postsynaptic cell during LTP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Dell, T J -- Huang, P L -- Dawson, T M -- Dinerman, J L -- Snyder, S H -- Kandel, E R -- Fishman, M C -- DA-00074/DA/NIDA NIH HHS/ -- DA-00266/DA/NIDA NIH HHS/ -- MH-45923/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1994 Jul 22;265(5171):542-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, College of Physicians and Surgeons of Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7518615" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/antagonists & inhibitors/genetics/*metabolism ; Animals ; Arginine/*analogs & derivatives/pharmacology ; Electric Stimulation ; Endothelium/enzymology ; Hippocampus/drug effects/enzymology/*physiology ; In Vitro Techniques ; *Long-Term Potentiation/drug effects ; Mice ; Mutation ; Nitric Oxide/*metabolism ; Nitric Oxide Synthase ; Nitroarginine ; Pyramidal Cells/drug effects/enzymology/*physiology ; Synaptic Transmission/drug effects
    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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    Solubilized adenosine receptors in the brain: regulation of guanine nucleotides (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-03-26
    Description: Adenosine receptors associated with a reduction of adenylate cyclase and labeled by tritium-labeled cyclohexyladenosine can be solubilized from brain membranes with sodium cholate. Regulation of receptor binding by guanine nucleotides is retained in the soluble state. Influences of cations observed in membrane preparations of adenosine receptors are no longer detected with the solubilized receptors. The apparent retention of a complex of receptors and guanosine triphosphate binding but not cation binding protein in the soluble state may permit a molecular analysis of receptor regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gavish, M -- Goodman, R R -- Snyder, S H -- DA-00266/DA/NIDA NIH HHS/ -- MH-18501/MH/NIMH NIH HHS/ -- NS-16375/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1982 Mar 26;215(4540):1633-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6280275" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/*physiology ; Animals ; Brain/*physiology ; Cations, Divalent/pharmacology ; Cattle ; Cell Membrane/metabolism ; Guanine Nucleotides/*pharmacology ; Receptors, Cell Surface/*drug effects ; Receptors, Purinergic ; Solubility
    Print ISSN: 0036-8075
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  • 8
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    Two distinct central serotonin receptors with different physiological functions (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-05-15
    Description: Two distinct serotonin (5-hydroxytryptamine) receptors designated serotonin 1 and serotonin 2 bind tritium-labeled serotonin and tritium-labeled spiroperidol, respectively. Drug potencies at serotonin 2 sites, but not at serotonin 1 sites, predict their effects on the "serotonin behavioral syndrome," indicating that serotonin 2 sites mediate these behaviors. The limited correlation of drug effects with regulation by guanine nucleotides suggests that serotonin 1 sites might be linked to adenylate cyclase. Drug specificities of serotonin-elicited synaptic inhibition and excitation may reflect serotonin 1 and serotonin 2 receptor interactions, respectively.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peroutka, S J -- Lebovitz, R M -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1981 May 15;212(4496):827-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7221567" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Animals ; Behavior, Animal/*physiology ; Brain/*physiology ; Guanine Nucleotides/physiology ; Kinetics ; Male ; Rats ; Receptors, Serotonin/*physiology ; Serotonin/metabolism ; Spiperone/metabolism ; Structure-Activity Relationship
    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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  • 9
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    Brain peptides as neurotransmitters (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-08-29
    Description: Numerous peptides appear to be neurotransmitter candidates in the brain. Some, such as the opioid peptide enkephalins, neurotensin, and substance P, were first isolaterd from the brain. Peptides, such as cholecystokinin and vasoactive intestinal polypeptide, were known as intestinal hormones and later recognized as brain constituents. Certain hypothalamic-releasing hormones, pituitary peptides, and blood-derived peptides like angiotensin II and bradykinin, may also be central neurotransmitters. The diversity of localization of these peptides throughout the brain implies a multiplicity of potential roles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Snyder, S H -- New York, N.Y. -- Science. 1980 Aug 29;209(4460):976-83.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6157191" target="_blank"〉PubMed〈/a〉
    Keywords: Angiotensins/physiology ; Animals ; Bradykinin/physiology ; Brain/*physiology ; Carnosine/physiology ; Cholecystokinin/physiology ; Endorphins/physiology ; Gastrins/physiology ; Glucagon/physiology ; Humans ; Insulin/physiology ; Nerve Tissue Proteins/physiology ; Neurotensin/physiology ; Peptides/*physiology ; Pituitary Hormone-Releasing Hormones/physiology ; Receptors, Opioid/physiology ; Substance P/physiology ; Vasoactive Intestinal Peptide/physiology ; Vasopressins/physiology
    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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