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  • Articles  (1,027)
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  • Articles  (1,027)
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  • 1
    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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  • 2
    Publication Date: 2002-04-06
    Description: Higher order chromatin structure presents a barrier to the recognition and repair of DNA damage. Double-strand breaks (DSBs) induce histone H2AX phosphorylation, which is associated with the recruitment of repair factors to damaged DNA. To help clarify the physiological role of H2AX, we targeted H2AX in mice. Although H2AX is not essential for irradiation-induced cell-cycle checkpoints, H2AX-/- mice were radiation sensitive, growth retarded, and immune deficient, and mutant males were infertile. These pleiotropic phenotypes were associated with chromosomal instability, repair defects, and impaired recruitment of Nbs1, 53bp1, and Brca1, but not Rad51, to irradiation-induced foci. Thus, H2AX is critical for facilitating the assembly of specific DNA-repair complexes on damaged DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721576/" 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/PMC4721576/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celeste, Arkady -- Petersen, Simone -- Romanienko, Peter J -- Fernandez-Capetillo, Oscar -- Chen, Hua Tang -- Sedelnikova, Olga A -- Reina-San-Martin, Bernardo -- Coppola, Vincenzo -- Meffre, Eric -- Difilippantonio, Michael J -- Redon, Christophe -- Pilch, Duane R -- Olaru, Alexandru -- Eckhaus, Michael -- Camerini-Otero, R Daniel -- Tessarollo, Lino -- Livak, Ferenc -- Manova, Katia -- Bonner, William M -- Nussenzweig, Michel C -- Nussenzweig, Andre -- Z99 CA999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):922-7. Epub 2002 Apr 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, NIH, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934988" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology/physiology ; Base Sequence ; Cell Aging ; Cell Cycle ; Cells, Cultured ; *Chromosome Aberrations ; DNA Damage ; *DNA Repair ; Female ; Gene Targeting ; Histones/chemistry/*genetics/*physiology ; Immunoglobulin Class Switching ; Infertility, Male/genetics/physiopathology ; Lymphocyte Count ; Male ; Meiosis ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; Phosphorylation ; *Recombination, Genetic ; Spermatocytes/physiology ; T-Lymphocytes/immunology/physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2003-04-05
    Description: The ability to visualize, track, and quantify molecules and events in living cells with high spatial and temporal resolution is essential for understanding biological systems. Only recently has it become feasible to carry out these tasks due to the advent of fluorescent protein technology. Here, we trace the development of highly visible and minimally perturbing fluorescent proteins that, together with updated fluorescent imaging techniques, are providing unprecedented insights into the movement of proteins and their interactions with cellular components in living cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lippincott-Schwartz, Jennifer -- Patterson, George H -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):87-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. jlippin@helix.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12677058" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Physiological Phenomena ; Diagnostic Imaging/*methods ; Fluorescence ; Fluorescence Recovery After Photobleaching/methods ; Fluorometry/methods ; Green Fluorescent Proteins ; Kinetics ; Light ; *Luminescent Proteins/chemistry/genetics/metabolism ; Microscopy/*methods ; Microscopy, Fluorescence/*methods ; Mutagenesis ; Protein Engineering ; Proteins/*metabolism ; Recombinant Fusion Proteins ; Spectrometry, Fluorescence
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2002-12-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Funes, Soledad -- Davidson, Edgar -- Reyes-Prieto, Adrian -- Magallon, Susana -- Herion, Pascal -- King, Michael P -- Gonzalez-Halphen, Diego -- HL59646/HL/NHLBI NIH HHS/ -- TW01176/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2155.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto de Fisiologia Celular, Universidad Nacional Autonoma de Mexico (UNAM), 04510 D.F., Mexico.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481129" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Apicomplexa/enzymology/*genetics/ultrastructure ; *Biological Evolution ; Cell Nucleus/genetics ; Chlamydomonas reinhardtii/enzymology/genetics ; Chlorophyta/enzymology/*genetics ; Cloning, Molecular ; DNA, Mitochondrial/genetics ; Electron Transport Complex IV/chemistry/*genetics ; *Gene Transfer, Horizontal ; Genes ; Genes, Protozoan ; Molecular Sequence Data ; Phylogeny ; Plastids/*genetics ; Symbiosis ; Toxoplasma/enzymology/genetics
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    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-08-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ingolia, Nicholas T -- Murray, Andrew W -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):948-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology and Bauer Center for Genomics Research, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12169717" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Animals ; Biological Evolution ; *Cell Cycle Proteins ; Cells, Cultured ; Dual Specificity Phosphatase 1 ; *Feedback, Physiological ; Immediate-Early Proteins/*metabolism ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/*metabolism ; Models, Biological ; *Phosphoprotein Phosphatases ; Platelet-Derived Growth Factor/metabolism/pharmacology ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-05-11
    Description: Breast cancer manifests itself in the mammary epithelium, yet there is a growing recognition that mammary stromal cells also play an important role in tumorigenesis. During its developmental cycle, the mammary gland displays many of the properties associated with breast cancer, and many of the stromal factors necessary for mammary development also promote or protect against breast cancer. Here we review our present knowledge of the specific factors and cell types that contribute to epithelial-stromal crosstalk during mammary development. To find cures for diseases like breast cancer that rely on epithelial-stromal crosstalk, we must understand how these different cell types communicate with each other.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2788989/" 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/PMC2788989/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wiseman, Bryony S -- Werb, Zena -- CA57621/CA/NCI NIH HHS/ -- R01 CA057621/CA/NCI NIH HHS/ -- R01 CA057621-07/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 May 10;296(5570):1046-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy, University of California, 513 Parnassus Avenue, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004111" target="_blank"〉PubMed〈/a〉
    Keywords: Adipocytes/cytology/physiology ; Animals ; Apoptosis ; Breast/cytology/embryology/*growth & development/physiology ; Breast Neoplasms/pathology/*physiopathology ; Cell Communication ; Epithelial Cells/physiology ; Extracellular Matrix/physiology ; Female ; Humans ; Mammary Glands, Animal/cytology/embryology/*growth & development/physiology ; Mammary Neoplasms, Animal/pathology/*physiopathology ; Morphogenesis ; Neoplasm Metastasis ; Pregnancy ; Signal Transduction ; Stromal Cells/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallo, Robert C -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1728-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Human Virology and Department of Microbiology and Immunology, University of Maryland, Baltimore, MD 21201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459576" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Serodiagnosis/history ; Acquired Immunodeficiency Syndrome/diagnosis/*history/immunology/virology ; CD4-Positive T-Lymphocytes/virology ; Cell Line ; Cells, Cultured ; France ; *HIV/classification/isolation & purification/physiology ; History, 20th Century ; Human T-lymphotropic virus 1/isolation & purification/physiology ; Human T-lymphotropic virus 2/isolation & purification/physiology ; Humans ; Interleukin-2/history/isolation & purification/physiology ; Patents as Topic/history ; RNA-Directed DNA Polymerase/history/isolation & purification/metabolism ; United States ; Virus Cultivation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gallo, Robert C -- Montagnier, Luc -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1730-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Human Virology and Department of Microbiology and Immunology, University of Maryland, Baltimore, MD 21201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459577" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/immunology/therapeutic use ; *Acquired Immunodeficiency Syndrome/drug therapy/prevention & ; control/transmission/virology ; Anti-HIV Agents/therapeutic use ; Biomedical Research ; Clinical Trials as Topic ; Developed Countries ; Developing Countries ; Drug Costs ; Female ; HIV/drug effects ; Health Services/economics ; Humans ; Infant, Newborn ; Infectious Disease Transmission, Vertical ; International Cooperation ; Pregnancy ; Pregnancy Complications, Infectious/drug therapy ; Research Support as Topic ; Technology Transfer ; United Nations
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2002-06-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Copeland, Neal G -- Jenkins, Nancy A -- O'Brien, Stephen J -- New York, N.Y. -- Science. 2002 May 31;296(5573):1617-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mouse Cancer Genetics Program, National Cancer Institute, Frederick, MD, 21702, USA. copeland@ncifcrf.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040165" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Biological Evolution ; Chromosome Aberrations ; Chromosomes/*genetics ; Chromosomes, Human/genetics ; Computational Biology ; Conserved Sequence ; Evolution, Molecular ; Gene Duplication ; Gene Rearrangement ; Genes ; Genome ; *Genome, Human ; Genomics ; Humans ; Mice ; Mice, Inbred Strains/*genetics ; Multigene Family ; *Sequence Analysis, DNA ; Species Specificity ; Synteny
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2003-04-12
