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  • Signal Transduction  (180)
  • American Association for the Advancement of Science (AAAS)  (180)
  • PANGAEA
  • 2000-2004  (180)
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  • American Association for the Advancement of Science (AAAS)  (180)
  • PANGAEA
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  • 1
    Publication Date: 2003-11-08
    Description: Drosophila melanogaster is a proven model system for many aspects of human biology. Here we present a two-hybrid-based protein-interaction map of the fly proteome. A total of 10,623 predicted transcripts were isolated and screened against standard and normalized complementary DNA libraries to produce a draft map of 7048 proteins and 20,405 interactions. A computational method of rating two-hybrid interaction confidence was developed to refine this draft map to a higher confidence map of 4679 proteins and 4780 interactions. Statistical modeling of the network showed two levels of organization: a short-range organization, presumably corresponding to multiprotein complexes, and a more global organization, presumably corresponding to intercomplex connections. The network recapitulated known pathways, extended pathways, and uncovered previously unknown pathway components. This map serves as a starting point for a systems biology modeling of multicellular organisms, including humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giot, L -- Bader, J S -- Brouwer, C -- Chaudhuri, A -- Kuang, B -- Li, Y -- Hao, Y L -- Ooi, C E -- Godwin, B -- Vitols, E -- Vijayadamodar, G -- Pochart, P -- Machineni, H -- Welsh, M -- Kong, Y -- Zerhusen, B -- Malcolm, R -- Varrone, Z -- Collis, A -- Minto, M -- Burgess, S -- McDaniel, L -- Stimpson, E -- Spriggs, F -- Williams, J -- Neurath, K -- Ioime, N -- Agee, M -- Voss, E -- Furtak, K -- Renzulli, R -- Aanensen, N -- Carrolla, S -- Bickelhaupt, E -- Lazovatsky, Y -- DaSilva, A -- Zhong, J -- Stanyon, C A -- Finley, R L Jr -- White, K P -- Braverman, M -- Jarvie, T -- Gold, S -- Leach, M -- Knight, J -- Shimkets, R A -- McKenna, M P -- Chant, J -- Rothberg, J M -- HG01536/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2003 Dec 5;302(5651):1727-36. Epub 2003 Nov 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CuraGen Corporation, 555 Long Wharf Drive, New Haven, CT 06511, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14605208" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Cell Cycle ; Cell Differentiation ; Cloning, Molecular ; Computational Biology ; DNA, Complementary ; Drosophila Proteins/*metabolism ; Drosophila melanogaster/*genetics/*metabolism/physiology ; Genes, Insect ; Immunity, Innate ; Mathematics ; Models, Statistical ; Photoreceptor Cells, Invertebrate/cytology ; Protein Binding ; *Protein Interaction Mapping ; *Proteome ; RNA Splicing ; RNA, Messenger/genetics/metabolism ; Receptor, Epidermal Growth Factor/metabolism ; Signal Transduction ; Transcription, Genetic ; Two-Hybrid System Techniques
    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
    Publication Date: 2004-12-18
    Description: Fat tissue produces a variety of secreted proteins (adipocytokines) with important roles in metabolism. We isolated a newly identified adipocytokine, visfatin, that is highly enriched in the visceral fat of both humans and mice and whose expression level in plasma increases during the development of obesity. Visfatin corresponds to a protein identified previously as pre-B cell colony-enhancing factor (PBEF), a 52-kilodalton cytokine expressed in lymphocytes. Visfatin exerted insulin-mimetic effects in cultured cells and lowered plasma glucose levels in mice. Mice heterozygous for a targeted mutation in the visfatin gene had modestly higher levels of plasma glucose relative to wild-type littermates. Surprisingly, visfatin binds to and activates the insulin receptor. Further study of visfatin's physiological role may lead to new insights into glucose homeostasis and/or new therapies for metabolic disorders such as diabetes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fukuhara, Atsunori -- Matsuda, Morihiro -- Nishizawa, Masako -- Segawa, Katsumori -- Tanaka, Masaki -- Kishimoto, Kae -- Matsuki, Yasushi -- Murakami, Mirei -- Ichisaka, Tomoko -- Murakami, Hiroko -- Watanabe, Eijiro -- Takagi, Toshiyuki -- Akiyoshi, Megumi -- Ohtsubo, Tsuguteru -- Kihara, Shinji -- Yamashita, Shizuya -- Makishima, Makoto -- Funahashi, Tohru -- Yamanaka, Shinya -- Hiramatsu, Ryuji -- Matsuzawa, Yuji -- Shimomura, Iichiro -- New York, N.Y. -- Science. 