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  • Articles  (60)
  • Rats  (60)
  • Cell & Developmental Biology
  • 2000-2004  (60)
  • 1980-1984
  • 2002  (60)
  • Chemistry and Pharmacology  (60)
  • Biology  (60)
  • Electrical Engineering, Measurement and Control Technology
  • Energy, Environment Protection, Nuclear Power Engineering
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  • Articles  (60)
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  • 2000-2004  (60)
  • 1980-1984
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  • 1
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    Cancer. BRCA2 enters the fray (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, John H -- Elledge, Stephen J -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1822-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228708" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; BRCA1 Protein/metabolism ; BRCA2 Protein/*chemistry/*metabolism ; Binding Sites ; Breast Neoplasms/genetics ; Crystallography, X-Ray ; DNA/*metabolism ; DNA Damage ; *DNA Repair ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/metabolism ; Female ; Genes, BRCA1 ; Genes, BRCA2 ; Genetic Predisposition to Disease ; Humans ; Mice ; Ovarian Neoplasms/genetics ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rad51 Recombinase ; Rats ; Recombination, Genetic ; Replication Protein A
    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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    Control of synaptic strength by glial TNFalpha (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: Activity-dependent modulation of synaptic efficacy in the brain contributes to neural circuit development and experience-dependent plasticity. Although glia are affected by activity and ensheathe synapses, their influence on synaptic strength has largely been ignored. Here, we show that a protein produced by glia, tumor necrosis factor alpha (TNFalpha), enhances synaptic efficacy by increasing surface expression of AMPA receptors. Preventing the actions of endogenous TNFalpha has the opposite effects. Thus, the continual presence of TNFalpha is required for preservation of synaptic strength at excitatory synapses. Through its effects on AMPA receptor trafficking, TNFalpha may play roles in synaptic plasticity and modulating responses to neural injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beattie, Eric C -- Stellwagen, David -- Morishita, Wade -- Bresnahan, Jacqueline C -- Ha, Byeong Keun -- Von Zastrow, Mark -- Beattie, Michael S -- Malenka, Robert C -- DA00439/DA/NIDA NIH HHS/ -- MH063394/MH/NIMH NIH HHS/ -- NS 31193/NS/NINDS NIH HHS/ -- NS38079/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2282-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nancy Pritzker Laboratory, Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, Palo Alto, CA 94304, USA. beattie.2@osu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/pharmacology ; Astrocytes/*metabolism ; Cells, Cultured ; Culture Media, Conditioned/pharmacology ; Gene Expression Regulation/drug effects ; Hippocampus/cytology/metabolism ; Neuronal Plasticity/drug effects ; Neurons/drug effects/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/metabolism ; Receptors, Tumor Necrosis Factor ; Receptors, Tumor Necrosis Factor, Type I ; Synapses/drug effects/*metabolism ; Synaptic Transmission/drug effects ; Tumor Necrosis Factor-alpha/antagonists & inhibitors/*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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    BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: Mutations in the BRCA2 (breast cancer susceptibility gene 2) tumor suppressor lead to chromosomal instability due to defects in the repair of double-strand DNA breaks (DSBs) by homologous recombination, but BRCA2's role in this process has been unclear. Here, we present the 3.1 angstrom crystal structure of a approximately 90-kilodalton BRCA2 domain bound to DSS1, which reveals three oligonucleotide-binding (OB) folds and a helix-turn-helix (HTH) motif. We also (i) demonstrate that this BRCA2 domain binds single-stranded DNA, (ii) present its 3.5 angstrom structure bound to oligo(dT)9, (iii) provide data that implicate the HTH motif in dsDNA binding, and (iv) show that BRCA2 stimulates RAD51-mediated recombination in vitro. These findings establish that BRCA2 functions directly in homologous recombination and provide a structural and biochemical basis for understanding the loss of recombination-mediated DSB repair in BRCA2-associated cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Haijuan -- Jeffrey, Philip D -- Miller, Julie -- Kinnucan, Elspeth -- Sun, Yutong -- Thoma, Nicolas H -- Zheng, Ning -- Chen, Phang-Lang -- Lee, Wen-Hwa -- Pavletich, Nikola P -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1837-48.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Sloan-Kettering Division, Joan and Sanford I. Weill Graduate School of Medical Sciences, Cornell University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228710" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; BRCA2 Protein/*chemistry/genetics/*metabolism ; Binding Sites ; Crystallography, X-Ray ; DNA/metabolism ; *DNA Repair ; DNA, Single-Stranded/*metabolism ; DNA-Binding Proteins/metabolism ; Genes, BRCA2 ; Helix-Turn-Helix Motifs ; Humans ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Mice ; Molecular Sequence Data ; Mutation ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/chemistry/*metabolism ; Rad51 Recombinase ; Rats ; *Recombination, 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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  • 4
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    Protein structure. Harmless proteins twist into troublemakers (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2002 Apr 5;296(5565):28-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934996" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid beta-Peptides/chemistry ; Animals ; Humans ; Mice ; Protein Conformation ; *Protein Folding ; *Protein Structure, Quaternary ; Proteins/*chemistry ; Rats
    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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    Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: The second messenger cyclic adenosine monophosphate (cAMP) is the most important modulator of sympathetic control over cardiac contractility. In cardiac myocytes and many other cell types, however, cAMP transduces the signal generated upon stimulation of various receptors and activates different cellular functions, raising the issue of how specificity can be achieved. In the general field of signal transduction, the view is emerging that specificity is guaranteed by tight localization of signaling events. Here, we show that in neonatal rat cardiac myocytes, beta-adrenergic stimulation generates multiple microdomains with increased concentration of cAMP in correspondence with the region of the transverse tubule/junctional sarcoplasmic reticulum membrane. The restricted pools of cAMP show a range of action as small as approximately 1 micrometer, and free diffusion of the second messenger is limited by the activity of phosphodiesterases. Furthermore, we demonstrate that such gradients of cAMP specifically activate a subset of protein kinase A molecules anchored in proximity to the T tubule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaccolo, Manuela -- Pozzan, Tullio -- TCP00089/Telethon/Italy -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1711-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Sciences and Venetian Institute for Molecular Medicine, University of Padua, Via Orus 2, 35129 Padua, Italy. manuela.zaccolo@unipd.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872839" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; A Kinase Anchor Proteins ; Adaptor Proteins, Signal Transducing ; Animals ; Animals, Newborn ; Cells, Cultured ; Colforsin/pharmacology ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Fluorescence ; Green Fluorescent Proteins ; Intracellular Membranes/metabolism ; Kinetics ; Luminescent Proteins ; Myocardium/*cytology/*metabolism/ultrastructure ; Norepinephrine/pharmacology ; Phosphodiesterase Inhibitors/pharmacology ; Proto-Oncogene Proteins/pharmacology ; Rats ; Receptors, Adrenergic, beta/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sarcoplasmic Reticulum/*metabolism ; Second Messenger Systems ; 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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    Partitioning of the matrix fraction of the Golgi apparatus during mitosis in animal cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-02
    Description: The Golgi apparatus is partitioned during mitosis in animal cells by a process of fragmentation, dispersal, and reassembly in each daughter cell. We fractionated the Golgi apparatus in vivo using the drug brefeldin A or a dominant-negative mutant of the Sar1p protein. After these treatments, Golgi enzymes moved back to the endoplasmic reticulum, leaving behind a matrix of Golgi structural proteins. Under these conditions, cells still entered and exited mitosis normally, and their Golgi matrix partitioned in a manner very similar to that of the complete organelle. Thus, the matrix may be the partitioning unit of the Golgi apparatus and may carry the Golgi enzyme-containing membranes into the daughter cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seemann, Joachim -- Pypaert, Marc -- Taguchi, Tomohiko -- Malsam, Jorg -- Warren, Graham -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Ludwig Institute for Cancer Research, Yale University School of Medicine, 333 Cedar Street, Post Office Box 208002, New Haven, CT 06520-8002, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823640" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Animals ; Autoantigens ; Brefeldin A/pharmacology ; Cell Line ; Endoplasmic Reticulum/enzymology ; Golgi Apparatus/*metabolism/ultrastructure ; HeLa Cells ; Humans ; Interphase ; Intracellular Membranes/metabolism/ultrastructure ; Mannosidases/metabolism ; Membrane Proteins/metabolism ; Metaphase ; Microscopy, Electron ; Microscopy, Fluorescence ; *Mitosis ; Monomeric GTP-Binding Proteins/pharmacology ; N-Acetylglucosaminyltransferases/metabolism ; Protein Disulfide-Isomerases/metabolism ; Rats ; *Saccharomyces cerevisiae Proteins ; Telophase ; 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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  • 7
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    Parallel single-cell monitoring of receptor-triggered membrane translocation of a calcium-sensing protein module (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Time courses of translocation of fluorescently conjugated proteins to the plasma membrane were simultaneously measured in thousands of individual rat basophilic leukemia cells. We found that the C2 domain---a calcium-sensing, lipid-binding protein module that is an essential regulator of protein kinase C and numerous other proteins---targeted proteins to the plasma membrane transiently if calcium was released from internal stores, and persistently in response to entry of extracellular calcium across the plasma membrane. The C2 domain translocation time courses of stimulated cells clustered into only two primary modes. Hence, the reversible recruitment of families of signaling proteins from one cellular compartment to another is a rapid bifurcation mechanism for inducing discrete states of cellular signaling networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teruel, Mary N -- Meyer, Tobias -- CA83229/CA/NCI NIH HHS/ -- GM062144/GM/NIGMS NIH HHS/ -- HG00057/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1910-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Stanford University Medical School, 269 Campus Drive, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884760" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins ; Calcium/*metabolism ; *Calcium Signaling ; Cell Membrane/*metabolism ; Cytosol/metabolism ; Fluorescence ; Fluorescent Dyes ; Isoenzymes/chemistry/*metabolism ; Kinetics ; Luminescent Proteins ; Platelet Activating Factor/pharmacology ; Protein Binding ; Protein Kinase C/chemistry/*metabolism ; Protein Structure, Tertiary ; *Protein Transport ; Rats ; Receptors, Cell Surface/*metabolism ; Recombinant Fusion Proteins/metabolism ; Software ; Thapsigargin/pharmacology ; Transfection ; 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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  • 8
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    Development. Putting the brakes on regeneration (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKerracher, Lisa -- Ellezam, Benjamin -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1819-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Pathologie et Biologie Cellulaire, Universite de Montreal, 2900 Edouard-Montpetit, Montreal, Quebec, H3T 1J4 Canada. mckerral@patho.umontreal.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052945" target="_blank"〉PubMed〈/a〉