    Description: Rapid turnover of the tumor suppressor protein p53 requires the MDM2 ubiquitin ligase, and both interact with p300-CREB-binding protein transcriptional coactivator proteins. p53 is stabilized by the binding of p300 to the oncoprotein E1A, suggesting that p300 regulates p53 degradation. Purified p300 exhibited intrinsic ubiquitin ligase activity that was inhibited by E1A. In vitro, p300 with MDM2 catalyzed p53 polyubiquitination, whereas MDM2 catalyzed p53 monoubiquitination. E1A expression caused a decrease in polyubiquitinated but not monoubiquitinated p53 in cells. Thus, generation of the polyubiquitinated forms of p53 that are targeted for proteasome degradation requires the intrinsic ubiquitin ligase activities of MDM2 and p300.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grossman, Steven R -- Deato, Maria E -- Brignone, Chrystelle -- Chan, Ho Man -- Kung, Andrew L -- Tagami, Hideaki -- Nakatani, Yoshihiro -- Livingston, David M -- CA15751/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):342-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690203" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/metabolism ; Animals ; Catalysis ; Cells, Cultured ; E1A-Associated p300 Protein ; Embryo, Mammalian ; Fibroblasts/metabolism ; Humans ; Ligases/antagonists & inhibitors/metabolism ; Mice ; Nuclear Proteins/antagonists & inhibitors/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Trans-Activators/antagonists & inhibitors/*metabolism ; Transfection ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/*metabolism ; Ubiquitin-Protein Ligases ; Ubiquitins/*metabolism
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  • 11
    Publication Date: 2003-07-05
    Description: Raf kinases have been linked to endothelial cell survival. Here, we show that basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF) differentially activate Raf, resulting in protection from distinct pathways of apoptosis in human endothelial cells and chick embryo vasculature. bFGF activated Raf-1 via p21-activated protein kinase-1 (PAK-1) phosphorylation of serines 338 and 339, resulting in Raf-1 mitochondrial translocation and endothelial cell protection from the intrinsic pathway of apoptosis, independent of the mitogen-activated protein kinase kinase-1 (MEK1). In contrast, VEGF activated Raf-1 via Src kinase, leading to phosphorylation of tyrosines 340 and 341 and MEK1-dependent protection from extrinsic-mediated apoptosis. These findings implicate Raf-1 as a pivotal regulator of endothelial cell survival during angiogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alavi, Alireza -- Hood, John D -- Frausto, Ricardo -- Stupack, Dwayne G -- Cheresh, David A -- CA45726/CA/NCI NIH HHS/ -- CA50286/CA/NCI NIH HHS/ -- CA75924/CA/NCI NIH HHS/ -- P01 CA78045/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 4;301(5629):94-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, 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/12843393" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cell Survival ; Cells, Cultured ; Chick Embryo ; Endothelial Growth Factors/pharmacology ; Endothelium, Vascular/*cytology/drug effects ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Fibroblast Growth Factor 2/pharmacology ; Flavonoids/pharmacology ; Humans ; Intercellular Signaling Peptides and Proteins/pharmacology ; Lymphokines/pharmacology ; MAP Kinase Kinase 1 ; Mitochondria/metabolism ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinase Kinases/antagonists & inhibitors/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Neovascularization, Pathologic ; *Neovascularization, Physiologic/drug effects ; Phosphorylation ; Point Mutation ; Protein Transport ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; Proto-Oncogene Proteins B-raf ; Proto-Oncogene Proteins c-raf/chemistry/genetics/*metabolism ; Signal Transduction ; Umbilical Veins ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors ; p21-Activated Kinases ; src-Family Kinases/antagonists & inhibitors/metabolism
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  • 12
    Publication Date: 2003-11-01
    Description: Mutations in MeCP2, which encodes a protein that has been proposed to function as a global transcriptional repressor, are the cause of Rett syndrome (RT T), an X-linked progressive neurological disorder. Although the selective inactivation of MeCP2 in neurons is sufficient to confer a Rett-like phenotype in mice, the specific functions of MeCP2 in postmitotic neurons are not known. We find that MeCP2 binds selectively to BDNF promoter III and functions to repress expression of the BDNF gene. Membrane depolarization triggers the calcium-dependent phosphorylation and release of MeCP2 from BDNF promoter III, thereby facilitating transcription. These studies indicate that MeCP2 plays a key role in the control of neuronal activity-dependent gene regulation and suggest that the deregulation of this process may underlie the pathology of RT T.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wen G -- Chang, Qiang -- Lin, Yingxi -- Meissner, Alexander -- West, Anne E -- Griffith, Eric C -- Jaenisch, Rudolf -- Greenberg, Michael E -- HD 18655/HD/NICHD NIH HHS/ -- NS28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):885-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593183" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor/*genetics ; Calcium/*metabolism ; Cell Membrane/physiology ; Cells, Cultured ; *Chromosomal Proteins, Non-Histone ; Cloning, Molecular ; CpG Islands ; DNA Methylation ; DNA-Binding Proteins/*metabolism ; Electrophoretic Mobility Shift Assay ; *Gene Expression Regulation ; Gene Silencing ; Histones/metabolism ; Methyl-CpG-Binding Protein 2 ; Methylation ; Mice ; Mice, Knockout ; Neurons/metabolism/physiology ; Phosphorylation ; Potassium Chloride/pharmacology ; Precipitin Tests ; Promoter Regions, Genetic ; Rats ; *Repressor Proteins ; Rett Syndrome/genetics ; *Transcription, Genetic
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  • 13
    Publication Date: 2000-01-05
    Description: The nematode pharynx has a potassium channel with unusual properties, which allows the muscles to repolarize quickly and with the proper delay. Here, the Caenorhabditis elegans exp-2 gene is shown to encode this channel. EXP-2 is a Kv-type (voltage-activated) potassium channel that has inward-rectifying properties resembling those of the structurally dissimilar human ether-a-go-go-related gene (HERG) channel. Null and gain-of-function mutations affect pharyngeal muscle excitability in ways that are consistent with the electrophysiological behavior of the channel, and thereby demonstrate a direct link between the kinetics of this unusual channel and behavior.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3791429/" 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/PMC3791429/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, M W -- Fleischhauer, R -- Dent, J A -- Joho, R H -- Avery, L -- HL46154/HL/NHLBI NIH HHS/ -- NS28407/NS/NINDS NIH HHS/ -- R01 HL046154/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2501-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9148, USA. wdavis@biology.utah.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617464" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Feeding Behavior ; Genes, Helminth ; Genes, Reporter ; Ion Channel Gating ; Kinetics ; Membrane Potentials ; Models, Molecular ; Muscles/metabolism ; Mutation ; Neurons/metabolism ; Oocytes/metabolism ; Pharyngeal Muscles/physiology ; Potassium Channels/chemistry/genetics/*physiology ; Protein Conformation ; RNA, Complementary/genetics ; Recombinant Fusion Proteins/biosynthesis ; Xenopus laevis
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  • 14
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-04-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brenner, S -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2173-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Sciences Institute, Berkeley, CA 94704, USA. brenner@molsci.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10744539" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Computational Biology ; Drosophila melanogaster/genetics ; *Gene Expression Regulation ; Genes ; *Genome ; *Molecular Biology ; *Proteins/chemistry/genetics/physiology ; Sequence Analysis, DNA
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  • 15
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-06
    Description: A human cytomegalovirus gene array was used to identify a previously unidentified class of viral transcripts. These transcripts, termed virion RNAs, were packaged within infectious virions and were delivered to the host cell on infection. This mechanism of herpesvirus gene expression allows for viral genes to be expressed within an infected cell immediately after virus entry and in the absence of transcription from the viral genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bresnahan, W A -- Shenk, T -- CA85786/CA/NCI NIH HHS/ -- F32 AI010448/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2373-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875924" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/metabolism ; Cells, Cultured ; Cytomegalovirus/*genetics/*physiology ; Dactinomycin/pharmacology ; Gene Expression ; Genes, Viral ; Genome, Viral ; Golgi Apparatus/metabolism ; Humans ; Nucleic Acid Hybridization ; Nucleic Acid Synthesis Inhibitors/pharmacology ; Oligonucleotide Array Sequence Analysis ; RNA, Messenger/*genetics/isolation & purification/metabolism ; RNA, Viral/*genetics/isolation & purification/metabolism ; Recombinant Fusion Proteins/metabolism ; Transcription, Genetic ; Viral Proteins/genetics/metabolism ; Virion/*genetics/physiology ; Virus Assembly
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  • 16
    Publication Date: 2000-09-01