2005 Jan 21;307(5708):426-30. Epub 2004 Dec 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine and Pathophysiology, Graduate School of Medicine, and Department of Organismal Biosystems, Graduate School of Frontier Biosciences, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604363" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/drug effects/metabolism ; Adipose Tissue/*metabolism ; Animals ; Binding Sites ; Blood Glucose/analysis ; Cell Line ; Cells, Cultured ; Cytokines/blood/genetics/*metabolism/pharmacology ; Diabetes Mellitus, Type 2/metabolism ; Dose-Response Relationship, Drug ; Female ; Gene Expression Profiling ; Gene Expression Regulation/drug effects ; Gene Targeting ; Humans ; Insulin/blood/*metabolism ; Insulin Resistance ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Obese ; Molecular Mimicry ; Muscle Cells/metabolism ; Nicotinamide Phosphoribosyltransferase ; Phosphorylation ; Receptor, Insulin/metabolism ; Recombinant Proteins/pharmacology ; Signal Transduction ; Subcutaneous Tissue ; Viscera
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2001-02-27
    Description: The mammalian innate immune system retains from Drosophila a family of homologous Toll-like receptors (TLRs) that mediate responses to microbial ligands. Here, we show that TLR2 activation leads to killing of intracellular Mycobacterium tuberculosis in both mouse and human macrophages, through distinct mechanisms. In mouse macrophages, bacterial lipoprotein activation of TLR2 leads to a nitric oxide-dependent killing of intracellular tubercle bacilli, but in human monocytes and alveolar macrophages, this pathway was nitric oxide-independent. Thus, mammalian TLRs respond (as Drosophila Toll receptors do) to microbial ligands and also have the ability to activate antimicrobial effector pathways at the site of infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thoma-Uszynski, S -- Stenger, S -- Takeuchi, O -- Ochoa, M T -- Engele, M -- Sieling, P A -- Barnes, P F -- Rollinghoff, M -- Bolcskei, P L -- Wagner, M -- Akira, S -- Norgard, M V -- Belisle, J T -- Godowski, P J -- Bloom, B R -- Modlin, R L -- AI 07118/AI/NIAID NIH HHS/ -- AI 22553/AI/NIAID NIH HHS/ -- AI 47868/AI/NIAID NIH HHS/ -- AR 40312/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Feb 23;291(5508):1544-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Dermatology, Department of Microbiology and Immunology and Molecular Biology Institute, UCLA School of Medicine, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11222859" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/immunology ; Cell Line ; Cells, Cultured ; *Drosophila Proteins ; Humans ; Interferon-gamma/immunology/pharmacology ; Ligands ; Lipoproteins/*immunology ; Macrophage Activation ; Macrophages/immunology/metabolism/*microbiology ; Macrophages, Alveolar/immunology/metabolism/microbiology ; Macrophages, Peritoneal/immunology/metabolism/microbiology ; Membrane Glycoproteins/*metabolism ; Mice ; Monocytes/immunology/metabolism/*microbiology ; Mycobacterium tuberculosis/growth & development/*immunology ; Nitric Oxide/*metabolism ; Nitric Oxide Synthase/antagonists & inhibitors/metabolism ; Nitric Oxide Synthase Type II ; Receptors, Cell Surface/*metabolism ; Signal Transduction ; Toll-Like Receptor 2 ; Toll-Like Receptors ; Tumor Necrosis Factor-alpha/immunology/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2004-07-13