    Keywords: Amacrine Cells/*physiology ; Animals ; Axonal Transport ; Axons/*physiology ; *Cell Communication ; Cell Differentiation ; Cell Polarity ; Cells, Cultured ; Coculture Techniques ; Dendrites/*physiology ; Embryo, Mammalian ; Nerve Crush ; *Nerve Regeneration ; Optic Nerve/cytology/physiology ; Peripheral Nerves/transplantation ; Rats ; Retinal Ganglion Cells/*physiology ; Signal Transduction ; Spinal Cord/cytology/physiology
    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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    Biodegradable, elastic shape-memory polymers for potential biomedical applications (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-27
    Description: The introduction of biodegradable implant materials as well as minimally invasive surgical procedures in medicine has substantially improved health care within the past few decades. This report describes a group of degradable thermoplastic polymers that are able to change their shape after an increase in temperature. Their shape-memory capability enables bulky implants to be placed in the body through small incisions or to perform complex mechanical deformations automatically. A smart degradable suture was created to illustrate the potential of these shape-memory thermoplastics in biomedical applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lendlein, Andreas -- Langer, Robert -- New York, N.Y. -- Science. 2002 May 31;296(5573):1673-6. Epub 2002 Apr 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉mnemoScience GmbH, Pauwelsstrabetae 19, D-52074 Aachen, Germany. a.lendlein@mnemoscience.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11976407" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biocompatible Materials/chemical synthesis/chemistry ; Chemistry, Physical ; Dioxanes/chemistry ; Elasticity ; Elastomers ; Isocyanates/chemistry ; Mechanics ; Physicochemical Phenomena ; Polyesters/chemistry ; *Polymers/chemical synthesis/chemistry ; *Prostheses and Implants ; Rats ; Stress, Mechanical ; *Sutures ; Temperature ; Thermodynamics
    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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    Correlated bursts of activity in the neonatal hippocampus in vivo (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-18
    Description: The behavior of immature cortical networks in vivo remains largely unknown. Using multisite extracellular and patch-clamp recordings, we observed recurrent bursts of synchronized neuronal activity lasting 0.5 to 3 seconds that occurred spontaneously in the hippocampus of freely moving and anesthetized rat pups. The influence of slow rhythms (0.33 and 0.1 hertz) and the contribution of both gamma-aminobutyric acid A-mediated and glutamate receptor-mediated synaptic signals in the generation of hippocampal bursts was reminiscent of giant depolarizing potentials observed in vitro. This earliest pattern, which diversifies during the second postnatal week, could provide correlated activity for immature neurons and may underlie activity-dependent maturation of the hippocampal network.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leinekugel, Xavier -- Khazipov, Rustem -- Cannon, Robert -- Hirase, Hajime -- Ben-Ari, Yehezkel -- Buzsaki, Gyorgy -- FO6 TW02290/TW/FIC NIH HHS/ -- N0T 43994/PHS HHS/ -- NS 34994/NS/NINDS NIH HHS/ -- NS 43157/NS/NINDS NIH HHS/ -- RR09754/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2049-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INMED, Institut National de la Sante et de la Recherche Medicale (INSERM) U29, Avenue de Luminy, Boite Postale 13, 13273 Marseille Cedex 09, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12065842" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Evoked Potentials ; Hippocampus/*physiology ; Neurons/*physiology ; Patch-Clamp Techniques ; Pyramidal Cells/physiology ; Rats ; Rats, Wistar ; Receptors, GABA-A/physiology ; Receptors, Glutamate/physiology ; Synapses/physiology ; Synaptic Transmission ; gamma-Aminobutyric Acid/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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  • 11
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    Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-28
    Description: Unc104/KIF1A belongs to a class of monomeric kinesin motors that have been thought to possess an unusual motility mechanism. Unlike the unidirectional motion driven by the coordinated actions of the two heads in conventional kinesins, single-headed KIF1A was reported to undergo biased diffusional motion along microtubules. Here, we show that Unc104/KIF1A can dimerize and move unidirectionally and processively with rapid velocities characteristic of transport in living cells. These results suggest that Unc104/KIF1A operates in vivo by a mechanism similar to conventional kinesin and that regulation of motor dimerization may be used to control transport by this class of kinesins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomishige, Michio -- Klopfenstein, Dieter R -- Vale, Ronald D -- AR42895/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2263-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Howard Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351789" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/chemistry/physiology ; Diffusion ; Dimerization ; Humans ; Kinesin/*chemistry/physiology ; Liposomes ; Microtubules/*physiology ; Molecular Motor Proteins/*chemistry/*physiology ; Molecular Sequence Data ; Movement ; Mutation ; Nerve Tissue Proteins/*chemistry/*physiology ; Protein Structure, Tertiary ; Rats ; Recombinant Fusion Proteins/chemistry
    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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  • 12
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    Mediation of hippocampal mossy fiber long-term potentiation by presynaptic Ih channels (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-05
    Description: Hippocampal mossy fiber long-term potentiation (LTP) is expressed presynaptically, but the exact mechanisms remain unknown. Here, we demonstrate the involvement of the hyperpolarization-activated cation channel (Ih) in the expression of mossy fiber LTP. Established LTP was blocked and reversed by Ih channel antagonists. Whole-cell recording from granule cells revealed that repetitive stimulation causes a calcium- and Ih-dependent long-lasting depolarization mediated by protein kinase A. Depolarization at the terminals would be expected to enhance transmitter release, whereas somatic depolarization would enhance the responsiveness of granule cells to afferent input. Thus, Ih channels play an important role in the long-lasting control of transmitter release and neuronal excitability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mellor, Jack -- Nicoll, Roger A -- Schmitz, Dietmar -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):143-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778053" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Animals ; Benzazepines/pharmacology ; Calcium/metabolism ; Cesium/pharmacology ; Chlorides/pharmacology ; Colforsin/pharmacology ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Cyclic Nucleotide-Gated Cation Channels ; Dentate Gyrus/cytology/drug effects/physiology ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels ; In Vitro Techniques ; Ion Channels/antagonists & inhibitors/*physiology ; Isoquinolines/pharmacology ; Long-Term Potentiation/drug effects/*physiology ; Membrane Potentials ; *Membrane Proteins ; Models, Neurological ; Mossy Fibers, Hippocampal/drug effects/*physiology ; *Nerve Tissue Proteins ; Patch-Clamp Techniques ; Potassium/pharmacology ; Potassium Channels ; Presynaptic Terminals/*physiology ; Pyramidal Cells/drug effects/physiology ; Pyrimidines/pharmacology ; Rats ; Rats, Sprague-Dawley ; *Sulfonamides ; Synaptic Transmission
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    Signaling pathways for PC12 cell differentiation: making the right connections (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-01
    Description: A key issue in signal transduction is how signaling pathways common to many systems-so-called canonical signaling cassettes-integrate signals from molecules having a wide spectrum of activities, such as hormones and neurotrophins, to deliver distinct biological outcomes. The neuroendocrine cell line PC12, derived from rat pheochromocytoma, provides an example of how one canonical signaling cassette-the Raf --〉 mitogen-activated protein kinase kinase (MEK) --〉 extracellular signal-regulated kinase (ERK) pathway-can promote distinct outcomes, which in this case include neuritogenesis, gene induction, and proliferation. Two growth hormones, epidermal growth factor (EGF) and nerve growth factor (NGF), use the same pathway to cause PC12 proliferation and differentiation, respectively. In addition, pituitary adenylate cyclase-activating polypeptide (PACAP), a neurotransmitter that also causes differentiation, uses the same canonical cassette as NGF but in a different way. The Connections Map for PC12 Cell Differentiation brings into focus the complex array of specific cellular responses that rely on canonical signal transduction systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vaudry, D -- Stork, P J S -- Lazarovici, P -- Eiden, L E -- New York, N.Y. -- Science. 2002 May 31;296(5573):1648-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Molecular Neuroscience, Laboratory of Cellular and Molecular Regulation, National Institute of Mental Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040181" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Differentiation ; Cell Division ; Cyclic AMP/metabolism ; Epidermal Growth Factor/metabolism/pharmacology ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/metabolism ; Models, Biological ; Nerve Growth Factor/metabolism/pharmacology ; Neurites/physiology ; Neuropeptides/metabolism/pharmacology ; PC12 Cells/*physiology ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Rats ; Receptor, trkA/metabolism ; Receptors, Cell Surface/metabolism ; Response Elements ; Transcription, Genetic
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  • 14
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    Reactivation of ocular dominance plasticity in the adult visual cortex (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: In young animals, monocular deprivation leads to an ocular dominance shift, whereas in adults after the critical period there is no such shift. Chondroitin sulphate proteoglycans (CSPGs) are components of the extracellular matrix (ECM) inhibitory for axonal sprouting. We tested whether the developmental maturation of the ECM is inhibitory for experience-dependent plasticity in the visual cortex. The organization of CSPGs into perineuronal nets coincided with the end of the critical period and was delayed by dark rearing. After CSPG degradation with chondroitinase-ABC in adult rats, monocular deprivation caused an ocular dominance shift toward the nondeprived eye. The mature ECM is thus inhibitory for experience-dependent plasticity, and degradation of CSPGs reactivates cortical plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pizzorusso, Tommaso -- Medini, Paolo -- Berardi, Nicoletta -- Chierzi, Sabrina -- Fawcett, James W -- Maffei, Lamberto -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1248-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scuola Normale Superiore, 56100 Pisa, Italy. tommaso@in.pi.cnr.it〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424383" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/physiology ; Chondroitin ABC Lyase/*metabolism ; Chondroitin Sulfate Proteoglycans/*metabolism ; Darkness ; *Dominance, Ocular ; Extracellular Matrix/*metabolism ; Extracellular Matrix Proteins/metabolism ; Glycosaminoglycans/metabolism ; Lectins, C-Type ; Light ; Nerve Tissue Proteins/metabolism ; *Neuronal Plasticity ; Neurons/physiology ; Rats ; Synapses/physiology ; Time Factors ; Visual Acuity ; Visual Cortex/*physiology
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  • 15
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    Generation of live young from xenografted mouse ovaries (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Snow, Melanie -- Cox, Shae-Lee -- Jenkin, Graham -- Trounson, Alan -- Shaw, Jillian -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2227.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Monash University, Victoria, Australia, 3800.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351780" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Embryo Loss ; Embryo Transfer ; Embryonic and Fetal Development ; Female ; Fertility ; Fertilization in Vitro ; Gonadotropins, Equine/administration & dosage ; Male ; Mice ; Mice, Inbred Strains ; Mice, Nude ; Oocytes/*physiology ; Ovariectomy ; Ovary/*transplantation ; Pregnancy ; Pregnancy Outcome ; Rats ; *Reproductive Techniques, Assisted ; *Transplantation, Heterologous
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  • 16