    Description: Activation of the transcription factor nuclear factor (NF)-kappaB by proinflammatory stimuli leads to increased expression of genes involved in inflammation. Activation of NF-kappaB requires the activity of an inhibitor of kappaB (IkappaB)-kinase (IKK) complex containing two kinases (IKKalpha and IKKbeta) and the regulatory protein NEMO (NF-kappaB essential modifier). An amino-terminal alpha-helical region of NEMO associated with a carboxyl-terminal segment of IKKalpha and IKKbeta that we term the NEMO-binding domain (NBD). A cell-permeable NBD peptide blocked association of NEMO with the IKK complex and inhibited cytokine-induced NF-kappaB activation and NF-kappaB-dependent gene expression. The peptide also ameliorated inflammatory responses in two experimental mouse models of acute inflammation. The NBD provides a target for the development of drugs that would block proinflammatory activation of the IKK complex without inhibiting basal NF-kappaB activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉May, M J -- D'Acquisto, F -- Madge, L A -- Glockner, J -- Pober, J S -- Ghosh, S -- AI 33443/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 1;289(5484):1550-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology and Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10968790" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/chemistry/pharmacology ; COS Cells ; Cells, Cultured ; E-Selectin/biosynthesis/genetics ; Endothelium, Vascular/metabolism ; Gene Expression Regulation ; HeLa Cells ; Humans ; I-kappa B Kinase ; Inflammation/drug therapy ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; NF-kappa B/*metabolism ; Peptides/chemistry/*pharmacology ; Point Mutation ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism
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  • 17
    Publication Date: 2000-05-29
    Description: Pathogenic mycobacteria, including the agent of tuberculosis, Mycobacterium tuberculosis, must replicate in macrophages for long-term persistence within their niche during chronic infection: organized collections of macrophages and lymphocytes called granulomas. We identified several genes preferentially expressed when Mycobacterium marinum, the cause of fish and amphibian tuberculosis, resides in host granulomas and/or macrophages. Two were homologs of M. tuberculosis PE/PE-PGRS genes, a family encoding numerous repetitive glycine-rich proteins of unknown function. Mutation of two PE-PGRS genes produced M. marinum strains incapable of replication in macrophages and with decreased persistence in granulomas. Our results establish a direct role in virulence for some PE-PGRS proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ramakrishnan, L -- Federspiel, N A -- Falkow, S -- AI 32396/AI/NIAID NIH HHS/ -- K08 AI 01400/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 May 26;288(5470):1436-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. lalitar@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827956" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/chemistry/*genetics ; Cells, Cultured ; Disease Models, Animal ; Gene Expression Profiling ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Glycine/analysis ; Granuloma/*microbiology/pathology ; Humans ; Macrophages/*microbiology ; Mutation ; Mycobacterium Infections, Nontuberculous/*microbiology/pathology ; Mycobacterium marinum/*genetics/growth & development/*pathogenicity ; Mycobacterium tuberculosis/genetics/pathogenicity ; Promoter Regions, Genetic ; Rana pipiens ; Tuberculosis/microbiology ; Virulence
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  • 18
    Publication Date: 2000-07-15
    Description: Bone morphogenetic proteins (BMPs) have multiple functions in the developing nervous system. A member of this family, BMP-9, was found to be highly expressed in the embryonic mouse septum and spinal cord, indicating a possible role in regulating the cholinergic phenotype. In cultured neurons, BMP-9 directly induced the expression of the cholinergic gene locus encoding choline acetyltransferase and the vesicular acetylcholine transporter and up-regulated acetylcholine synthesis. The effect was reversed upon withdrawal of BMP-9. Intracerebroventricular injection of BMP-9 increased acetylcholine levels in vivo. Although certain other BMPs also up-regulated the cholinergic phenotype in vitro, they were less effective than BMP-9. These data indicate that BMP-9 is a differentiating factor for cholinergic central nervous system neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lopez-Coviella, I -- Berse, B -- Krauss, R -- Thies, R S -- Blusztajn, J K -- P01 AG09525/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 14;289(5477):313-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry and Department of Pathology and Laboratory Medicine, Boston University School of Medicine, Boston, MA 02118, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10894782" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/biosynthesis ; Animals ; Bone Morphogenetic Proteins/*physiology ; Carrier Proteins/genetics ; Cells, Cultured ; Central Nervous System ; Choline O-Acetyltransferase/genetics ; Embryo, Mammalian/metabolism ; Fibroblast Growth Factor 2/physiology ; Gene Expression Regulation, Developmental ; Gene Expression Regulation, Enzymologic ; Growth Differentiation Factor 2 ; *Membrane Transport Proteins ; Mice ; Neurons/metabolism ; Phenotype ; RNA, Messenger/metabolism ; Septum of Brain/embryology/metabolism ; Spinal Cord/embryology/metabolism ; Up-Regulation ; Vesicular Acetylcholine Transport Proteins ; *Vesicular Transport Proteins
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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-15
    Description: Many South Africans long dreamed of the day when the oppressive apartheid system would end. That day has come, but now the country faces a new disaster: one of the world's worst HIV epidemics--and most confusing government responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 2000 Jun 23;288(5474):2168-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10896606" target="_blank"〉PubMed〈/a〉
    Keywords: *Acquired Immunodeficiency Syndrome/epidemiology ; Anti-HIV Agents/therapeutic use ; Disease Outbreaks ; Female ; Government ; HIV Infections/drug therapy/epidemiology ; Humans ; Male ; Pregnancy ; Pregnancy Complications, Infectious/drug therapy ; Public Policy ; *Research ; South Africa/epidemiology
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  • 20
    Publication Date: 2000-02-11
    Description: The nonclassical major histocompatibility complex (MHC) class I molecule HLA-E inhibits natural killer (NK) cell-mediated lysis by interacting with CD94/NKG2A receptors. Surface expression of HLA-E depends on binding of conserved peptides derived from MHC class I molecules. The same peptide is present in the leader sequence of the human cytomegalovirus (HCMV) glycoprotein UL40 (gpUL40). It is shown that, independently of the transporter associated with antigen processing, gpUL40 can up-regulate expression of HLA-E, which protects targets from NK cell lysis. While classical MHC class I molecules are down-regulated, HLA-E is up-regulated by HCMV. Induction of HLA-E surface expression by gpUL40 may represent an escape route for HCMV.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomasec, P -- Braud, V M -- Rickards, C -- Powell, M B -- McSharry, B P -- Gadola, S -- Cerundolo, V -- Borysiewicz, L K -- McMichael, A J -- Wilkinson, G W -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1031.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Wales College of Medicine, Cardiff CF14 4XN, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669413" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; *Antigens, CD ; Cell Line ; Cell Membrane/immunology ; Cells, Cultured ; Conserved Sequence ; Cytomegalovirus/genetics/immunology/*metabolism ; Cytotoxicity, Immunologic ; Down-Regulation ; HLA Antigens/immunology/*metabolism ; Histocompatibility Antigens Class I/immunology/*metabolism ; Humans ; Killer Cells, Natural/*immunology ; Molecular Sequence Data ; Open Reading Frames ; Protein Sorting Signals/chemistry/*metabolism ; Receptors, Immunologic/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Transfection ; Up-Regulation ; Viral Proteins/chemistry/genetics/*metabolism
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  • 21
    Publication Date: 2000-05-08
    Description: The c-Jun NH2-terminal kinase (JNK) is activated when cells are exposed to ultraviolet (UV) radiation. However, the functional consequence of JNK activation in UV-irradiated cells has not been established. It is shown here that JNK is required for UV-induced apoptosis in primary murine embryonic fibroblasts. Fibroblasts with simultaneous targeted disruptions of all the functional Jnk genes were protected against UV-stimulated apoptosis. The absence of JNK caused a defect in the mitochondrial death signaling pathway, including the failure to release cytochrome c. These data indicate that mitochondria are influenced by proapoptotic signal transduction through the JNK pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tournier, C -- Hess, P -- Yang, D D -- Xu, J -- Turner, T K -- Nimnual, A -- Bar-Sagi, D -- Jones, S N -- Flavell, R A -- Davis, R J -- New York, N.Y. -- Science. 2000 May 5;288(5467):870-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular Medicine, Department of Biochemistry & Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10797012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptotic Protease-Activating Factor 1 ; Caspase 3 ; Caspase 9 ; Caspases/metabolism ; Cell Count ; Cell Division ; Cells, Cultured ; Cytochrome c Group/*metabolism ; DNA Fragmentation ; Enzyme Activation ; Fibroblasts ; Gene Targeting ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Signaling System ; Methyl Methanesulfonate/pharmacology ; Mice ; Mitochondria/metabolism ; Mitogen-Activated Protein Kinases/genetics/*metabolism ; NF-kappa B/metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Tumor Suppressor Protein p53/metabolism ; Ultraviolet Rays
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-09-23
    Description: Multicellular organisms use the products of highly polymorphic genes to distinguish self from conspecific nonself cells or tissues. These allorecognition polymorphisms may regulate somatic interactions between hosts and pathogens or between competitors (to avoid various forms of parasitism), as well as reproductive interactions between mates or between gametes (to avoid inbreeding). In both cases, rare alleles may be advantageous, but it remains unclear which mechanism maintains the genetic polymorphism for specificity in self/nonself recognition. Contrary to earlier reports, we show that mate selection cannot be a strong force maintaining allorecognition polymorphism in two colonial marine invertebrates. Instead, the regulation of intraspecific competitive interactions appears to promote the evolution of polymorphisms in these species.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grosberg, R K -- Hart, M W -- New York, N.Y. -- Science. 2000 Sep 22;289(5487):2111-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Evolution and Ecology and Center for Population Biology, One Shields Drive, University of California, Davis, CA 95616, USA. rkgrosberg@ucdavis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11000110" target="_blank"〉PubMed〈/a〉