    Description: Erythropoietin (EPO) is both hematopoietic and tissue protective, putatively through interaction with different receptors. We generated receptor subtype-selective ligands allowing the separation of EPO's bioactivities at the cellular level and in animals. Carbamylated EPO (CEPO) or certain EPO mutants did not bind to the classical EPO receptor (EPOR) and did not show any hematopoietic activity in human cell signaling assays or upon chronic dosing in different animal species. Nevertheless, CEPO and various nonhematopoietic mutants were cytoprotective in vitro and conferred neuroprotection against stroke, spinal cord compression, diabetic neuropathy, and experimental autoimmune encephalomyelitis at a potency and efficacy comparable to EPO.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leist, Marcel -- Ghezzi, Pietro -- Grasso, Giovanni -- Bianchi, Roberto -- Villa, Pia -- Fratelli, Maddalena -- Savino, Costanza -- Bianchi, Marina -- Nielsen, Jacob -- Gerwien, Jens -- Kallunki, Pekka -- Larsen, Anna Kirstine -- Helboe, Lone -- Christensen, Soren -- Pedersen, Lars O -- Nielsen, Mette -- Torup, Lars -- Sager, Thomas -- Sfacteria, Alessandra -- Erbayraktar, Serhat -- Erbayraktar, Zubeyde -- Gokmen, Necati -- Yilmaz, Osman -- Cerami-Hand, Carla -- Xie, Qiao-Wen -- Coleman, Thomas -- Cerami, Anthony -- Brines, Michael -- New York, N.Y. -- Science. 2004 Jul 9;305(5681):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉H. Lundbeck A/S, 2500 Valby, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15247477" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Binding Sites ; Cells, Cultured ; Diabetic Neuropathies/drug therapy ; Drug Design ; Encephalomyelitis, Autoimmune, Experimental/drug therapy ; Erythropoiesis ; Erythropoietin/*analogs & ; derivatives/chemistry/genetics/metabolism/pharmacology/*therapeutic use ; Female ; Hematocrit ; Humans ; Ligands ; Mice ; Mice, Inbred C3H ; Mutagenesis ; Nervous System Diseases/*drug therapy ; Neurons/metabolism ; Neuroprotective Agents/chemistry/metabolism/pharmacology/*therapeutic use ; Rats ; Rats, Sprague-Dawley ; Receptors, Erythropoietin/metabolism ; Recombinant Proteins ; Signal Transduction ; Spinal Cord Compression/drug therapy ; Stroke/drug therapy ; Structure-Activity Relationship
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  • 5
    Publication Date: 2002-10-05
    Description: We have identified 242 Anopheles gambiae genes from 18 gene families implicated in innate immunity and have detected marked diversification relative to Drosophila melanogaster. Immune-related gene families involved in recognition, signal modulation, and effector systems show a marked deficit of orthologs and excessive gene expansions, possibly reflecting selection pressures from different pathogens encountered in these insects' very different life-styles. In contrast, the multifunctional Toll signal transduction pathway is substantially conserved, presumably because of counterselection for developmental stability. Representative expression profiles confirm that sequence diversification is accompanied by specific responses to different immune challenges. Alternative RNA splicing may also contribute to expansion of the immune repertoire.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Christophides, George K -- Zdobnov, Evgeny -- Barillas-Mury, Carolina -- Birney, Ewan -- Blandin, Stephanie -- Blass, Claudia -- Brey, Paul T -- Collins, Frank H -- Danielli, Alberto -- Dimopoulos, George -- Hetru, Charles -- Hoa, Ngo T -- Hoffmann, Jules A -- Kanzok, Stefan M -- Letunic, Ivica -- Levashina, Elena A -- Loukeris, Thanasis G -- Lycett, Gareth -- Meister, Stephan -- Michel, Kristin -- Moita, Luis F -- Muller, Hans-Michael -- Osta, Mike A -- Paskewitz, Susan M -- Reichhart, Jean-Marc -- Rzhetsky, Andrey -- Troxler, Laurent -- Vernick, Kenneth D -- Vlachou, Dina -- Volz, Jennifer -- von Mering, Christian -- Xu, Jiannong -- Zheng, Liangbiao -- Bork, Peer -- Kafatos, Fotis C -- New York, N.Y. -- Science. 2002 Oct 4;298(5591):159-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12364793" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Animals ; Anopheles/*genetics/*immunology/metabolism/microbiology/parasitology ; Apoptosis ; Bacteria/immunology ; Catechol Oxidase/metabolism ; Computational Biology ; Drosophila Proteins/chemistry/genetics/metabolism ; Drosophila melanogaster/genetics/immunology/metabolism ; Enzyme Precursors/metabolism ; Gene Expression Regulation ; *Genes, Insect ; Genome ; Immunity, Innate ; Insect Proteins/chemistry/genetics/metabolism ; Multigene Family ; Peptides/metabolism ; Phylogeny ; Plasmodium/immunology/physiology ; Protein Structure, Tertiary ; Selection, Genetic ; Serine Endopeptidases/metabolism ; Serpins/metabolism ; Signal Transduction