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    Phototransduction by retinal ganglion cells that set the circadian clock (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: Light synchronizes mammalian circadian rhythms with environmental time by modulating retinal input to the circadian pacemaker-the suprachiasmatic nucleus (SCN) of the hypothalamus. Such photic entrainment requires neither rods nor cones, the only known retinal photoreceptors. Here, we show that retinal ganglion cells innervating the SCN are intrinsically photosensitive. Unlike other ganglion cells, they depolarized in response to light even when all synaptic input from rods and cones was blocked. The sensitivity, spectral tuning, and slow kinetics of this light response matched those of the photic entrainment mechanism, suggesting that these ganglion cells may be the primary photoreceptors for this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berson, David M -- Dunn, Felice A -- Takao, Motoharu -- EY12793/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1070-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Brown University, Providence, RI, 02912 USA. David_Berson@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834835" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/ultrastructure ; *Biological Clocks ; *Circadian Rhythm ; Dendrites/ultrastructure ; Isoquinolines ; Kinetics ; Light ; *Light Signal Transduction ; Patch-Clamp Techniques ; Rats ; Rats, Sprague-Dawley ; Retinal Ganglion Cells/chemistry/cytology/*physiology ; Rod Opsins/analysis/physiology ; Suprachiasmatic Nucleus/cytology/*physiology
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  • 17
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    Immunology. Antibodies kill by producing ozone (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, Jean -- New York, N.Y. -- Science. 2002 Nov 15;298(5597):1319.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434030" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Catalytic/*physiology ; Arthus Reaction ; Catalysis ; Escherichia coli/*physiology ; Humans ; Hydrogen Peroxide/metabolism ; Neutrophils/metabolism ; Oxidants/metabolism ; Oxidation-Reduction ; Ozone/*metabolism ; Rats ; Singlet Oxygen/metabolism
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  • 18
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    Amacrine-signaled loss of intrinsic axon growth ability by retinal ganglion cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-08
    Description: The central nervous system (CNS) loses the ability to regenerate early during development, but it is not known why. The retina has long served as a simple model system for study of CNS regeneration. Here we show that amacrine cells signal neonatal rat retinal ganglion cells (RGCs) to undergo a profound and apparently irreversible loss of intrinsic axon growth ability. Concurrently, retinal maturation triggers RGCs to greatly increase their dendritic growth ability. These results suggest that adult CNS neurons fail to regenerate not only because of CNS glial inhibition but also because of a loss of intrinsic axon growth ability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldberg, Jeffrey L -- Klassen, Matthew P -- Hua, Ying -- Barres, Ben A -- 2T32GM07365/GM/NIGMS NIH HHS/ -- R01 EY11030/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 7;296(5574):1860-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford University School of Medicine, Department of Neurobiology, Sherman Fairchild Science Building D231, 299 Campus Drive, Stanford, CA 94305-5125, USA. jlgoldbe@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12052959" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Amacrine Cells/*physiology ; Animals ; Animals, Newborn ; Axons/*physiology/ultrastructure ; Cell Aging ; *Cell Communication ; Cell Separation ; Cells, Cultured ; Culture Media, Conditioned ; Culture Techniques ; Cyclic AMP/metabolism ; Dendrites/physiology/ultrastructure ; Embryo, Mammalian ; Nerve Regeneration ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Rats ; Retina/cytology ; Retinal Ganglion Cells/*physiology/transplantation/ultrastructure ; Signal Transduction ; Superior Colliculi/physiology
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  • 19
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    Neuronal calcium sensor 1 and activity-dependent facilitation of P/Q-type calcium currents at presynaptic nerve terminals (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-23
    Description: P/Q-type presynaptic calcium currents (IpCa) undergo activity-dependent facilitation during repetitive activation at the calyx of the Held synapse. We investigated whether neuronal calcium sensor 1 (NCS-1) may underlie this phenomenon. Direct loading of NCS-1 into the nerve terminal mimicked activity-dependent IpCa facilitation by accelerating the activation time of IpCa in a Ca2+-dependent manner. A presynaptically loaded carboxyl-terminal peptide of NCS-1 abolished IpCa facilitation. These results suggest that residual Ca2+ activates endogenous NCS-1, thereby facilitating IpCa. Because both P/Q-type Ca2+ channels and NCS-1 are widely expressed in mammalian nerve terminals, NCS-1 may contribute to the activity-dependent synaptic facilitation at many synapses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsujimoto, Tetsuhiro -- Jeromin, Andreas -- Saitoh, Naoto -- Roder, John C -- Takahashi, Tomoyuki -- New York, N.Y. -- Science. 2002 Mar 22;295(5563):2276-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurophysiology, University of Tokyo Faculty of Medicine, Tokyo 113-0033, Japan. tujimoto-tky@umin.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11910115" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Amino Acid Sequence ; Animals ; Brain Stem/cytology/drug effects/metabolism ; Calcium/*metabolism/pharmacology ; Calcium Channels/*metabolism ; Calcium-Binding Proteins/administration & ; dosage/chemistry/*metabolism/pharmacology ; Electric Conductivity ; In Vitro Techniques ; Ion Channel Gating/drug effects ; Molecular Sequence Data ; Neuronal Calcium-Sensor Proteins ; Neuropeptides/administration & dosage/chemistry/*metabolism/pharmacology ; Presynaptic Terminals/drug effects/*metabolism ; Rats ; Rats, Wistar
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  • 20
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    Neurobiology. What the synapse tells the neuron (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mel, Bartlett W -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1845-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Engineering and Neuroscience Graduate Program, University of Southern California, Los Angeles, CA 90089, USA. mel@usc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884739" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/metabolism ; Calcium Signaling ; Dendrites/*physiology ; *Excitatory Postsynaptic Potentials ; Hippocampus/cytology/physiology ; Neocortex/cytology/*physiology ; Patch-Clamp Techniques ; Pyramidal Cells/*physiology ; Rats ; Synapses/*physiology ; Synaptic Transmission
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  • 21
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    Place cells and place recognition maintained by direct entorhinal-hippocampal circuitry (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Place cells in hippocampal area CA1 may receive positional information from the intrahippocampal associative network in area CA3 or directly from the entorhinal cortex. To determine whether direct entorhinal connections support spatial firing and spatial memory, we removed all input from areas CA3 to CA1, thus isolating the CA1 area. Pyramidal cells in the isolated CA1 area developed sharp and stable place fields. Rats with an isolated CA1 area showed normal acquisition of an associative hippocampal-dependent spatial recognition task. Spatial recall was impaired. These results suggest that the hippocampus contains two functionally separable memory circuits: The direct entorhinal-CA1 system is sufficient for recollection-based recognition memory, but recall depends on intact CA3-CA1 connectivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brun, Vegard H -- Otnass, Mona K -- Molden, Sturla -- Steffenach, Hill-Aina -- Witter, Menno P -- Moser, May-Britt -- Moser, Edvard I -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2243-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neuroscience Unit, Medical-Technical Research Centre, Norwegian University of Science and Technology, 7489 Trondheim, Norway.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077421" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Brain Mapping ; Denervation ; Electrodes, Implanted ; Entorhinal Cortex/*physiology ; Hippocampus/*cytology/*physiology ; Interneurons/physiology ; Maze Learning ; Memory/*physiology ; Mental Recall/physiology ; Nerve Net/physiology ; Neural Pathways ; Pyramidal Cells/*physiology ; Rats ; Space Perception/*physiology
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  • 22
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    Alternative splicing and neuritic mRNA translocation under long-term neuronal hypersensitivity (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-01-19
    Description: To explore neuronal mechanisms underlying long-term consequences of stress, we studied stress-induced changes in the neuritic translocation of acetylcholinesterase (AChE) splice variants. Under normal conditions, we found the synaptic AChE-S mRNA and protein in neurites. Corticosterone, anticholinesterases, and forced swim, each facilitated a rapid (minutes), yet long-lasting (weeks), shift from AChE-S to the normally rare AChE-R mRNA, promoted AChE-R mRNA translocation into neurites, and induced enzyme secretion. Weeks after stress, electrophysiological measurements in hippocampus slices displayed apparently normal evoked synaptic responses but extreme hypersensitivity to both anticholinesterases and atropine. Our findings suggest that neuronal hypersensitivity under stress involves neuritic replacement of AChE-S with AChE-R.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meshorer, Eran -- Erb, Christina -- Gazit, Roi -- Pavlovsky, Lev -- Kaufer, Daniela -- Friedman, Alon -- Glick, David -- Ben-Arie, Nissim -- Soreq, Hermona -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):508-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, The Institute of Life Sciences and The Eric Roland Center for Neurodegenerative Diseases, The Hebrew University of Jerusalem, Israel 91904.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799248" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Acetylcholinesterase/*genetics/*metabolism ; Action Potentials ; *Alternative Splicing ; Animals ; Atropine/pharmacology ; Cells, Cultured ; Cerebellum/cytology ; Cholinesterase Inhibitors/pharmacology ; Corticosterone/pharmacology ; Hippocampus/cytology/metabolism/physiology ; In Situ Hybridization, Fluorescence ; In Vitro Techniques ; Mice ; Mice, Transgenic ; Neurites/*metabolism ; Neurons/*metabolism ; Oligonucleotides, Antisense/pharmacology ; PC12 Cells ; Physostigmine/pharmacology ; RNA, Messenger/genetics/*metabolism ; Rats ; Stress, Physiological/genetics/*physiopathology ; Time Factors
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  • 23
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    Microbiology. A binding contract for anthrax (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bull, James J -- Parrish, Colin R -- New York, N.Y. -- Science. 2002 Jul 12;297(5579):201-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Integrative Biology and Institute for Cellular and Molecular Biology, University of Texas, Austin, TX 78712, USA. bull@bull.biosci.utexas.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12114612" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anthrax/prevention & control/therapy ; Anthrax Vaccines/adverse effects/immunology ; Antibodies, Bacterial/genetics/*immunology/metabolism/therapeutic use ; Antibody Affinity ; Antigen-Antibody Complex/blood ; *Antigens, Bacterial ; Antitoxins/genetics/*immunology/metabolism/therapeutic use ; Bacillus anthracis/*immunology ; Bacterial Toxins/*immunology/metabolism/toxicity ; Bioterrorism ; Drug Industry ; Escherichia coli/genetics ; Genetic Engineering ; Humans ; Immunization, Passive ; Macrophages, Alveolar/metabolism ; Peptide Library ; Rats ; Receptors, Peptide/metabolism ; Recombinant Proteins
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  • 24