    Keywords: *Alleles ; Animals ; Biological Evolution ; Cnidaria/*genetics/physiology ; Crosses, Genetic ; Female ; Genes ; Genotype ; Major Histocompatibility Complex ; Male ; *Polymorphism, Genetic ; *Sexual Behavior, Animal ; Urochordata/*genetics/physiology
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  • 23
    Publication Date: 2000-04-25
    Description: Major histocompatibility complex class II (MHC II) molecules capture peptides within the endocytic pathway to generate T cell receptor (TCR) ligands. Immature dendritic cells (DCs) sequester intact antigens in lysosomes, processing and converting antigens into peptide-MHC II complexes upon induction of DC maturation. The complexes then accumulate in distinctive, nonlysosomal MHC II+ vesicles that appear to migrate to the cell surface. Although the vesicles exclude soluble lysosomal contents and antigen-processing machinery, many contain MHC I and B7 costimulatory molecules. After arrival at the cell surface, the MHC and costimulatory molecules remain clustered. Thus, transport of peptide-MHC II complexes by DCs not only accomplishes transfer from late endocytic compartments to the plasma membrane, but does so in a manner that selectively concentrates TCR ligands and costimulatory molecules for T cell contact.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turley, S J -- Inaba, K -- Garrett, W S -- Ebersold, M -- Unternaehrer, J -- Steinman, R M -- Mellman, I -- AI-13013/AI/NIAID NIH HHS/ -- AI-34098/AI/NIAID NIH HHS/ -- AI-39672/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):522-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Section of Immunobiology, 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/10775112" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; *Antigen Presentation ; Antigens, CD/immunology/metabolism ; Antigens, CD86 ; B-Lymphocytes/immunology/metabolism ; Bicyclo Compounds, Heterocyclic/pharmacology ; Biological Transport ; Cell Membrane/immunology/metabolism ; Cells, Cultured ; Dendritic Cells/*immunology/*metabolism ; Endocytosis ; Endosomes/immunology/metabolism ; Histocompatibility Antigens Class I/immunology/metabolism ; Histocompatibility Antigens Class II/immunology/*metabolism ; Kinetics ; Ligands ; Lipopolysaccharides/immunology ; Lysosomes/immunology/metabolism ; Membrane Glycoproteins/immunology/metabolism ; Mice ; Mice, Inbred C3H ; Muramidase/immunology/*metabolism ; Peptide Fragments/immunology/*metabolism ; Receptors, Antigen, T-Cell/metabolism ; Thiazoles/pharmacology ; Thiazolidines
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-04-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2133-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10744529" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Chemoreceptor Cells/*physiology ; Humans ; Mice ; Multigene Family ; Receptors, Cell Surface/genetics/*physiology ; *Taste ; Taste Buds/*physiology ; Transducin/biosynthesis
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-02-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):947-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10691562" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Benzodiazepines/adverse effects/toxicity ; Brain/cytology/*drug effects/growth & development ; Ethanol/blood/*toxicity ; Female ; Humans ; Infant, Newborn ; Nerve Degeneration ; Neurons/cytology/*drug effects ; Pregnancy ; Rats ; Receptors, GABA/*drug effects/metabolism ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/*drug effects/metabolism
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-09-23
    Description: In this month's essay, Paul Nurse recapitulates the ontogeny of one of the most important theories in the history of biology, the cell theory, which proposes that all forms of life are composed of cells. Along the way, he lays out the wondrous molecular complexities and processes that he and others have discovered in the course of their studies of the lives of cells. In particular, Nurse focuses on the mechanisms and controls of cell reproduction that ultimately allow growth, development, and evolution to occur.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nurse, P -- New York, N.Y. -- Science. 2000 Sep 8;289(5485):1711-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Imperial Cancer Research Fund, London, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11001740" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Biological Evolution ; Catalysis ; Cell Biology/*history ; *Cell Cycle ; Cell Division ; *Cell Physiological Phenomena ; DNA Replication ; Energy Metabolism ; Enzymes/metabolism ; Genes ; History, 17th Century ; History, 18th Century ; History, 19th Century ; History, 20th Century ; Humans ; Neoplasms/genetics/pathology ; Organelles/metabolism ; Signal Transduction
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  • 27
    Publication Date: 2000-08-19
    Description: Pig cloning will have a marked impact on the optimization of meat production and xenotransplantation. To clone pigs from differentiated cells, we microinjected the nuclei of porcine (Sus scrofa) fetal fibroblasts into enucleated oocytes, and development was induced by electroactivation. The transfer of 110 cloned embryos to four surrogate mothers produced an apparently normal female piglet. The clonal provenance of the piglet was indicated by her coat color and confirmed by DNA microsatellite analysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Onishi, A -- Iwamoto, M -- Akita, T -- Mikawa, S -- Takeda, K -- Awata, T -- Hanada, H -- Perry, A C -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1188-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Breeding and Genetics, National Institute of Animal Industry, Tsukuba Norin Danchi, Ibaraki-ken 305-0901, Japan. onishi@niai.affrc.go.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10947985" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Cloning, Organism/*methods ; Electric Stimulation ; Embryo Transfer ; Embryonic and Fetal Development ; Female ; Fetus/cytology ; Fibroblasts/ultrastructure ; Microinjections ; Microsatellite Repeats ; *Nuclear Transfer Techniques ; Oocytes ; Pregnancy ; *Swine/embryology/genetics
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  • 28
    Publication Date: 2001-03-27
    Description: Receptor-mediated activation of heterotrimeric GTP-binding proteins (G-proteins) was visualized in living Dictyostelium discoideum cells by monitoring fluorescence resonance energy transfer (FRET) between alpha- and beta- subunits fused to cyan and yellow fluorescent proteins. The G-protein heterotrimer rapidly dissociated and reassociated upon addition and removal of chemoattractant. During continuous stimulation, G-protein activation reached a dose-dependent steady-state level. Even though physiological responses subsided, the activation did not decline. Thus, adaptation occurs at another point in the signaling pathway, and occupied receptors, whether or not they are phosphorylated, catalyze the G-protein cycle. Construction of similar energy-transfer pairs of mammalian G-proteins should enable direct in situ mechanistic studies and applications such as drug screening and identifying ligands of newly found G-protein-coupled receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janetopoulos, C -- Jin, T -- Devreotes, P -- GM28007/GM/NIGMS NIH HHS/ -- GM34933/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 23;291(5512):2408-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins Medical Institutions, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11264536" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Bacterial Proteins ; Cyclic AMP/metabolism/*pharmacology ; Deoxyadenine Nucleotides/pharmacology ; Dictyostelium/*metabolism ; Energy Transfer ; Fluorescence ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Heterotrimeric GTP-Binding Proteins/*metabolism ; Kinetics ; Ligands ; Luminescent Proteins ; Microscopy, Fluorescence ; Phosphorylation ; Receptors, Cyclic AMP/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Spectrometry, Fluorescence ; Transformation, Genetic
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  • 29
    Publication Date: 2001-01-06
    Description: All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins. It has therefore been speculated that DExH/D proteins may also affect RNA-protein interactions. We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate-dependent fashion. NPH-II increases the rate of U1A dissociation by more than three orders of magnitude while retaining helicase processivity. This indicates that DExH/D proteins can effectively catalyze protein displacement from RNA and thereby participate in the structural reorganization of ribonucleoprotein assemblies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jankowsky, E -- Gross, C H -- Shuman, S -- Pyle, A M -- New York, N.Y. -- Science. 2001 Jan 5;291(5501):121-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11141562" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions/metabolism ; Acid Anhydride Hydrolases/chemistry/*metabolism ; Adenosine Triphosphate/metabolism ; Base Sequence ; Binding Sites ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleoside-Triphosphatase ; Protein Binding ; Protein Conformation ; RNA/chemistry/*metabolism ; RNA Helicases/chemistry/*metabolism ; *RNA-Binding Proteins ; Ribonucleoprotein, U1 Small Nuclear/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barres, B A -- Smith, S J -- New York, N.Y. -- Science. 2001 Nov 9;294(5545):1296-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University School of Medicine, Fairchild Science Building, Stanford, CA 94305-5125, USA. barres@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11701918" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apolipoproteins E/metabolism/pharmacology ; Astrocytes/*metabolism ; Brain/metabolism ; Cells, Cultured ; Cholesterol/*metabolism/pharmacology ; Coculture Techniques ; Mice ; Neuroglia/metabolism ; Neuronal Plasticity ; Neurons/metabolism/*physiology ; Recombinant Proteins/pharmacology ; Signal Transduction ; Synapses/*physiology
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  • 31
    Publication Date: 2001-07-21