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  • 6
    Publication Date: 2001-11-10
    Description: We describe a molecular switch based on the controlled methylation of nucleosome and the transcriptional cofactors, the CREB-binding proteins (CBP)/p300. The CBP/p300 methylation site is localized to an arginine residue that is essential for stabilizing the structure of the KIX domain, which mediates CREB recruitment. Methylation of KIX by coactivator-associated arginine methyltransferase 1 (CARM1) blocks CREB activation by disabling the interaction between KIX and the kinase inducible domain (KID) of CREB. Thus, CARM1 functions as a corepressor in cyclic adenosine monophosphate signaling pathway via its methyltransferase activity while acting as a coactivator for nuclear hormones. These results provide strong in vivo and in vitro evidence that histone methylation plays a key role in hormone-induced gene activation and define cofactor methylation as a new regulatory mechanism in hormone signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, W -- Chen, H -- Du, K -- Asahara, H -- Tini, M -- Emerson, B M -- Montminy, M -- Evans, R M -- 9R01DK57978/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2507-11. Epub 2001 Nov 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Expression Laboratory, Department of Biological Chemistry, University of California Davis Cancer Center/Basic Science, Sacramento, CA 95817, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11701890" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/metabolism ; Amino Acid Sequence ; Animals ; Apoptosis ; Cell Line ; Cyclic AMP Response Element-Binding Protein/metabolism ; Dimerization ; E1A-Associated p300 Protein ; *Gene Expression Regulation ; Genes, Reporter ; Histone Acetyltransferases ; Histones/metabolism ; Methylation ; Molecular Sequence Data ; Nerve Growth Factor/pharmacology ; Nuclear Proteins/chemistry/*metabolism ; PC12 Cells ; Protein Structure, Tertiary ; Protein-Arginine N-Methyltransferases/*metabolism ; Rats ; Receptors, Retinoic Acid/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Somatostatin/genetics ; Trans-Activators/chemistry/*metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic ; Transcriptional Activation ; Transfection ; Tretinoin/metabolism/pharmacology
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  • 7
    Publication Date: 2001-12-18
    Description: Agrobacterium tumefaciens is a plant pathogen capable of transferring a defined segment of DNA to a host plant, generating a gall tumor. Replacing the transferred tumor-inducing genes with exogenous DNA allows the introduction of any desired gene into the plant. Thus, A. tumefaciens has been critical for the development of modern plant genetics and agricultural biotechnology. Here we describe the genome of A. tumefaciens strain C58, which has an unusual structure consisting of one circular and one linear chromosome. We discuss genome architecture and evolution and additional genes potentially involved in virulence and metabolic parasitism of host plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goodner, B -- Hinkle, G -- Gattung, S -- Miller, N -- Blanchard, M -- Qurollo, B -- Goldman, B S -- Cao, Y -- Askenazi, M -- Halling, C -- Mullin, L -- Houmiel, K -- Gordon, J -- Vaudin, M -- Iartchouk, O -- Epp, A -- Liu, F -- Wollam, C -- Allinger, M -- Doughty, D -- Scott, C -- Lappas, C -- Markelz, B -- Flanagan, C -- Crowell, C -- Gurson, J -- Lomo, C -- Sear, C -- Strub, G -- Cielo, C -- Slater, S -- R15 GM61690-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2323-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Hiram College, Hiram, OH 44234, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743194" target="_blank"〉PubMed〈/a〉