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    Retrograde support of neuronal survival without retrograde transport of nerve growth factor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Application of nerve growth factor (NGF) covalently cross-linked to beads increased the phosphorylation of TrkA and Akt, but not of mitogen-activated protein kinase, in cultured rat sympathetic neurons. NGF beads or iodine-125-labeled NGF beads supplied to distal axons resulted in the survival of over 80% of the neurons for 30 hours, with little or no retrograde transport of iodine-125-labeled NGF; whereas application of free iodine-125-labeled NGF (0.5 nanograms per milliliter) produced 20-fold more retrograde transport, but only 29% of the neurons survived. Thus, in contrast to widely accepted theory, a neuronal survival signal can reach the cell bodies unaccompanied by the NGF that initiated it.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacInnis, Bronwyn L -- Campenot, Robert B -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1536-9. Epub 2002 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, 6-14 Medical Sciences Building, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799202" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*metabolism ; Cell Survival/drug effects ; Cells, Cultured ; Chromones/pharmacology ; Cross-Linking Reagents ; Enzyme Inhibitors/pharmacology ; Iodine Radioisotopes ; Microspheres ; Mitogen-Activated Protein Kinases/metabolism ; Morpholines/pharmacology ; Nerve Growth Factor/*metabolism/pharmacology ; Neurons/metabolism/*physiology ; Phosphatidylinositol 3-Kinases/antagonists & inhibitors/metabolism ; Phosphorylation ; Protein Transport ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Rats, Sprague-Dawley ; Receptor, trkA/metabolism ; Signal Transduction ; Superior Cervical Ganglion
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  • 25
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    Myeloperoxidase, a leukocyte-derived vascular NO oxidase (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-29
    Description: Myeloperoxidase (MPO) is an abundant mammalian phagocyte hemoprotein thought to primarily mediate host defense reactions. Although its microbicidal functions are well established in vitro, humans deficient in MPO are not at unusual risk of infection. MPO was observed herein to modulate the vascular signaling and vasodilatory functions of nitric oxide (NO) during acute inflammation. After leukocyte degranulation, MPO localized in and around vascular endothelial cells in a rodent model of acute endotoxemia and impaired endothelium-dependent relaxant responses, to which MPO-deficient mice were resistant. Altered vascular responsiveness was due to catalytic consumption of NO by substrate radicals generated by MPO. Thus MPO can directly modulate vascular inflammatory responses by regulating NO bioavailability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eiserich, Jason P -- Baldus, Stephan -- Brennan, Marie-Luise -- Ma, Wenxin -- Zhang, Chunxiang -- Tousson, Albert -- Castro, Laura -- Lusis, Aldons J -- Nauseef, William M -- White, C Roger -- Freeman, Bruce A -- I01 BX000513/BX/BLRD VA/ -- R01 HL067930/HL/NHLBI NIH HHS/ -- R03 TW005682/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 28;296(5577):2391-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Division of Nephrology, University of California, Davis, CA 95616, USA. jpeiserich@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12089442" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta ; Catalysis ; Cattle ; Cells, Cultured ; Chromans/metabolism/pharmacology ; Coculture Techniques ; Cyclic GMP/metabolism ; Endothelium, Vascular/enzymology/*physiology ; Endotoxemia/enzymology ; Humans ; Hydrogen Peroxide/metabolism/pharmacology ; Inflammation/*enzymology/physiopathology ; Leukocytes/*enzymology ; Mice ; Mice, Inbred C57BL ; Muscle, Smooth, Vascular/metabolism ; Mutation ; Nitric Oxide/*metabolism ; Oxidation-Reduction ; Peroxidase/genetics/*metabolism ; Rats ; Rats, Sprague-Dawley ; Signal Transduction ; Transfection ; Tumor Cells, Cultured ; *Vasodilation
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  • 26
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    SynCAM, a synaptic adhesion molecule that drives synapse assembly (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: Synapses, the junctions between nerve cells through which they communicate, are formed by the coordinated assembly and tight attachment of pre- and postsynaptic specializations. We now show that SynCAM is a brain-specific, immunoglobulin domain-containing protein that binds to intracellular PDZ-domain proteins and functions as a homophilic cell adhesion molecule at the synapse. Expression of the isolated cytoplasmic tail of SynCAM in neurons inhibited synapse assembly. Conversely, expression of full-length SynCAM in nonneuronal cells induced synapse formation by cocultured hippocampal neurons with normal release properties. Glutamatergic synaptic transmission was reconstituted in these nonneuronal cells by coexpressing glutamate receptors with SynCAM, which suggests that a single type of adhesion molecule and glutamate receptor are sufficient for a functional postsynaptic response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biederer, Thomas -- Sara, Yildirim -- Mozhayeva, Marina -- Atasoy, Deniz -- Liu, Xinran -- Kavalali, Ege T -- Sudhof, Thomas C -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1525-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Basic Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Thomas.Biederer@UTSouthwestern.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202822" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/cytology/*physiology ; Brain Chemistry ; Cell Adhesion Molecules/chemistry/isolation & purification/*physiology ; Cell Adhesion Molecules, Neuronal/chemistry/isolation & purification/*physiology ; Cell Line ; Coculture Techniques ; Exocytosis ; Humans ; Immunoglobulins ; Molecular Sequence Data ; Neurons/physiology ; Prosencephalon/chemistry/physiology ; Protein Structure, Tertiary ; Rats ; Receptors, AMPA/physiology ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid ; Synapses/chemistry/*physiology ; Synaptic Transmission/physiology ; Transfection ; Tumor Suppressor Proteins
    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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    S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: Matrix metalloproteinases (MMPs) are implicated in the pathogenesis of neurodegenerative diseases and stroke. However, the mechanism of MMP activation remains unclear. We report that MMP activation involves S-nitrosylation. During cerebral ischemia in vivo, MMP-9 colocalized with neuronal nitric oxide synthase. S-Nitrosylation activated MMP-9 in vitro and induced neuronal apoptosis. Mass spectrometry identified the active derivative of MMP-9, both in vitro and in vivo, as a stable sulfinic or sulfonic acid, whose formation was triggered by S-nitrosylation. These findings suggest a potential extracellular proteolysis pathway to neuronal cell death in which S-nitrosylation activates MMPs, and further oxidation results in a stable posttranslational modification with pathological activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, Zezong -- Kaul, Marcus -- Yan, Boxu -- Kridel, Steven J -- Cui, Jiankun -- Strongin, Alex -- Smith, Jeffrey W -- Liddington, Robert C -- Lipton, Stuart A -- AR08505/AR/NIAMS NIH HHS/ -- P01 HD29587/HD/NICHD NIH HHS/ -- R01 AR42750/AR/NIAMS NIH HHS/ -- R01 CA 69306/CA/NCI NIH HHS/ -- R01 EY05477/EY/NEI NIH HHS/ -- R01 EY09024/EY/NEI NIH HHS/ -- R01 NS41207/NS/NINDS NIH HHS/ -- T32 AG00252/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 16;297(5584):1186-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neuroscience and Aging, Program in Cell Adhesion and Extracellular Matrix Biology, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183632" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Brain Ischemia/*enzymology/pathology ; Cell Line ; Cells, Cultured ; Cerebral Cortex/blood supply/*enzymology/pathology ; Cysteine/*analogs & derivatives/metabolism/pharmacology ; Enzyme Activation ; Enzyme Precursors/genetics/metabolism ; Humans ; Matrix Metalloproteinase 9/chemistry/*metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Models, Molecular ; Neurons/*physiology ; Nitric Oxide/metabolism ; Nitric Oxide Synthase/antagonists & inhibitors/metabolism ; Nitric Oxide Synthase Type I ; Oxidation-Reduction ; Phenylmercuric Acetate/*analogs & derivatives/pharmacology ; Rats ; Recombinant Proteins/metabolism ; Reperfusion ; S-Nitrosothiols/*metabolism/pharmacology ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 28
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    Treatment of ischemic brain damage by perturbing NMDA receptor- PSD-95 protein interactions (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: N-methyl-D-aspartate receptors (NMDARs) mediate ischemic brain damage but also mediate essential neuronal excitation. To treat stroke without blocking NMDARs, we transduced neurons with peptides that disrupted the interaction of NMDARs with the postsynaptic density protein PSD-95. This procedure dissociated NMDARs from downstream neurotoxic signaling without blocking synaptic activity or calcium influx. The peptides, when applied either before or 1 hour after an insult, protected cultured neurons from excitotoxicity, reduced focal ischemic brain damage in rats, and improved their neurological function. This approach circumvents the negative consequences associated with blocking NMDARs and may constitute a practical stroke therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aarts, Michelle -- Liu, Yitao -- Liu, Lidong -- Besshoh, Shintaro -- Arundine, Mark -- Gurd, James W -- Wang, Yu-Tian -- Salter, Michael W -- Tymianski, Michael -- NS 39060/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):846-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Toronto Western Hospital Research Institute, 11-416 MC-PAV, 399 Bathurst Street, Toronto, Ontario M5T 2S8, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399596" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Brain/*drug effects/metabolism ; Brain Ischemia/*drug therapy/metabolism ; Calcium/metabolism ; Cells, Cultured ; Cerebral Infarction/*drug therapy/metabolism ; Cyclic GMP/metabolism ; Guanylate Kinase ; In Vitro Techniques ; Intracellular Signaling Peptides and Proteins ; Male ; Membrane Proteins ; Mice ; Mice, Inbred C57BL ; N-Methylaspartate/pharmacology ; Nerve Tissue Proteins/chemistry/*metabolism ; Neurons/drug effects/physiology ; Patch-Clamp Techniques ; Peptides/administration & dosage/*pharmacology/therapeutic use ; Protein Binding ; Rats ; Rats, Sprague-Dawley ; Rats, Wistar ; Receptors, N-Methyl-D-Aspartate/*chemistry/*metabolism ; Recombinant Fusion Proteins/administration & dosage/pharmacology/therapeutic use ; Signal Transduction ; Synaptic Transmission/drug effects
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    Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-03
    Description: Cellular communication in the nervous system is mediated by chemical messengers that include amino acids, monoamines, peptide hormones, and lipids. An interesting question is how neurons regulate signals that are transmitted by membrane-embedded lipids. Here, we report the 2.8 angstrom crystal structure of the integral membrane protein fatty acid amide hydrolase (FAAH), an enzyme that degrades members of the endocannabinoid class of signaling lipids and terminates their activity. The structure of FAAH complexed with an arachidonyl inhibitor reveals how a set of discrete structural alterations allows this enzyme, in contrast to soluble hydrolases of the same family, to integrate into cell membranes and establish direct access to the bilayer from its active site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bracey, Michael H -- Hanson, Michael A -- Masuda, Kim R -- Stevens, Raymond C -- Cravatt, Benjamin F -- R01 DA013173/DA/NIDA NIH HHS/ -- R01 DA013173-02/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1793-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459591" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/antagonists & inhibitors/*chemistry/metabolism ; Animals ; Arachidonic Acids/metabolism ; *Bacterial Proteins ; Binding Sites ; Cannabinoid Receptor Modulators ; Catalysis ; Catalytic Domain ; Cell Membrane/*enzymology ; Crystallography, X-Ray ; Dimerization ; Endocannabinoids ; Helix-Turn-Helix Motifs ; Lipid Bilayers ; Models, Molecular ; Organophosphonates/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Rats ; Recombinant Proteins/chemistry/metabolism ; Signal Transduction ; Solubility
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    DNA repair pathway stimulated by the forkhead transcription factor FOXO3a through the Gadd45 protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: The signaling pathway from phosphoinositide 3-kinase to the protein kinase Akt controls organismal life-span in invertebrates and cell survival and proliferation in mammals by inhibiting the activity of members of the FOXO family of transcription factors. We show that mammalian FOXO3a also functions at the G2 to M checkpoint in the cell cycle and triggers the repair of damaged DNA. By gene array analysis, FOXO3a was found to modulate the expression of several genes that regulate the cellular response to stress at the G2-M checkpoint. The growth arrest and DNA damage response gene Gadd45a appeared to be a direct target of FOXO3a that mediates part of FOXO3a's effects on DNA repair. These findings indicate that in mammals FOXO3a regulates the resistance of cells to stress by inducing DNA repair and thereby may also affect organismal life-span.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tran, Hien -- Brunet, Anne -- Grenier, Jill M -- Datta, Sandeep R -- Fornace, Albert J Jr -- DiStefano, Peter S -- Chiang, Lillian W -- Greenberg, Michael E -- NIHP30-HD18655/HD/NICHD NIH HHS/ -- P01-HD24926/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):530-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital and Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964479" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chromones/pharmacology ; DNA Damage ; *DNA Repair ; DNA-Binding Proteins/genetics/*metabolism ; Forkhead Transcription Factors ; G2 Phase ; Gene Expression Profiling ; Gene Expression Regulation ; Genes, Reporter ; Humans ; Intracellular Signaling Peptides and Proteins ; Mitosis ; Morpholines/pharmacology ; Promoter Regions, Genetic ; Proteins/genetics/*metabolism ; Rats ; Recombinant Fusion Proteins/metabolism ; Tamoxifen/*analogs & derivatives/pharmacology ; Transcription Factors/genetics/*metabolism ; Transfection ; Ultraviolet Rays