    Description: The promoters of cell adhesion are ligands, which are often attached to flexible tethers that bind to surface receptors on adjacent cells. Using a combination of Monte Carlo simulations, diffusion reaction theory, and direct experiments (surface force measurements) of the biotin-streptavidin system, we have quantified polymer chain dynamics and the kinetics and spatial range of tethered ligand-receptor binding. The results show that the efficiency of strong binding does not depend solely on the molecular architecture or binding energy of the receptor-ligand pair, nor on the equilibrium configuration of the polymer tether, but rather on its "rare" extended conformations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeppesen, C -- Wong, J Y -- Kuhl, T L -- Israelachvili, J N -- Mullah, N -- Zalipsky, S -- Marques, C M -- GM-17876/GM/NIGMS NIH HHS/ -- GM-47334/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jul 20;293(5529):465-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Materials Research Laboratory, Department of Chemical Engineering, University of California, Santa Barbara, CA 93106, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11463908" target="_blank"〉PubMed〈/a〉
    Keywords: Biotin/*chemistry/metabolism ; Chemistry, Physical ; Diffusion ; Kinetics ; Ligands ; Mathematics ; Monte Carlo Method ; Physicochemical Phenomena ; Polyethylene Glycols ; Polymers/*chemistry ; Protein Conformation ; Streptavidin/*chemistry/metabolism ; Surface Properties ; Thermodynamics
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  • 32
    Publication Date: 2001-11-03
    Description: SNAREs (soluble NSF-attachment protein receptors) are generally acknowledged as central components of membrane fusion reactions, but their precise function has remained enigmatic. Competing hypotheses suggest roles for SNAREs in mediating the specificity of fusion, catalyzing fusion, or actually executing fusion. We generated knockout mice lacking synaptobrevin/VAMP 2, the vesicular SNARE protein responsible for synaptic vesicle fusion in forebrain synapses, to make use of the exquisite temporal resolution of electrophysiology in measuring fusion. In the absence of synaptobrevin 2, spontaneous synaptic vesicle fusion and fusion induced by hypertonic sucrose were decreased approximately 10-fold, but fast Ca2+-triggered fusion was decreased more than 100-fold. Thus, synaptobrevin 2 may function in catalyzing fusion reactions and stabilizing fusion intermediates but is not absolutely required for synaptic fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schoch, S -- Deak, F -- Konigstorfer, A -- Mozhayeva, M -- Sara, Y -- Sudhof, T C -- Kavalali, E T -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1117-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Basic Neuroscience, Department of Molecular Genetics, Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Dallas, TX 75390-9111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691998" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/metabolism/pharmacology ; Cells, Cultured ; Hypertonic Solutions ; *Membrane Fusion ; Membrane Proteins/genetics/*physiology ; Mice ; Mice, Knockout ; Mutation ; Patch-Clamp Techniques ; Potassium/pharmacology ; Presynaptic Terminals/physiology ; Prosencephalon/physiology ; R-SNARE Proteins ; SNARE Proteins ; Sucrose/pharmacology ; Synapses/*physiology ; Synaptic Transmission ; Synaptic Vesicles/*physiology ; *Vesicular Transport Proteins
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  • 33
    Publication Date: 2001-11-27
    Description: Adhesions between fibroblastic cells and extracellular matrix have been studied extensively in vitro, but little is known about their in vivo counterparts. Here, we characterized the composition and function of adhesions in three-dimensional (3D) matrices derived from tissues or cell culture. "3D-matrix adhesions" differ from focal and fibrillar adhesions characterized on 2D substrates in their content of alpha5beta1 and alphavbeta3 integrins, paxillin, other cytoskeletal components, and tyrosine phosphorylation of focal adhesion kinase (FAK). Relative to 2D substrates, 3D-matrix interactions also display enhanced cell biological activities and narrowed integrin usage. These distinctive in vivo 3D-matrix adhesions differ in structure, localization, and function from classically described in vitro adhesions, and as such they may be more biologically relevant to living organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cukierman, E -- Pankov, R -- Stevens, D R -- Yamada, K M -- New York, N.Y. -- Science. 2001 Nov 23;294(5547):1708-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11721053" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; *Cell Adhesion/drug effects ; Cell Culture Techniques/methods ; Cell Division ; Cell Movement ; Cell Size ; Cells, Cultured ; Culture Techniques/methods ; Cycloheximide/pharmacology ; Cytoskeletal Proteins/metabolism ; Extracellular Matrix/chemistry/metabolism ; Fibroblasts/chemistry/*cytology/*metabolism ; Fibronectins/metabolism ; Fluorescent Antibody Technique, Indirect ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Focal Adhesions/chemistry/metabolism ; Glutaral/metabolism ; Humans ; Imaging, Three-Dimensional/*methods ; Integrins/metabolism ; Mice ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Conformation ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Time Factors
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  • 34
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-04-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pellman, D -- New York, N.Y. -- Science. 2001 Mar 30;291(5513):2555-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatric Oncology, Dana-Farber Cancer Institute, and Pediatric Hematology/Oncology, Children's Hospital, Harvard Medical School, 44 Binney Street, Boston, MA 02115, USA. david_pellman@dfci.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11286276" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Aneuploidy ; Animals ; Cell Transformation, Neoplastic ; Cells, Cultured ; Chromosome Aberrations ; Chromosome Segregation ; Chromosomes/*physiology ; Colonic Neoplasms/*genetics/metabolism/pathology ; Cytoskeletal Proteins/chemistry/*metabolism ; *Genes, APC ; Humans ; Kinetochores/*metabolism ; Mice ; Microtubule-Associated Proteins/metabolism ; Microtubules/*metabolism ; Mitosis ; Mutation ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases ; Spindle Apparatus/metabolism ; Stem Cells/cytology/metabolism ; *Trans-Activators ; beta Catenin
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  • 35
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-07-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, T T -- New York, N.Y. -- Science. 2001 Jun 29;292(5526):2431-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11441877" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*drug therapy/prevention & ; control/transmission ; Anti-HIV Agents/*therapeutic use ; Drug Industry ; Female ; Health Policy ; Health Services Accessibility ; Humans ; Infant, Newborn ; Infectious Disease Transmission, Vertical/prevention & control ; Nevirapine/therapeutic use ; Pregnancy ; Pregnancy Complications, Infectious/drug therapy ; South Africa
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  • 36
    Publication Date: 2001-03-10
    Description: Filopodia that extend from neuronal growth cones sample the environment for extracellular guidance cues, but the signals they transmit to growth cones are unknown. Filopodia were observed generating localized transient elevations of intracellular calcium ([Ca2+]i) that propagate back to the growth cone and stimulate global Ca2+ elevations. The frequency of filopodial Ca2+ transients was substrate-dependent and may be due in part to influx of Ca2+ through channels activated by integrin receptors. These transients slowed neurite outgrowth by reducing filopodial motility and promoted turning when stimulated differentially within filopodia on one side of the growth cone. These rapid signals appear to serve both as autonomous regulators of filopodial movement and as frequency-coded signals integrated within the growth cone and could be a common signaling process for many motile cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gomez, T M -- Robles, E -- Poo , M -- Spitzer, N C -- New York, N.Y. -- Science. 2001 Mar 9;291(5510):1983-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Center for Molecular Genetics, University of California, San Diego, La Jolla, CA 92093, USA. tmgomez@facstaff.wisc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11239161" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD29/metabolism ; Calcium/*metabolism ; *Calcium Signaling ; Cell Movement ; Cells, Cultured ; Culture Techniques ; Embryo, Nonmammalian/cytology ; Growth Cones/metabolism/*physiology ; Integrins/metabolism ; Laminin/pharmacology ; Microscopy, Confocal ; Neurites/metabolism/*physiology ; Neurons/physiology ; Oligopeptides/pharmacology ; Pseudopodia/*metabolism ; Tenascin/pharmacology ; Xenopus/embryology
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  • 37
    Publication Date: 2001-03-17
    Description: The role of NF-kappaB-inducing kinase (NIK) in cytokine signaling remains controversial. To identify the physiologic functions of NIK, we disrupted the NIK locus by gene targeting. Although NIK-/- mice displayed abnormalities in both lymphoid tissue development and antibody responses, NIK-/- cells manifested normal NF-kappaB DNA binding activity when treated with a variety of cytokines, including tumor necrosis factor (TNF), interleukin-1 (IL-1), and lymphotoxin-beta (LTbeta). However, NIK was selectively required for gene transcription induced through ligation of LTbeta receptor but not TNF receptors. These results reveal that NIK regulates the transcriptional activity of NF-kappaB in a receptor-restricted manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yin, L -- Wu, L -- Wesche, H -- Arthur, C D -- White, J M -- Goeddel, D V -- Schreiber, R D -- New York, N.Y. -- Science. 2001 Mar 16;291(5511):2162-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Immunology, Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11251123" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; B-Lymphocytes/metabolism ; Cells, Cultured ; DNA/metabolism ; Fibroblasts/metabolism ; Gene Targeting ; Genes, Reporter ; Interleukin-1/metabolism/pharmacology ; Ligands ; Lymphoid Tissue/abnormalities ; Lymphotoxin beta Receptor ; Mice ; Mice, Inbred C57BL ; NF-kappa B/genetics/*metabolism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Receptors, Tumor Necrosis Factor/immunology/*metabolism ; Signal Transduction ; *Transcription, Genetic ; Tumor Necrosis Factor-alpha/metabolism/pharmacology