    Keywords: Agrobacterium tumefaciens/classification/*genetics/pathogenicity/physiology ; Bacterial Proteins/chemistry/genetics/metabolism ; Carrier Proteins/chemistry/genetics/metabolism ; Cell Cycle ; Chromosomes, Bacterial/genetics ; DNA Replication ; Genes, Bacterial ; *Genome, Bacterial ; Molecular Sequence Data ; Phylogeny ; Plant Tumors/microbiology ; Plants/microbiology ; Plasmids ; Replicon ; Rhizobiaceae/genetics ; *Sequence Analysis, DNA ; Signal Transduction ; Sinorhizobium meliloti/genetics ; Synteny ; Telomere ; Virulence/genetics
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  • 8
    Publication Date: 2001-03-17
    Description: Caenorhabditis elegans oocytes, like those of most animals, arrest during meiotic prophase. Sperm promote the resumption of meiosis (maturation) and contraction of smooth muscle-like gonadal sheath cells, which are required for ovulation. We show that the major sperm cytoskeletal protein (MSP) is a bipartite signal for oocyte maturation and sheath contraction. MSP also functions in sperm locomotion, playing a role analogous to actin. Thus, during evolution, MSP has acquired extracellular signaling and intracellular cytoskeletal functions for reproduction. Proteins with MSP-like domains are found in plants, fungi, and other animals, suggesting that related signaling functions may exist in other phyla.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, M A -- Nguyen, V Q -- Lee, M H -- Kosinski, M -- Schedl, T -- Caprioli, R M -- Greenstein, D -- CA09592/CA/NCI NIH HHS/ -- GM57173/GM/NIGMS NIH HHS/ -- GM58008/GM/NIGMS NIH HHS/ -- HD07043/HD/NICHD NIH HHS/ -- HD25614/HD/NICHD NIH HHS/ -- R01 GM057173/GM/NIGMS NIH HHS/ -- R01 HD025614/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 16;291(5511):2144-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11251118" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans/*physiology ; Carrier Proteins/chemistry/physiology ; Cytoskeleton/chemistry/physiology ; Disorders of Sex Development ; Enzyme Activation ; Evolution, Molecular ; Female ; Gonads/cytology/physiology ; Helminth Proteins/chemistry/immunology/pharmacology/*physiology ; MAP Kinase Signaling System ; Male ; *Meiosis ; Membrane Proteins/chemistry/physiology ; Microinjections ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; Oocytes/*physiology ; Ovulation ; Phylogeny ; Protein Folding ; Protein Structure, Tertiary ; Pseudopodia/physiology ; Recombinant Proteins/pharmacology ; Signal Transduction ; Sperm Motility ; Spermatozoa/chemistry/*physiology
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  • 9
    Publication Date: 2002-06-22
    Description: The production of functional female gametes is essential for the propagation of all vertebrate species. The growth of oocytes within ovarian follicles and their development to mature eggs have fascinated biologists for centuries, and scientists have long realized the importance of the ovarian follicle's somatic cells in nurturing oogenesis and delivering the oocyte to the oviduct by ovulation. Recent studies have revealed key roles of the oocyte in folliculogenesis and established that bidirectional communication between the oocyte and companion somatic cells is essential for development of an egg competent to undergo fertilization and embryogenesis. The challenge for the future is to identify the factors that participate in this communication and their mechanisms of action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matzuk, Martin M -- Burns, Kathleen H -- Viveiros, Maria M -- Eppig, John J -- CA60651/CA/NCI NIH HHS/ -- CA62392/CA/NCI NIH HHS/ -- EY07102/EY/NEI NIH HHS/ -- GM07330/GM/NIGMS NIH HHS/ -- HD07495/HD/NICHD NIH HHS/ -- HD23839/HD/NICHD NIH HHS/ -- HD32067/HD/NICHD NIH HHS/ -- HD33438/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2178-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030, USA. mmatzuk@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077402" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Communication ; Embryonic and Fetal Development ; Female ; Granulosa Cells/physiology ; Oocytes/*physiology ; *Oogenesis ; Ovarian Follicle/*physiology ; Signal Transduction
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  • 10
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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