    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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    Neuroscience. How neurons know that it's c-c-c-c-cold outside (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seydel, Caroline -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1451-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859171" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cold Temperature ; Face/innervation ; Menthol/*metabolism/pharmacology ; Mice ; Neurons, Afferent/*physiology ; Potassium/metabolism ; Potassium Channels/*physiology ; Rats ; Receptors, Drug/*physiology ; Sensation/*physiology ; Thermoreceptors/*physiology
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    Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-04
    Description: Huntington's disease (HD) is an inherited neurodegenerative disease caused by expansion of a polyglutamine tract in the huntingtin protein. Transcriptional dysregulation has been implicated in HD pathogenesis. Here, we report that huntingtin interacts with the transcriptional activator Sp1 and coactivator TAFII130. Coexpression of Sp1 and TAFII130 in cultured striatal cells from wild-type and HD transgenic mice reverses the transcriptional inhibition of the dopamine D2 receptor gene caused by mutant huntingtin, as well as protects neurons from huntingtin-induced cellular toxicity. Furthermore, soluble mutant huntingtin inhibits Sp1 binding to DNA in postmortem brain tissues of both presymptomatic and affected HD patients. Understanding these early molecular events in HD may provide an opportunity to interfere with the effects of mutant huntingtin before the development of disease symptoms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dunah, Anthone W -- Jeong, Hyunkyung -- Griffin, April -- Kim, Yong-Man -- Standaert, David G -- Hersch, Steven M -- Mouradian, M Maral -- Young, Anne B -- Tanese, Naoko -- Krainc, Dimitri -- 5R37AG13617/AG/NIA NIH HHS/ -- AT00613/AT/NCCIH NIH HHS/ -- NS02174/NS/NINDS NIH HHS/ -- NS34361/NS/NINDS NIH HHS/ -- NS35255/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2238-43. Epub 2002 May 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Center for Aging, Genetics and Neurodegeneration, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Caudate Nucleus/metabolism ; Cell Death ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; Corpus Striatum/cytology/embryology/metabolism ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Down-Regulation ; Gene Expression Regulation ; Humans ; Huntington Disease/*genetics/metabolism ; Mice ; Mice, Transgenic ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neurons/physiology ; Nuclear Proteins/chemistry/genetics/*metabolism ; Peptides ; Promoter Regions, Genetic ; Rats ; Receptors, Dopamine D2/genetics ; Solubility ; Sp1 Transcription Factor/chemistry/*metabolism ; *TATA-Binding Protein Associated Factors ; *Transcription Factor TFIID ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic ; Transfection ; Trinucleotide Repeat Expansion ; Two-Hybrid System Techniques
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    Structural basis for gluten intolerance in celiac sprue (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-28
    Description: Celiac Sprue, a widely prevalent autoimmune disease of the small intestine, is induced in genetically susceptible individuals by exposure to dietary gluten. A 33-mer peptide was identified that has several characteristics suggesting it is the primary initiator of the inflammatory response to gluten in Celiac Sprue patients. In vitro and in vivo studies in rats and humans demonstrated that it is stable toward breakdown by all gastric, pancreatic, and intestinal brush-border membrane proteases. The peptide reacted with tissue transglutaminase, the major autoantigen in Celiac Sprue, with substantially greater selectivity than known natural substrates of this extracellular enzyme. It was a potent inducer of gut-derived human T cell lines from 14 of 14 Celiac Sprue patients. Homologs of this peptide were found in all food grains that are toxic to Celiac Sprue patients but are absent from all nontoxic food grains. The peptide could be detoxified in in vitro and in vivo assays by exposure to a bacterial prolyl endopeptidase, suggesting a strategy for oral peptidase supplement therapy for Celiac Sprue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shan, Lu -- Molberg, Oyvind -- Parrot, Isabelle -- Hausch, Felix -- Filiz, Ferda -- Gray, Gary M -- Sollid, Ludvig M -- Khosla, Chaitan -- R01 DK100619/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 27;297(5590):2275-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351792" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Celiac Disease/*immunology/therapy ; Cell Line ; Edible Grain/chemistry ; Endopeptidases/metabolism ; Epitopes, T-Lymphocyte ; GTP-Binding Proteins/metabolism ; Gliadin/*chemistry/*immunology/metabolism ; HLA-DQ Antigens/immunology ; Humans ; Immunodominant Epitopes ; Intestinal Mucosa/enzymology/*immunology ; Intestine, Small/enzymology/*immunology ; Lymphocyte Activation ; Microvilli/enzymology ; Molecular Sequence Data ; Peptide Fragments/chemistry/immunology ; Rats ; Recombinant Proteins/chemistry/metabolism ; Sequence Homology, Amino Acid ; Serine Endopeptidases/administration & dosage/metabolism/therapeutic use ; T-Lymphocytes/*immunology ; Transglutaminases/metabolism
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    Melanopsin-containing retinal ganglion cells: architecture, projections, and intrinsic photosensitivity (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: The primary circadian pacemaker, in the suprachiasmatic nucleus (SCN) of the mammalian brain, is photoentrained by light signals from the eyes through the retinohypothalamic tract. Retinal rod and cone cells are not required for photoentrainment. Recent evidence suggests that the entraining photoreceptors are retinal ganglion cells (RGCs) that project to the SCN. The visual pigment for this photoreceptor may be melanopsin, an opsin-like protein whose coding messenger RNA is found in a subset of mammalian RGCs. By cloning rat melanopsin and generating specific antibodies, we show that melanopsin is present in cell bodies, dendrites, and proximal axonal segments of a subset of rat RGCs. In mice heterozygous for tau-lacZ targeted to the melanopsin gene locus, beta-galactosidase-positive RGC axons projected to the SCN and other brain nuclei involved in circadian photoentrainment or the pupillary light reflex. Rat RGCs that exhibited intrinsic photosensitivity invariably expressed melanopsin. Hence, melanopsin is most likely the visual pigment of phototransducing RGCs that set the circadian clock and initiate other non-image-forming visual functions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885915/" 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/PMC2885915/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hattar, S -- Liao, H W -- Takao, M -- Berson, D M -- Yau, K W -- R37 EY006837/EY/NEI NIH HHS/ -- R37 EY006837-13/EY/NEI NIH HHS/ -- R37 EY006837-14/EY/NEI NIH HHS/ -- R37 EY006837-15/EY/NEI NIH HHS/ -- R37 EY006837-15S1/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1065-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834834" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/chemistry ; *Biological Clocks ; Brain/*cytology ; Cell Membrane/chemistry ; *Circadian Rhythm ; Cloning, Molecular ; Dendrites/chemistry ; Fluorescent Antibody Technique ; Lac Operon ; *Light ; Mice ; Microscopy, Confocal ; Molecular Sequence Data ; Optic Nerve/cytology ; Rats ; Retinal Ganglion Cells/*chemistry/physiology ; Rod Opsins/*analysis/chemistry/genetics/*physiology ; Suprachiasmatic Nucleus/cytology ; Visual Pathways/cytology ; beta-Galactosidase/analysis
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    Neurobiology. TRK makes the retrograde (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Freda D -- Kaplan, David R -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1471-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Neuronal Survival and Brain Tumor Research Centre, Montreal Neurological Institute, McGill University, 3801 rue University, Montreal, Quebec H3A 2B4, Canada. freda.miller@mcgill.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859179" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*metabolism ; Cell Survival ; Enzyme Activation ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/metabolism ; Models, Neurological ; Nerve Growth Factor/*metabolism ; Neurons/metabolism/*physiology ; Phosphatidylinositol 3-Kinases/metabolism ; Protein Transport ; Rats ; Receptor, trkA/*metabolism ; *Signal Transduction ; Transport Vesicles/metabolism
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    Neuroscience. Researchers thrilled with seminal discovery (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1460-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202793" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ejaculation/*physiology ; Humans ; Lumbosacral Region ; Male ; Neurons/*physiology ; Rats ; Spinal Cord/cytology/*physiology
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    Vitamin D receptor as an intestinal bile acid sensor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-05-23
    Description: The vitamin D receptor (VDR) mediates the effects of the calcemic hormone 1alpha,25-dihydroxyvitamin D3 [1,25(OH)2D3]. We show that VDR also functions as a receptor for the secondary bile acid lithocholic acid (LCA), which is hepatotoxic and a potential enteric carcinogen. VDR is an order of magnitude more sensitive to LCA and its metabolites than are other nuclear receptors. Activation of VDR by LCA or vitamin D induced expression in vivo of CYP3A, a cytochrome P450 enzyme that detoxifies LCA in the liver and intestine. These studies offer a mechanism that may explain the proposed protective effects of vitamin D and its receptor against colon cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Makishima, Makoto -- Lu, Timothy T -- Xie, Wen -- Whitfield, G Kerr -- Domoto, Hideharu -- Evans, Ronald M -- Haussler, Mark R -- Mangelsdorf, David J -- New York, N.Y. -- Science. 2002 May 17;296(5571):1313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9050, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016314" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Aryl Hydrocarbon Hydroxylases ; Binding, Competitive ; COS Cells ; Cell Line ; Colonic Neoplasms/prevention & control ; Cytochrome P-450 CYP3A ; Cytochrome P-450 Enzyme System/genetics/metabolism ; DNA-Binding Proteins/metabolism ; Dimerization ; Gene Expression Regulation, Enzymologic ; Histone Acetyltransferases ; Humans ; Intestine, Small/*metabolism ; Ligands ; Lithocholic Acid/analogs & derivatives/*metabolism/pharmacology ; Male ; Mice ; Nuclear Receptor Coactivator 1 ; Oxidoreductases, N-Demethylating/genetics/metabolism ; Promoter Regions, Genetic ; Rats ; Receptors, Calcitriol/agonists/genetics/*metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Receptors, Steroid/metabolism ; Transcription Factors/metabolism ; Transfection
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    Germline transmission and tissue-specific expression of transgenes delivered by lentiviral vectors (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-12
    Description: Single-cell mouse embryos were infected in vitro with recombinant lentiviral vectors to generate transgenic mice carrying the green fluorescent protein (GFP) gene driven by a ubiquitously expressing promoter. Eighty percent of founder mice carried at least one copy of the transgene, and 90% of these expressed GFP at high levels. Progeny inherited the transgene(s) and displayed green fluorescence. Mice generated using lentiviral vectors with muscle-specific and T lymphocyte-specific promoters expressed high levels of GFP only in the appropriate cell types. We have also generated transgenic rats that express GFP at high levels, suggesting that this technique can be used to produce other transgenic animal species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lois, Carlos -- Hong, Elizabeth J -- Pease, Shirley -- Brown, Eric J -- Baltimore, David -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):868-72. Epub 2002 Jan 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786607" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Genetically Modified ; Blotting, Southern ; Blotting, Western ; Cell Lineage ; Crosses, Genetic ; DNA, Recombinant ; Embryo Transfer ; Embryo, Mammalian/*metabolism/virology ; Female ; Gene Dosage ; *Gene Expression ; Gene Silencing ; Genes, Reporter ; *Genetic Vectors ; Green Fluorescent Proteins ; HIV-1/genetics ; Hepatitis B Virus, Woodchuck/genetics ; Lentivirus/*genetics ; Luminescent Proteins/biosynthesis/genetics ; Male ; Mice ; Mice, Transgenic ; Muscle, Skeletal/embryology/metabolism ; Organ Specificity ; Promoter Regions, Genetic ; Proviruses/genetics ; Rats ; *Transgenes ; Virus Integration