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  • 38
    Publication Date: 2001-08-18
    Description: The LKB1 tumor suppressor gene, mutated in Peutz-Jeghers syndrome, encodes a serine/threonine kinase of unknown function. Here we show that mice with a targeted disruption of Lkb1 die at midgestation, with the embryos showing neural tube defects, mesenchymal cell death, and vascular abnormalities. Extraembryonic development was also severely affected; the mutant placentas exhibited defective labyrinth layer development and the fetal vessels failed to invade the placenta. These phenotypes were associated with tissue-specific deregulation of vascular endothelial growth factor (VEGF) expression, including a marked increase in the amount of VEGF messenger RNA. Moreover, VEGF production in cultured Lkb1(-/-) fibroblasts was elevated in both normoxic and hypoxic conditions. These findings place Lkb1 in the VEGF signaling pathway and suggest that the vascular defects accompanying Lkb1 loss are mediated at least in part by VEGF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ylikorkala, A -- Rossi, D J -- Korsisaari, N -- Luukko, K -- Alitalo, K -- Henkemeyer, M -- Makela, T P -- New York, N.Y. -- Science. 2001 Aug 17;293(5533):1323-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular and Cancer Biology Program, Haartman Institute and Biomedicum Helsinki, Post Office Box 63, University of Helsinki, Helsinki 00014, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11509733" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Vessels/*abnormalities/embryology ; Cell Death ; Cell Hypoxia ; Cells, Cultured ; DNA-Binding Proteins/metabolism ; Embryo, Mammalian/*metabolism ; Embryonic and Fetal Development ; Endothelial Growth Factors/*genetics/*metabolism ; Endothelium, Vascular/abnormalities/cytology/embryology ; *Gene Expression Regulation, Developmental ; Gene Targeting ; Hypoxia-Inducible Factor 1 ; Hypoxia-Inducible Factor 1, alpha Subunit ; In Situ Hybridization ; Lymphokines/*genetics/*metabolism ; Mesoderm/cytology ; Mice ; Mice, Inbred C57BL ; Muscle, Smooth, Vascular/abnormalities/cytology/embryology ; Neural Tube Defects/embryology ; Nuclear Proteins/metabolism ; Phenotype ; Placenta/blood supply/embryology/metabolism ; Protein-Serine-Threonine Kinases/deficiency/genetics/*physiology ; RNA, Messenger/genetics/metabolism ; Signal Transduction ; *Transcription Factors ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors
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  • 39
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-09-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 2001 Sep 21;293(5538):2192-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11567120" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/metabolism/pathology/*physiopathology ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; *Apoptosis ; Brain/*metabolism/pathology ; Carrier Proteins/metabolism ; Caspases/*metabolism ; Cells, Cultured ; DNA Fragmentation ; Enzyme Activation ; Humans ; In Situ Nick-End Labeling ; JNK Mitogen-Activated Protein Kinases ; Mice ; Microfilament Proteins/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Nerve Degeneration ; Neurons/metabolism/pathology/*physiology ; Synapses/enzymology
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  • 40
    Publication Date: 2001-11-17
    Description: Proteins are transported from the endoplasmic reticulum (ER) in vesicles formed by coat protein complex II (COPII). Soluble secretory proteins are thought to leave the ER in these vesicles by "bulk flow" or through recognition by hypothetical shuttling receptors. We found that Erv29p, a conserved transmembrane protein, was directly required for packaging glycosylated pro-alpha-factor (gpalphaf) into COPII vesicles in Saccharomyces cerevisiae. Further, an Erv29p-gpalphaf complex was isolated from ER-derived transport vesicles. In vivo, export of gpalphaf from the ER was saturable and depended on the expression level of Erv29p. These results indicate that membrane receptors can link soluble cargo proteins to the COPII coat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belden, W J -- Barlowe, C -- New York, N.Y. -- Science. 2001 Nov 16;294(5546):1528-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11711675" target="_blank"〉PubMed〈/a〉
    Keywords: COP-Coated Vesicles/*metabolism ; Carboxypeptidases/metabolism ; Cathepsin A ; Cross-Linking Reagents ; Dimerization ; Endoplasmic Reticulum/*metabolism ; Glycosylation ; Golgi Apparatus/metabolism ; Kinetics ; Membrane Proteins/chemistry/genetics/isolation & purification/*metabolism ; Membrane Transport Proteins ; Peptides/chemistry/genetics/isolation & purification/*metabolism ; Precipitin Tests ; Protein Folding ; Protein Precursors/chemistry/isolation & purification/*metabolism ; Protein Transport ; Qb-SNARE Proteins ; Saccharomyces cerevisiae/genetics/*metabolism/ultrastructure ; *Saccharomyces cerevisiae Proteins ; Solubility ; Succinimides/pharmacology ; *Vesicular Transport Proteins
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davenport, R J -- New York, N.Y. -- Science. 2001 Apr 27;292(5517):620.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11330309" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; GTP-Binding Proteins/metabolism ; Genes ; Genetic Variation ; Humans ; Mice ; Receptors, Cell Surface/chemistry/*genetics/metabolism ; *Receptors, G-Protein-Coupled ; Saccharin ; Sucrose ; Taste/*genetics ; Taste Buds/*metabolism
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  • 42
    Publication Date: 2001-06-09
    Description: The p53 protein is present in low amounts in normally growing cells and is activated in response to physiological insults. MDM2 regulates p53 either through inhibiting p53's transactivating function in the nucleus or by targeting p53 degradation in the cytoplasm. We identified a previously unknown nuclear export signal (NES) in the amino terminus of p53, spanning residues 11 to 27 and containing two serine residues phosphorylated after DNA damage, which was required for p53 nuclear export in colloboration with the carboxyl-terminal NES. Serine-15-phosphorylated p53 induced by ultraviolet irradiation was not exported. Thus, DNA damage-induced phosphorylation may achieve optimal p53 activation by inhibiting both MDM2 binding to, and the nuclear export of, p53.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Y -- Xiong, Y -- CA65572/CA/NCI NIH HHS/ -- K01 CA087580/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 8;292(5523):1910-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, and Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, NC 27599-7295, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11397945" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amino Acid Sequence ; Animals ; Cell Fusion ; Cell Line ; Cell Nucleus/*metabolism ; Cells, Cultured ; Cytoplasm/metabolism ; *DNA Damage ; Mice ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Phosphorylation ; Phosphoserine/metabolism ; *Protein Sorting Signals ; Protein Structure, Tertiary ; Proteins/genetics/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Recombinant Fusion Proteins/metabolism ; Transfection ; Tumor Suppressor Protein p14ARF ; Tumor Suppressor Protein p53/*chemistry/genetics/*metabolism ; Ubiquitins/metabolism ; Ultraviolet Rays
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  • 43
    Publication Date: 2001-11-03
    Description: The mechanisms controlling neural stem cell proliferation are poorly understood. Here we demonstrate that the PTEN tumor suppressor plays an important role in regulating neural stem/progenitor cells in vivo and in vitro. Mice lacking PTEN exhibited enlarged, histoarchitecturally abnormal brains, which resulted from increased cell proliferation, decreased cell death, and enlarged cell size. Neurosphere cultures revealed a greater proliferation capacity for tripotent Pten-/- central nervous system stem/progenitor cells, which can be attributed, at least in part, to a shortened cell cycle. However, cell fate commitments of the progenitors were largely undisturbed. Our results suggest that PTEN negatively regulates neural stem cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Groszer, M -- Erickson, R -- Scripture-Adams, D D -- Lesche, R -- Trumpp, A -- Zack, J A -- Kornblum, H I -- Liu, X -- Wu, H -- MH062800-01/MH/NIMH NIH HHS/ -- NS38489/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 7;294(5549):2186-9. Epub 2001 Nov 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular and Medical Pharmacology, 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/11691952" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Astrocytes/cytology ; Brain/abnormalities/*cytology/embryology ; Cell Count ; Cell Differentiation ; *Cell Division ; Cell Lineage ; Cell Size ; Cells, Cultured ; Female ; Flow Cytometry ; Fluoresceins/metabolism ; Gene Deletion ; Intermediate Filament Proteins/metabolism ; Male ; Mice ; Mice, Knockout ; *Nerve Tissue Proteins ; Nestin ; Neurons/*cytology ; PTEN Phosphohydrolase ; Phosphoric Monoester Hydrolases/*genetics/*physiology ; Stem Cells/*cytology ; Succinimides/metabolism ; Tumor Suppressor Proteins/*genetics/*physiology
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  • 44
    Publication Date: 2001-04-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berkhout, B -- Das, A T -- Beerens, N -- New York, N.Y. -- Science. 2001 Apr 6;292(5514):7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Retrovirology, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11292864" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; Genes, vpr ; Genome, Viral ; HIV-1/*genetics ; Humans ; *Mutation ; Proviruses/genetics ; *RNA Editing ; *Transcription, Genetic
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berendsen, H J -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2304-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands. berendsen@chem.rug.nl〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743188" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Aquaporin 1 ; Aquaporins/chemistry/*metabolism ; Bacterial Outer Membrane Proteins/chemistry/*metabolism ; Cell Membrane Permeability ; *Computational Biology ; *Computer Simulation ; *Escherichia coli Proteins ; Hydrogen Bonding ; Kinetics ; Lipid Bilayers ; *Models, Biological ; Permeability ; Static Electricity ; Time Factors ; Water/*metabolism
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  • 46