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    Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Protein-protein interactions and calcium entry through the N-methyl-d-aspartate (NMDA)-type glutamate receptor regulate synaptic development and plasticity in the central nervous system. The EphB receptor tyrosine kinases are localized at excitatory synapses where they cluster and associate with NMDA receptors. We identified a mechanism whereby EphBs modulate NMDA receptor function. EphrinB2 activation of EphB in primary cortical neurons potentiates NMDA receptor-dependent influx of calcium. Treatment of cells with ephrinB2 led to NMDA receptor tyrosine phosphorylation through activation of the Src family of tyrosine kinases. These ephrinB2-dependent events result in enhanced NMDA receptor-dependent gene expression. Our findings indicate that ephrinB2 stimulation of EphB modulates the functional consequences of NMDA receptor activation and suggest a mechanism whereby activity-independent and activity-dependent signals converge to regulate the development and remodeling of synaptic connections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takasu, Mari A -- Dalva, Matthew B -- Zigmond, Richard E -- Greenberg, Michael E -- CA43855/CA/NCI NIH HHS/ -- HD18655/HD/NICHD NIH HHS/ -- NS12651/NS/NINDS NIH HHS/ -- NS17512/NS/NINDS NIH HHS/ -- R01 NS045500/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):491-5. Epub 2001 Dec 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, and the Department of Neurobiology, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799243" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor/pharmacology ; Calcium/*metabolism ; Cell Line ; Cells, Cultured ; Cerebral Cortex/cytology/embryology ; Cyclic AMP Response Element-Binding Protein/metabolism ; Ephrin-B2 ; *Gene Expression Regulation ; Genes, Reporter ; Glutamic Acid/metabolism ; Humans ; Immunoglobulin Fc Fragments ; Membrane Proteins/*metabolism/pharmacology ; Models, Neurological ; Mutation ; Neurons/*metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-fyn ; Rats ; Receptor Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptor, EphB4 ; Receptors, Eph Family ; Receptors, N-Methyl-D-Aspartate/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism/pharmacology ; Signal Transduction ; Synapses/metabolism ; Transcription, Genetic ; src-Family Kinases/metabolism
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    Identification of a potential ejaculation generator in the spinal cord (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: We tested the significance of a population of lumbar spinothalamic cells for male sexual behavior in rats. These cells are positioned to relay ejaculation-related signals from reproductive organs to the brain, and they express neurokinin-1 receptors. Ablation of these neurons by the selective toxin SSP-saporin resulted in a complete disruption of ejaculatory behavior. In contrast, other components of sexual behavior remained intact. These results suggest that this population of spinothalamic cells plays a pivotal role in generation of ejaculatory behavior and may be part of a spinal ejaculation generator.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Truitt, William A -- Coolen, Lique M -- MH60781/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1566-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Neurobiology, and Anatomy, Neuroscience Graduate Program, University of Cincinnati, College of Medicine, Post Office Box 670521, Cincinnati, OH 45267-0521, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202834" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ejaculation/*physiology ; Female ; Immunoenzyme Techniques ; Lumbosacral Region ; Male ; Neural Conduction ; Neurons/drug effects/metabolism/*physiology ; Rats ; Rats, Sprague-Dawley ; Receptors, Neurokinin-1/biosynthesis ; Recombinant Fusion Proteins/pharmacology ; Ribosome Inactivating Proteins, Type 1 ; Sexual Behavior, Animal/physiology ; Spinal Cord/anatomy & histology/cytology/*physiology ; Thalamus/cytology/*physiology
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    Targeting of cyclic AMP degradation to beta 2-adrenergic receptors by beta-arrestins (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: Catecholamines signal through the beta2-adrenergic receptor by promoting production of the second messenger adenosine 3',5'-monophosphate (cAMP). The magnitude of this signal is restricted by desensitization of the receptors through their binding to beta-arrestins and by cAMP degradation by phosphodiesterase (PDE) enzymes. We show that beta-arrestins coordinate both processes by recruiting PDEs to activated beta2-adrenergic receptors in the plasma membrane of mammalian cells. In doing so, the beta-arrestins limit activation of membrane-associated cAMP-activated protein kinase by simultaneously slowing the rate of cAMP production through receptor desensitization and increasing the rate of its degradation at the membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perry, Stephen J -- Baillie, George S -- Kohout, Trudy A -- McPhee, Ian -- Magiera, Maria M -- Ang, Kok Long -- Miller, William E -- McLean, Alison J -- Conti, Marco -- Houslay, Miles D -- Lefkowitz, Robert J -- HD20788/HD/NICHD NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):834-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399592" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/genetics/metabolism ; Adrenergic beta-Agonists/pharmacology ; Animals ; Arrestins/genetics/*metabolism ; COS Cells ; Cell Line ; Cell Membrane/metabolism ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 4 ; Cytosol/metabolism ; Humans ; Isoenzymes/metabolism ; Isoproterenol/pharmacology ; Mice ; Mutation ; Precipitin Tests ; Rats ; Receptors, Adrenergic, beta-2/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection
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    Signaling of rat Frizzled-2 through phosphodiesterase and cyclic GMP (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: The Frizzled-2 receptor (Rfz2) from rat binds Wnt proteins and can signal by activating calcium release from intracellular stores. We show that wild-type Rfz2 and a chimeric receptor consisting of the extracellular and transmembrane portions of the beta2-adrenergic receptor with cytoplasmic domains of Rfz2 also signaled through modulation of cyclic guanosine 3',5'-monophosphate (cGMP). Activation of either receptor led to a decline in the intracellular concentration of cGMP, a process that was inhibited in cells treated with pertussis toxin, reduced by suppression of the expression of the heterotrimeric GTP-binding protein (G protein) transducin, and suppressed through inhibition of cGMP-specific phosphodiesterase (PDE) activity. Moreover, PDE inhibitors blocked Rfz2-induced calcium transients in zebrafish embryos. Thus, Frizzled-2 appears to couple to PDEs and calcium transients through G proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ahumada, Adriana -- Slusarski, Diane C -- Liu, Xunxian -- Moon, Randall T -- Malbon, Craig C -- Wang, Hsien-yu -- T32-DK07521/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):2006-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Diabetes and Metabolic Diseases Research Center, University Medical Center, SUNY-Stony Brook, Stony Brook, NY 11794-8651, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471263" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Calcium/metabolism ; Cricetinae ; Culture Media, Conditioned ; Cyclic GMP/*metabolism ; Embryo, Nonmammalian/metabolism ; Frizzled Receptors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Molecular Sequence Data ; Pertussis Toxin/pharmacology ; Phosphodiesterase Inhibitors/pharmacology ; Phosphoric Diester Hydrolases/*metabolism ; Rats ; Receptors, Adrenergic, beta-2/chemistry/metabolism ; Receptors, G-Protein-Coupled ; Receptors, Neurotransmitter/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; *Signal Transduction ; Transducin/genetics/metabolism ; Transfection ; Tumor Cells, Cultured ; Zebrafish
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    Oscillatory expression of the bHLH factor Hes1 regulated by a negative feedback loop (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: Transcription of messenger RNAs (mRNAs) for Notch signaling molecules oscillates with 2-hour cycles, and this oscillation is important for coordinated somite segmentation. However, the molecular mechanism of such oscillation remains to be determined. Here, we show that serum treatment of cultured cells induces cyclic expression of both mRNA and protein of the Notch effector Hes1, a basic helix-loop-helix (bHLH) factor, with 2-hour periodicity. Cycling is cell-autonomous and depends on negative autoregulation of hes1 transcription and ubiquitin-proteasome-mediated degradation of Hes1 protein. Because Hes1 oscillation can be seen in many cell types, this clock may regulate timing in many biological systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirata, Hiromi -- Yoshiura, Shigeki -- Ohtsuka, Toshiyuki -- Bessho, Yasumasa -- Harada, Takahiro -- Yoshikawa, Kenichi -- Kageyama, Ryoichiro -- New York, N.Y. -- Science. 2002 Oct 25;298(5594):840-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399594" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/*analogs & derivatives/pharmacology ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Biological Clocks ; Blood ; Cell Line ; Cycloheximide/pharmacology ; Cysteine Endopeptidases/metabolism ; Feedback, Physiological ; Gene Expression Regulation ; Glycosyltransferases/genetics/metabolism ; Half-Life ; Homeodomain Proteins/biosynthesis/*genetics/*metabolism ; Leupeptins/pharmacology ; Mesoderm/metabolism ; Mice ; Multienzyme Complexes/metabolism ; PC12 Cells ; *Periodicity ; Protease Inhibitors/pharmacology ; Proteasome Endopeptidase Complex ; Protein Biosynthesis ; Protein Synthesis Inhibitors/pharmacology ; RNA, Messenger/biosynthesis/genetics/metabolism ; Rats ; Transcription, Genetic ; Transfection ; Ubiquitin/metabolism
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    Dependence of EPSP efficacy on synapse location in neocortical pyramidal neurons (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Neurons receive thousands of synaptic inputs throughout elaborate dendritic trees. Here we determine the somatic impact of excitatory postsynaptic potentials (EPSPs) generated at known dendritic sites in neocortical pyramidal neurons. As inputs became more distal, somatic EPSP amplitude decreased, whereas use-dependent depression increased. Despite marked attenuation (〉40-fold), when coactivated within a narrow time window (approximately 10 milliseconds), distal EPSPs could directly influence action potential output following dendritic spike generation. These findings reveal that distal EPSPs are ineffective sources of background somatic excitation, but through coincidence detection have a powerful transient signaling role.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, Stephen R -- Stuart, Greg J -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1907-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, John Curtin School of Medical Research, Australian National University, Canberra, ACT 0200, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884759" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Axons/physiology ; Dendrites/*physiology ; *Excitatory Postsynaptic Potentials ; Neocortex/cytology/*physiology ; Patch-Clamp Techniques ; Pyramidal Cells/*physiology ; Rats ; Rats, Wistar ; Synapses/*physiology ; Synaptic Transmission
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    Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-07
    Description: Cells have evolved multiple mechanisms to inhibit viral replication. To identify previously unknown antiviral activities, we screened mammalian complementary DNA (cDNA) libraries for genes that prevent infection by a genetically marked retrovirus. Virus-resistant cells were selected from pools of transduced clones, and an active antiviral cDNA was recovered. The gene encodes a CCCH-type zinc finger protein designated ZAP. Expression of the gene caused a profound and specific loss of viral messenger RNAs (mRNAs) from the cytoplasm without affecting the levels of nuclear mRNAs. The finding suggests the existence of a previously unknown machinery for the inhibition of virus replication, targeting a step in viral gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gao, Guangxia -- Guo, Xuemin -- Goff, Stephen P -- CA 30488/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1703-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, 701 West 168th Street, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215647" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antiviral Agents/chemistry/*genetics/isolation & purification/physiology ; Carrier Proteins/chemistry/*genetics/isolation & purification/physiology ; Cell Line ; Cloning, Molecular ; Gene Library ; Genetic Vectors/genetics ; Open Reading Frames ; Polymerase Chain Reaction ; RNA, Viral/*biosynthesis ; Rats ; Retroviridae/*genetics/immunology ; Tissue Distribution ; Virus Replication ; *Zinc Fingers
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    The neurotrophin receptor p75NTR as a positive modulator of myelination (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-11-09
    Description: Schwann cells in developing and regenerating peripheral nerves express elevated levels of the neurotrophin receptor p75NTR. Neurotrophins are key mediators of peripheral nervous system myelination. Our results show that myelin formation is inhibited in the absence of functional p75NTR and enhanced by blocking TrkC activity. Moreover, the enhancement of myelin formation by endogenous brain-derived neurotrophic factor is mediated by the p75NTR receptor, whereas TrkC receptors are responsible for neurotrophin-3 inhibition. Thus p75NTR and TrkC receptors have opposite effects on myelination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cosgaya, Jose M -- Chan, Jonah R -- Shooter, Eric M -- NS04270/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1245-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University School of Medicine, 299 Campus Drive, Fairchild Building, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424382" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/immunology ; Axons/physiology ; Brain-Derived Neurotrophic Factor/pharmacology/physiology ; Coculture Techniques ; Ganglia, Spinal/cytology ; Immunohistochemistry ; Mice ; Models, Neurological ; Myelin P0 Protein/metabolism ; Myelin Sheath/*physiology ; Myelin-Associated Glycoprotein/metabolism ; Neurotrophin 3/pharmacology/physiology ; Rats ; Rats, Sprague-Dawley ; Receptor, Nerve Growth Factor ; Receptor, trkB/metabolism ; Receptor, trkC/metabolism ; Receptors, Nerve Growth Factor/immunology/*physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Schwann Cells/*physiology ; Sciatic Nerve/cytology/metabolism ; Signal Transduction
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    Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-26
    Description: The DJ-1 gene encodes a ubiquitous, highly conserved protein. Here, we show that DJ-1 mutations are associated with PARK7, a monogenic form of human parkinsonism. The function of the DJ-1 protein remains unknown, but evidence suggests its involvement in the oxidative stress response. Our findings indicate that loss of DJ-1 function leads to neurodegeneration. Elucidating the physiological role of DJ-1 protein may promote understanding of the mechanisms of brain neuronal maintenance and pathogenesis of Parkinson's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonifati, Vincenzo -- Rizzu, Patrizia -- van Baren, Marijke J -- Schaap, Onno -- Breedveld, Guido J -- Krieger, Elmar -- Dekker, Marieke C J -- Squitieri, Ferdinando -- Ibanez, Pablo -- Joosse, Marijke -- van Dongen, Jeroen W -- Vanacore, Nicola -- van Swieten, John C -- Brice, Alexis -- Meco, Giuseppe -- van Duijn, Cornelia M -- Oostra, Ben A -- Heutink, Peter -- New York, N.Y. -- Science. 2003 Jan 10;299(5604):256-9. Epub 2002 Nov 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetic-Epidemiologic Unit, Department of Clinical Genetics, Department of Epidemiology and Biostatistics, Erasmus Medical Center Rotterdam, Post Office Box 1738, 3000 DR Rotterdam, Netherlands. bonifati@kgen.fgg.eur.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446870" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Base Sequence ; Brain/metabolism ; COS Cells ; Cell Nucleus/metabolism ; Chromosomes, Human, Pair 1 ; Cloning, Molecular ; Cytoplasm/metabolism ; DNA, Complementary ; Exons ; Genes, Recessive ; Humans ; Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; *Mutation ; Oncogene Proteins/chemistry/*genetics/metabolism ; Oxidative Stress ; PC12 Cells ; Parkinsonian Disorders/*genetics/metabolism ; Pedigree ; Physical Chromosome Mapping ; Point Mutation ; Protein Structure, Secondary ; Rats ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Deletion ; Transfection
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    Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Genetic determinants of longevity include the forkhead-related transcription factor DAF-16 in the worm Caenorhabditis elegans and the p66shc locus in mice. We demonstrate that p66shc regulates intracellular oxidant levels in mammalian cells and that hydrogen peroxide can negatively regulate forkhead activity. In p66shc-/- cells, the activity of the mammalian forkhead homolog FKHRL1 is increased and redox-dependent forkhead inactivation is reduced. In addition, expression of FKHRL1 results in an increase in both hydrogen peroxide scavenging and oxidative stress resistance. These results demonstrate an important functional relation between three distinct elements linked to aging: forkhead proteins, p66shc, and intracellular oxidants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nemoto, Shino -- Finkel, Toren -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2450-2. Epub 2002 Mar 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Branch, National Heart, Lung and Blood Institute, National Institutes of Health, Building 10/6N-240, 10 Center Drive, Bethesda, MD 20892-1622, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884717" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/pharmacology ; *Adaptor Proteins, Signal Transducing ; *Adaptor Proteins, Vesicular Transport ; Animals ; Azoles/pharmacology ; Blood ; Cells, Cultured ; Culture Media ; DNA-Binding Proteins/genetics/*metabolism ; Forkhead Transcription Factors ; Free Radical Scavengers/pharmacology ; Humans ; Hydrogen Peroxide/metabolism/pharmacology ; Mice ; Mutation ; Organoselenium Compounds/pharmacology ; Oxidation-Reduction ; Oxidative Stress ; PC12 Cells ; Phosphorylation ; *Protein-Serine-Threonine Kinases ; Proteins/genetics/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Reactive Oxygen Species/metabolism ; Shc Signaling Adaptor Proteins ; *Signal Transduction ; Transcription Factors/genetics/*metabolism ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Stem cells. Plasticity: time for a reappraisal? (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holden, Constance -- Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2126-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077383" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Marrow Cells/cytology/physiology ; Brain/cytology ; *Cell Differentiation ; *Cell Fusion ; Cell Separation ; Cells, Cultured ; Coculture Techniques ; Embryo, Mammalian/cytology ; Female ; Hematopoietic Stem Cells/physiology ; Humans ; Hybrid Cells/physiology ; Male ; Mesoderm/cytology ; Mice ; Neurons/physiology ; Rats ; Stem Cells/cytology/*physiology
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    Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-16
    Description: Recently, we showed that antibodies catalyze the generation of hydrogen peroxide (H2O2) from singlet molecular oxygen (1O2*) and water. Here, we show that this process can lead to efficient killing of bacteria, regardless of the antigen specificity of the antibody. H2O2 production by antibodies alone was found to be not sufficient for bacterial killing. Our studies suggested that the antibody-catalyzed water-oxidation pathway produced an additional molecular species with a chemical signature similar to that of ozone. This species is also generated during the oxidative burst of activated human neutrophils and during inflammation. These observations suggest that alternative pathways may exist for biological killing of bacteria that are mediated by potent oxidants previously unknown to biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wentworth, Paul Jr -- McDunn, Jonathan E -- Wentworth, Anita D -- Takeuchi, Cindy -- Nieva, Jorge -- Jones, Teresa -- Bautista, Cristina -- Ruedi, Julie M -- Gutierrez, Abel -- Janda, Kim D -- Babior, Bernard M -- Eschenmoser, Albert -- Lerner, Richard A -- 5T32AI07606/AI/NIAID NIH HHS/ -- GM43858/GM/NIGMS NIH HHS/ -- P01CA27489/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2195-9. Epub 2002 Nov 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12434011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Catalytic/immunology/*metabolism ; Arthus Reaction/*immunology/metabolism ; Blood Bactericidal Activity ; Catalase/metabolism ; Catalysis ; Escherichia coli/*immunology ; Hematoporphyrins/metabolism ; Humans ; Hydrogen Peroxide/metabolism ; Indigo Carmine/metabolism ; Inflammation/*immunology/metabolism ; Mice ; Neutrophil Activation ; Neutrophils/immunology/*metabolism ; Oxidation-Reduction ; Ozone/*metabolism ; Rabbits ; Rats ; Rats, Sprague-Dawley ; Respiratory Burst ; Singlet Oxygen/metabolism ; Ultraviolet Rays ; Water/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Cell proliferation. Common control for cancer, stem cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Normile, Dennis -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1869.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471231" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/*genetics/*physiology ; Cell Differentiation ; *Cell Division ; Cell Line ; GTP-Binding Proteins ; Gene Expression ; Genes ; Humans ; Mice ; Neoplasms/*genetics/pathology ; Nuclear Proteins/*genetics/*physiology ; Rats ; Stem Cells/cytology/*physiology ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Circadian clock. How the brain's clock gets daily enlightenment (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, Marcia -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):955-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834799" target="_blank"〉PubMed〈/a〉
    Keywords: Afferent Pathways ; Animals ; Axons/physiology ; *Biological Clocks ; Brain/cytology ; *Circadian Rhythm ; Dendrites/ultrastructure ; Electrophysiology ; *Light ; Light Signal Transduction ; Mice ; Neuropeptides/analysis ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Rats ; Retinal Ganglion Cells/chemistry/*physiology ; Rod Opsins/*analysis/chemistry/physiology ; Suprachiasmatic Nucleus/cytology
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    Neuroscience. Freeing the bain from the perineuronal net (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, Kevin -- Caterson, Bruce -- New York, N.Y. -- Science. 2002 Nov 8;298(5596):1187-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neuroscience Research Group and the Connective Tissue Biology Labs, Cardiff School of Biosciences, Cardiff University, Cardiff CF10 3US, UK. foxkd@cardiff.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12424361" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/physiology/transplantation ; Chondroitin ABC Lyase/*metabolism ; Chondroitin Sulfate Proteoglycans/*metabolism ; Dendrites/physiology ; Dominance, Ocular ; Extracellular Matrix/*metabolism/physiology ; Extracellular Matrix Proteins/metabolism ; Humans ; Hyaluronic Acid ; Neurites/physiology ; *Neuronal Plasticity ; Rats ; Synapses/physiology ; Vision, Ocular ; Visual Cortex/*physiology
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    Alteration of lymphocyte trafficking by sphingosine-1-phosphate receptor agonists (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-30
    Description: Blood lymphocyte numbers, essential for the development of efficient immune responses, are maintained by recirculation through secondary lymphoid organs. We show that lymphocyte trafficking is altered by the lysophospholipid sphingosine-1-phosphate (S1P) and by a phosphoryl metabolite of the immunosuppressive agent FTY720. Both species were high-affinity agonists of at least four of the five S1P receptors. These agonists produce lymphopenia in blood and thoracic duct lymph by sequestration of lymphocytes in lymph nodes, but not spleen. S1P receptor agonists induced emptying of lymphoid sinuses by retention of lymphocytes on the abluminal side of sinus-lining endothelium and inhibition of egress into lymph. Inhibition of lymphocyte recirculation by activation of S1P receptors may result in therapeutically useful immunosuppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mandala, Suzanne -- Hajdu, Richard -- Bergstrom, James -- Quackenbush, Elizabeth -- Xie, Jenny -- Milligan, James -- Thornton, Rosemary -- Shei, Gan-Ju -- Card, Deborah -- Keohane, CarolAnn -- Rosenbach, Mark -- Hale, Jeffrey -- Lynch, Christopher L -- Rupprecht, Kathleen -- Parsons, William -- Rosen, Hugh -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):346-9. Epub 2002 Mar 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Rheumatology, Merck Research Laboratories, Post Office Box 2000, Rahway, NJ 07065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923495" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/drug effects/*physiology ; Binding, Competitive ; CHO Cells ; Calcium/metabolism ; Cricetinae ; Cyclic AMP/metabolism ; Fingolimod Hydrochloride ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Humans ; Immunosuppressive Agents/metabolism/pharmacology ; Ligands ; Lymph Nodes/cytology/drug effects ; Lymphocyte Count ; Lymphopenia/chemically induced ; *Lysophospholipids ; Mice ; Organophosphates/chemical synthesis/chemistry/metabolism/*pharmacology ; Organophosphonates/chemical synthesis/chemistry/metabolism/*pharmacology ; Phosphorylation ; Propylene Glycols/*metabolism/pharmacology ; Rats ; Receptors, Cell Surface/*agonists/metabolism ; *Receptors, G-Protein-Coupled ; Receptors, Lysophospholipid ; Sphingosine/*analogs & derivatives/metabolism/*pharmacology ; Spleen/cytology/drug effects ; Stereoisomerism ; T-Lymphocytes/drug effects/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Disassembly of transcriptional regulatory complexes by molecular chaperones (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-22