    Publication Date: 2001-03-27
    Description: Many intracellular pathogens infect a broad range of host tissues, but the importance of T cells for immunity in these sites is unclear because most of our understanding of antimicrobial T cell responses comes from analyses of lymphoid tissue. Here, we show that in response to viral or bacterial infection, antigen-specific CD8 T cells migrated to nonlymphoid tissues and were present as long-lived memory cells. Strikingly, CD8 memory T cells isolated from nonlymphoid tissues exhibited effector levels of lytic activity directly ex vivo, in contrast to their splenic counterparts. These results point to the existence of a population of extralymphoid effector memory T cells poised for immediate response to infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masopust, D -- Vezys, V -- Marzo, A L -- Lefrancois, L -- AI41576/AI/NIAID NIH HHS/ -- DK45260/DK/NIDDK NIH HHS/ -- T32-AI07080/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 23;291(5512):2413-7. Epub 2001 Mar 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Immunology, Department of Medicine, University of Connecticut Health Center, Farmington, CT 06030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11264538" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CD8-Positive T-Lymphocytes/*immunology ; Cell Movement ; Cells, Cultured ; Flow Cytometry ; H-2 Antigens/immunology ; *Immunologic Memory ; Intestine, Small/immunology ; Listeria monocytogenes/genetics/immunology ; Listeriosis/*immunology ; Liver/immunology ; Lung/immunology ; Lymphocyte Activation ; Lymphoid Tissue/immunology ; Mice ; Mice, Inbred C57BL ; Ovalbumin/immunology ; Phenotype ; Rhabdoviridae Infections/*immunology ; T-Lymphocyte Subsets/*immunology ; Vesicular stomatitis Indiana virus/immunology
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  • 47
    Publication Date: 2001-06-16
    Description: Huntingtin is a 350-kilodalton protein of unknown function that is mutated in Huntington's disease (HD), a neurodegenerative disorder. The mutant protein is presumed to acquire a toxic gain of function that is detrimental to striatal neurons in the brain. However, loss of a beneficial activity of wild-type huntingtin may also cause the death of striatal neurons. Here we demonstrate that wild-type huntingtin up-regulates transcription of brain-derived neurotrophic factor (BDNF), a pro-survival factor produced by cortical neurons that is necessary for survival of striatal neurons in the brain. We show that this beneficial activity of huntingtin is lost when the protein becomes mutated, resulting in decreased production of cortical BDNF. This leads to insufficient neurotrophic support for striatal neurons, which then die. Restoring wild-type huntingtin activity and increasing BDNF production may be therapeutic approaches for treating HD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zuccato, C -- Ciammola, A -- Rigamonti, D -- Leavitt, B R -- Goffredo, D -- Conti, L -- MacDonald, M E -- Friedlander, R M -- Silani, V -- Hayden, M R -- Timmusk, T -- Sipione, S -- Cattaneo, E -- E.0840/Telethon/Italy -- New York, N.Y. -- Science. 2001 Jul 20;293(5529):493-8. Epub 2001 Jun 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacological Sciences, University of Milano, Via Balzaretti 9, 20133 Milano, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11408619" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Apoptosis ; Brain-Derived Neurotrophic Factor/biosynthesis/*genetics/metabolism ; Cell Survival ; Cells, Cultured ; Cerebral Cortex/cytology/*metabolism ; Corpus Striatum/cytology/*metabolism/pathology ; Exons ; Hippocampus/cytology/metabolism/pathology ; Humans ; Huntington Disease/*genetics/metabolism/pathology ; Mice ; Mice, Transgenic ; Mutation ; Nerve Degeneration ; Nerve Growth Factors/genetics/metabolism ; Nerve Tissue Proteins/genetics/*physiology ; Neurons/*metabolism/pathology ; Nuclear Proteins/genetics/*physiology ; Promoter Regions, Genetic ; Transcription, Genetic ; Transfection
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-03-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 2001 Feb 16;291(5507):1177-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11233420" target="_blank"〉PubMed〈/a〉
    Keywords: Chromosomes, Human ; Computational Biology ; CpG Islands ; DNA Transposable Elements ; DNA, Intergenic ; Databases, Factual ; Exons ; Expressed Sequence Tags ; Gene Duplication ; Genes ; *Genome, Human ; *Human Genome Project ; Humans ; Internet ; Polymorphism, Single Nucleotide ; Proteins/chemistry/genetics ; Repetitive Sequences, Nucleic Acid ; *Sequence Analysis, DNA ; Software
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  • 49
    Publication Date: 2001-09-05
    Description: The developmental signaling functions of cell surface heparan sulfate proteoglycans (HSPGs) are dependent on their sulfation states. Here, we report the identification of QSulf1, the avian ortholog of an evolutionarily conserved protein family related to heparan-specific N-acetyl glucosamine sulfatases. QSulf1 expression is induced by Sonic hedgehog in myogenic somite progenitors in quail embryos and is required for the activation of MyoD, a Wnt-induced regulator of muscle specification. QSulf1 is localized on the cell surface and regulates heparan-dependent Wnt signaling in C2C12 myogenic progenitor cells through a mechanism that requires its catalytic activity, providing evidence that QSulf1 regulates Wnt signaling through desulfation of cell surface HSPGs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dhoot, G K -- Gustafsson, M K -- Ai, X -- Sun, W -- Standiford, D M -- Emerson , C P Jr -- New York, N.Y. -- Science. 2001 Aug 31;293(5535):1663-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Veterinary Sciences, The Royal Veterinary College, University of London, Royal College Street, London NW1 OTU, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11533491" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Body Patterning ; CHO Cells ; Cell Membrane/metabolism ; Cells, Cultured ; Cloning, Molecular ; Coculture Techniques ; Cricetinae ; Embryo, Nonmammalian/metabolism ; Embryonic Development ; Hedgehog Proteins ; Heparan Sulfate Proteoglycans/*metabolism ; Heparin/metabolism/pharmacology ; Heparitin Sulfate/metabolism ; Molecular Sequence Data ; Muscles/cytology/*embryology/metabolism ; Mutation ; MyoD Protein/genetics/metabolism ; Oligonucleotides, Antisense ; Proto-Oncogene Proteins/*metabolism ; Quail/*embryology ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; *Signal Transduction ; Somites/metabolism ; Stem Cells/*metabolism ; Sulfatases/chemistry/genetics/*metabolism ; Trans-Activators/genetics/metabolism ; Transfection ; Wnt Proteins ; *Zebrafish Proteins
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  • 50
    Publication Date: 2001-02-07
    Description: The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals. These proteins maintain intracellular redox homeostasis to protect the organism from oxidative damage. Here we demonstrate the absence of glutathione reductase in Drosophila melanogaster, identify a new type of thioredoxin reductase, and provide evidence that a thioredoxin system supports GSSG reduction. Our data suggest that antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kanzok, S M -- Fechner, A -- Bauer, H -- Ulschmid, J K -- Muller, H M -- Botella-Munoz, J -- Schneuwly, S -- Schirmer, R -- Becker, K -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):643-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center of Biochemistry, Im Neuenheimer Feld 328, Heidelberg University, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158675" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Binding Sites ; Drosophila melanogaster/*enzymology/genetics/metabolism ; Genes, Insect ; Glutathione/*metabolism ; Glutathione Disulfide/metabolism ; Glutathione Reductase/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Mutation ; NADP/metabolism ; Oxidation-Reduction ; Sequence Alignment ; Species Specificity ; Substrate Specificity ; Thioredoxin-Disulfide Reductase/antagonists & ; inhibitors/chemistry/*genetics/*metabolism
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  • 51
    Publication Date: 2001-02-07
    Description: Although astrocytes constitute nearly half of the cells in our brain, their function is a long-standing neurobiological mystery. Here we show by quantal analyses, FM1-43 imaging, immunostaining, and electron microscopy that few synapses form in the absence of glial cells and that the few synapses that do form are functionally immature. Astrocytes increase the number of mature, functional synapses on central nervous system (CNS) neurons by sevenfold and are required for synaptic maintenance in vitro. We also show that most synapses are generated concurrently with the development of glia in vivo. These data demonstrate a previously unknown function for glia in inducing and stabilizing CNS synapses, show that CNS synapse number can be profoundly regulated by nonneuronal signals, and raise the possibility that glia may actively participate in synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ullian, E M -- Sapperstein, S K -- Christopherson, K S -- Barres, B A -- NS10784/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stanford University School of Medicine, Department of Neurobiology, Fairchild Science Building, Stanford, CA 94305-5125, USA. emu@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158678" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Astrocytes/*physiology ; Calcium/metabolism ; *Calcium-Binding Proteins ; Cell Communication ; Cells, Cultured ; Coculture Techniques ; Excitatory Postsynaptic Potentials ; Fluorescent Dyes/metabolism ; Glutamic Acid/pharmacology ; Ionomycin/pharmacology ; Membrane Glycoproteins/metabolism ; Microscopy, Electron ; Nerve Tissue Proteins/metabolism ; Neuronal Plasticity ; Patch-Clamp Techniques ; Pyridinium Compounds/metabolism ; Quaternary Ammonium Compounds/metabolism ; Rats ; Rats, Sprague-Dawley ; Retinal Ganglion Cells/*physiology/ultrastructure ; Superior Colliculi/embryology/growth & development/ultrastructure ; Synapses/*physiology/ultrastructure ; Synaptic Transmission ; Synaptic Vesicles/metabolism ; Synaptophysin/metabolism ; Synaptotagmins
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  • 52
    Publication Date: 2001-11-03