    Description: Many biological processes are initiated by cooperative assembly of large multicomponent complexes; however, mechanisms for modulating or terminating the actions of these complexes are not well understood. For example, hormone-bound intracellular receptors (IRs) nucleate formation of transcriptional regulatory complexes whose actions cease promptly upon hormone withdrawal. Here, we show that the p23 molecular chaperone localizes in vivo to genomic response elements in a hormone-dependent manner, disrupting receptor-mediated transcriptional activation in vivo and in vitro; Hsp90 weakly displayed similar activities. Indeed, p23 and Hsp90 also disrupted the activities of some non-IR-containing transcriptional regulatory complexes. We suggest that molecular chaperones promote disassembly of transcriptional regulatory complexes, thus enabling regulatory machineries to detect and respond to signaling changes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freeman, Brian C -- Yamamoto, Keith R -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2232-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Structural Biology, University of Illinois, Urbana-Champaign, 601 South Goodwin Avenue, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077419" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/metabolism ; Dexamethasone/metabolism/pharmacology ; HSP70 Heat-Shock Proteins/metabolism ; HSP90 Heat-Shock Proteins/*metabolism ; HeLa Cells ; Humans ; Molecular Chaperones/*metabolism ; Nuclear Receptor Coactivator 2 ; Phosphoproteins/*metabolism ; Promoter Regions, Genetic ; Rats ; Receptors, Cytoplasmic and Nuclear/*metabolism ; Receptors, Glucocorticoid/metabolism ; Receptors, Retinoic Acid/metabolism ; Receptors, Thyroid Hormone/metabolism ; Recombinant Fusion Proteins/metabolism ; *Response Elements ; Retinoid X Receptors ; Transcription Factors/metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Tryptophan Oxygenase/genetics ; Tumor Cells, Cultured ; Tyrosine Transaminase/genetics
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    Activation of orphan receptors by the hormone relaxin (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-26
    Description: Relaxin is a hormone important for the growth and remodeling of reproductive and other tissues during pregnancy. Although binding sites for relaxin are widely distributed, the nature of its receptor has been elusive. Here, we demonstrate that two orphan heterotrimeric guanine nucleotide binding protein (G protein)-coupled receptors, LGR7 and LGR8, are capable of mediating the action of relaxin through an adenosine 3',5'-monophosphate (cAMP)-dependent pathway distinct from that of the structurally related insulin and insulin-like growth factor family ligand. Treatment of antepartum mice with the soluble ligand-binding region of LGR7 caused parturition delay. The wide and divergent distribution of the two relaxin receptors implicates their roles in reproductive, brain, renal, cardiovascular, and other functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsu, Sheau Yu -- Nakabayashi, Koji -- Nishi, Shinya -- Kumagai, Jin -- Kudo, Masataka -- Sherwood, O David -- Hsueh, Aaron J W -- DK58534/DK/NIDDK NIH HHS/ -- HD23273/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):671-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Reproductive Biology, Department of Gynecology and Obstetrics, Stanford University School of Medicine, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809971" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Cyclic AMP/metabolism ; DNA, Complementary ; Female ; Gene Expression Profiling ; Genitalia, Female/metabolism ; Humans ; Labor, Obstetric/drug effects ; Ligands ; *Membrane Proteins ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Organ Specificity ; Peptide Fragments/pharmacology ; Pregnancy ; Protein Structure, Tertiary ; Rats ; Receptors, Cell Surface/chemistry/genetics/*physiology ; *Receptors, G-Protein-Coupled ; Receptors, Peptide/chemistry/genetics/*physiology ; Recombinant Fusion Proteins/metabolism ; Relaxin/pharmacology/*physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Signal Transduction ; Transfection
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    Activation of central melanocortin pathways by fenfluramine (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-27
    Description: D-fenfluramine (d-FEN) was once widely prescribed and was among the most effective weight loss drugs, but was withdrawn from clinical use because of reports of cardiac complications in a subset of patients. Discerning the neurobiology underlying the anorexic action of d-FEN may facilitate the development of new drugs to prevent and treat obesity. Through a combination of functional neuroanatomy, feeding, and electrophysiology studies in rodents, we show that d-FEN-induced anorexia requires activation of central nervous system melanocortin pathways. These results provide a mechanistic explanation of d-FEN's anorexic actions and indicate that drugs targeting these downstream melanocortin pathways may prove to be effective and more selective anti-obesity treatments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heisler, Lora K -- Cowley, Michael A -- Tecott, Laurence H -- Fan, Wei -- Low, Malcolm J -- Smart, James L -- Rubinstein, Marcelo -- Tatro, Jeffrey B -- Marcus, Jacob N -- Holstege, Henne -- Lee, Charlotte E -- Cone, Roger D -- Elmquist, Joel K -- F31HG00201/HG/NHGRI NIH HHS/ -- P01DK056116/DK/NIDDK NIH HHS/ -- P01DK55819/DK/NIDDK NIH HHS/ -- R01MH061583/MH/NIMH NIH HHS/ -- R01MH44694/MH/NIMH NIH HHS/ -- R01MH61624/MH/NIMH NIH HHS/ -- R03TW01233/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):609-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Endocrinology, Diabetes and Metabolism, Department of Medicine, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12142539" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Appetite Depressants/*pharmacology ; Arcuate Nucleus of Hypothalamus/*drug effects/metabolism ; Feeding Behavior/*drug effects ; Fenfluramine/*pharmacology ; Male ; Melanocyte-Stimulating Hormones/pharmacology ; Mice ; Mice, Obese ; Mice, Transgenic ; Neurons/drug effects/metabolism ; Paraventricular Hypothalamic Nucleus/drug effects/metabolism ; Patch-Clamp Techniques ; Pro-Opiomelanocortin/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptor, Melanocortin, Type 3 ; Receptor, Melanocortin, Type 4 ; Receptor, Serotonin, 5-HT2C ; Receptors, Corticotropin/metabolism ; Receptors, Serotonin/metabolism ; Serotonin/metabolism ; Serotonin Agents/pharmacology ; alpha-MSH/*metabolism
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    Corepressor-dependent silencing of chromosomal regions encoding neuronal genes (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-26
    Description: The molecular mechanisms by which central nervous system-specific genes are expressed only in the nervous system and repressed in other tissues remain a central issue in developmental and regulatory biology. Here, we report that the zinc-finger gene-specific repressor element RE-1 silencing transcription factor/neuronal restricted silencing factor (REST/NRSF) can mediate extraneuronal restriction by imposing either active repression via histone deacetylase recruitment or long-term gene silencing using a distinct functional complex. Silencing of neuronal-specific genes requires the recruitment of an associated corepressor, CoREST, that serves as a functional molecular beacon for the recruitment of molecular machinery that imposes silencing across a chromosomal interval, including transcriptional units that do not themselves contain REST/NRSF response elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lunyak, Victoria V -- Burgess, Robert -- Prefontaine, Gratien G -- Nelson, Charles -- Sze, Sing-Hoi -- Chenoweth, Josh -- Schwartz, Phillip -- Pevzner, Pavel A -- Glass, Christopher -- Mandel, Gail -- Rosenfeld, Michael G -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1747-52. Epub 2002 Oct 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute (HHMI), Department of Computer Science and Engineering, School of Medicine, University of California, San Diego, 9500 Gilman Drive, Room 345, La Jolla, CA 92093-0648, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12399542" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Carrier Proteins ; Cell Line ; *Chromosomal Proteins, Non-Histone ; Chromosomes/*genetics/metabolism ; Chromosomes, Human/genetics/metabolism ; Co-Repressor Proteins ; Computational Biology ; CpG Islands ; DNA Methylation ; DNA-Binding Proteins/metabolism ; Gene Expression Profiling ; Gene Expression Regulation ; *Gene Silencing ; Histone Deacetylases/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Methyl-CpG-Binding Protein 2 ; Mice ; Models, Genetic ; NAV1.2 Voltage-Gated Sodium Channel ; Nerve Growth Factors/genetics ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neurons/*metabolism ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Rats ; Repressor Proteins/chemistry/*metabolism ; Sodium Channels/genetics ; Transcription Factors/chemistry/*metabolism ; Transfection
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    Stem cell research. Rat brains respond to embryonic stem cells (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Jan 11;295(5553):254-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11786620" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/pathology ; Brain Neoplasms/etiology ; Cell Differentiation ; Cell Transplantation/adverse effects ; Dopamine/*biosynthesis ; Embryo, Mammalian/*cytology ; Mice ; Motor Activity ; Neurons/*cytology/metabolism ; Parkinsonian Disorders/*therapy ; Rats ; *Stem Cell Transplantation ; Stem Cells/*physiology ; Teratoma/etiology
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    Subthalamic GAD gene therapy in a Parkinson's disease rat model (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-10-12
    Description: The motor abnormalities of Parkinson's disease (PD) are caused by alterations in basal ganglia network activity, including disinhibition of the subthalamic nucleus (STN), and excessive activity of the major output nuclei. Using adeno-associated viral vector-mediated somatic cell gene transfer, we expressed glutamic acid decarboxylase (GAD), the enzyme that catalyzes synthesis of the neurotransmitter GABA, in excitatory glutamatergic neurons of the STN in rats. The transduced neurons, when driven by electrical stimulation, produced mixed inhibitory responses associated with GABA release. This phenotypic shift resulted in strong neuroprotection of nigral dopamine neurons and rescue of the parkinsonian behavioral phenotype. This strategy suggests that there is plasticity between excitatory and inhibitory neurotransmission in the mammalian brain that could be exploited for therapeutic benefit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luo, Jia -- Kaplitt, Michael G -- Fitzsimons, Helen L -- Zuzga, David S -- Liu, Yuhong -- Oshinsky, Michael L -- During, Matthew J -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):425-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Functional Genomics and Translational Neuroscience Laboratory, Department of Molecular Medicine and Pathology, University of Auckland, Auckland, New Zealand.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12376704" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dependovirus/genetics ; Disease Models, Animal ; Dopamine/metabolism ; Electric Stimulation ; Electrophysiology ; *Genetic Therapy ; Genetic Vectors ; Glutamate Decarboxylase/*genetics/metabolism ; Glutamic Acid/metabolism ; Humans ; Ibotenic Acid/pharmacology ; Isoenzymes/*genetics/metabolism ; Male ; Mesencephalon/metabolism/pathology ; Mice ; Motor Activity/drug effects ; Nerve Degeneration ; Neurons/*metabolism ; Oxidopamine/pharmacology ; Parkinsonian Disorders/metabolism/pathology/*therapy ; Phenotype ; Rats ; Stem Cells/virology ; Substantia Nigra/*metabolism/pathology/physiopathology ; Subthalamic Nucleus/*metabolism/pathology ; Synaptic Transmission ; Transgenes ; gamma-Aminobutyric Acid/metabolism
    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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