    Description: The bacterial macrolide rapamycin is an efficacious anticancer agent against solid tumors. In a hypoxic environment, the increase in mass of solid tumors is dependent on the recruitment of mitogens and nutrients. When nutrient concentrations change, particularly those of essential amino acids, the mammalian Target of Rapamycin (mTOR) functions in regulatory pathways that control ribosome biogenesis and cell growth. In bacteria, ribosome biogenesis is independently regulated by amino acids and adenosine triphosphate (ATP). Here we demonstrate that the mTOR pathway is influenced by the intracellular concentration of ATP, independent of the abundance of amino acids, and that mTOR itself is an ATP sensor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dennis, P B -- Jaeschke, A -- Saitoh, M -- Fowler, B -- Kozma, S C -- Thomas, G -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691993" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Adenosine Triphosphate/*metabolism ; Amino Acids/metabolism ; Androstadienes/pharmacology ; Carrier Proteins/metabolism ; Cell Line ; Deoxyglucose/pharmacology ; Enzyme Activation ; Homeostasis ; Humans ; Insulin/pharmacology ; Kinetics ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Recombinant Fusion Proteins/metabolism ; Ribosomal Protein S6 Kinases/antagonists & inhibitors/metabolism ; Ribosomes/metabolism ; Rotenone/pharmacology ; Signal Transduction ; Sirolimus/pharmacology ; TOR Serine-Threonine Kinases
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  • 53
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Enserink, M -- New York, N.Y. -- Science. 2001 Jan 5;291(5501):24-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11191991" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Artifacts ; Cell Membrane/parasitology/ultrastructure ; Cell Movement ; Cells, Cultured ; Hepatocytes/*parasitology/ultrastructure ; Humans ; Malaria/parasitology ; Mice ; Motion Pictures as Topic ; Plasmodium yoelii/growth & development/*physiology ; Vacuoles/physiology/ultrastructure
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez, J M -- Chu, S -- Oberhauser, A F -- New York, N.Y. -- Science. 2001 Apr 27;292(5517):653-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Mayo Foundation, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11330326" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Elasticity ; Ion Channels/chemistry ; Kinetics ; *Nucleic Acid Conformation ; Physicochemical Phenomena ; RNA/*chemistry ; RNA Stability ; RNA, Catalytic/*chemistry ; Stress, Mechanical ; Thermodynamics
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  • 55
    Publication Date: 2001-12-01
    Description: The first step in processing olfactory information, before neural filtering, is the physical capture of odor molecules from the surrounding fluid. Many animals capture odors from turbulent water currents or wind using antennae that bear chemosensory hairs. We used planar laser-induced fluorescence to reveal how lobster olfactory antennules hydrodynamically alter the spatiotemporal patterns of concentration in turbulent odor plumes. As antennules flick, water penetrates their chemosensory hair array during the fast downstroke, carrying fine-scale patterns of concentration into the receptor area. This spatial pattern, blurred by flow along the antennule during the downstroke, is retained during the slower return stroke and is not shed until the next flick.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koehl, M A -- Koseff, J R -- Crimaldi, J P -- McCay, M G -- Cooper, T -- Wiley, M B -- Moore, P A -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1948-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrative Biology, University of California, Berkeley, CA 94720-3140, USA. cnidaria@socrates.berkeley.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729325" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chemoreceptor Cells/physiology ; Fluorescence ; Kinetics ; Lasers ; Nephropidae/*physiology ; *Odors ; Smell/physiology ; *Water Movements
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  • 56
    Publication Date: 2001-02-24
    Description: Transgenic rhesus monkeys carrying the green fluorescent protein (GFP) gene were produced by injecting pseudotyped replication-defective retroviral vector into the perivitelline space of 224 mature rhesus oocytes, later fertilized by intracytoplasmic sperm injection. Of the three males born from 20 embryo transfers, one was transgenic when accessible tissues were assayed for transgene DNA and messenger RNA. All tissues that were studied from a fraternal set of twins, miscarried at 73 days, carried the transgene, as confirmed by Southern analyses, and the GFP transgene reporter was detected by both direct and indirect fluorescence imaging.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A W -- Chong, K Y -- Martinovich, C -- Simerly, C -- Schatten, G -- New York, N.Y. -- Science. 2001 Jan 12;291(5502):309-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oregon Regional Primate Research Center, Center for Women's Health, and Departments of Cell-Developmental Biology and Obstetrics-Gynecology, Oregon Health Sciences University, 505 NW 185th Avenue, Beaverton, OR 97006, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11209082" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Genetically Modified ; Animals, Newborn ; Blotting, Southern ; Embryo Transfer ; Embryonic and Fetal Development ; Female ; Fluorescent Antibody Technique ; Gene Expression ; *Gene Transfer Techniques ; *Gene Transfer, Horizontal ; Genetic Vectors ; Green Fluorescent Proteins ; Luminescent Proteins/*genetics ; Macaca mulatta/*genetics ; Male ; Moloney murine leukemia virus/genetics ; Oocytes ; Polymerase Chain Reaction ; Pregnancy ; Pregnancy Outcome ; Sperm Injections, Intracytoplasmic ; Transgenes
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  • 57
    Publication Date: 2001-11-03
    Description: In the exocytosis of neurotransmitter, fusion pore opening represents the first instant of fluid contact between the vesicle lumen and extracellular space. The existence of the fusion pore has been established by electrical measurements, but its molecular composition is unknown. The possibility that synaptotagmin regulates fusion pores was investigated with amperometry to monitor exocytosis of single dense-core vesicles. Overexpression of synaptotagmin I prolonged the time from fusion pore opening to dilation, whereas synaptotagmin IV shortened this time. Both synaptotagmin isoforms reduced norepinephrine flux through open fusion pores. Thus, synaptotagmin interacts with fusion pores, possibly by associating with a core complex of membrane proteins and/or lipid.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, C T -- Grishanin, R -- Earles, C A -- Chang, P Y -- Martin, T F -- Chapman, E R -- Jackson, M B -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1111-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Wisconsin Medical School, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691996" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Channels, P-Type/metabolism ; Calcium Channels, Q-Type/metabolism ; *Calcium-Binding Proteins ; Cell Membrane Structures/*metabolism ; Chromogranins/metabolism ; Electrophysiology ; *Exocytosis ; Kinetics ; *Membrane Fusion ; Membrane Glycoproteins/*metabolism ; Membrane Potentials ; Nerve Tissue Proteins/*metabolism ; Neurotransmitter Agents/*metabolism ; Norepinephrine/metabolism ; PC12 Cells ; Protein Isoforms ; Rats ; Recombinant Fusion Proteins/metabolism ; Secretory Vesicles/*metabolism ; Synaptic Transmission ; Synaptic Vesicles/metabolism ; Synaptotagmin I ; Synaptotagmins
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  • 58
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-05-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finkel, E -- New York, N.Y. -- Science. 2001 Apr 27;292(5517):624-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11330312" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis/*physiology ; Caenorhabditis elegans/physiology ; Caspase Inhibitors ; Caspases/*metabolism ; Cell Nucleus/metabolism ; Cells, Cultured ; Cysteine Proteinase Inhibitors/pharmacology ; Cytochrome c Group/metabolism ; Enzyme Activation ; Humans ; Intracellular Membranes/physiology ; Mice ; Mice, Knockout ; Mitochondria/*physiology ; Nuclear Proteins/metabolism ; Permeability ; Proteins/metabolism
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  • 59
    Publication Date: 2001-09-15
    Description: Infections with Plasmodium falciparum during pregnancy lead to the accumulation of parasitized red blood cells (infected erythrocytes, IEs) in the placenta. IEs of P. falciparum isolates that infect the human placenta were found to bind immunoglobulin G (IgG). A strain of P. falciparum cloned for IgG binding adhered massively to placental syncytiotrophoblasts in a pattern similar to that of natural infections. Adherence was inhibited by IgG-binding proteins, but not by glycosaminoglycans or enzymatic digestion of chondroitin sulfate A or hyaluronic acid. Normal, nonimmune IgG that is bound to a duffy binding-like domain beta of the P. falciparum erythrocyte membrane protein 1 (PfEMP1) might at the IE surface act as a bridge to neonatal Fc receptors of the placenta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flick, K -- Scholander, C -- Chen, Q -- Fernandez, V -- Pouvelle, B -- Gysin, J -- Wahlgren, M -- New York, N.Y. -- Science. 2001 Sep 14;293(5537):2098-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbiology and Tumor Biology Center (MTC), Karolinska Institutet and Swedish Institute for Infectious Disease Control, Box 280, S-171 77 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11557894" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Adhesion ; Chondroitin ABC Lyase/metabolism ; Chondroitin Sulfates/metabolism/pharmacology ; Cloning, Molecular ; Erythrocytes/metabolism/*parasitology ; Female ; Humans ; Hyaluronic Acid/pharmacology ; Hyaluronoglucosaminidase/metabolism ; Immunoglobulin G/immunology/*metabolism ; Malaria, Falciparum/immunology/*parasitology ; Placenta/blood supply/immunology/*parasitology ; Placenta Diseases/immunology/parasitology ; Plasmodium falciparum/genetics/immunology/metabolism ; Pregnancy ; Pregnancy Complications, Parasitic/immunology/*parasitology ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry/immunology/*metabolism ; Receptors, Fc/*metabolism ; Recombinant Fusion Proteins ; Staphylococcal Protein A/metabolism/pharmacology ; Trophoblasts/immunology/parasitology
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  • 60
    Publication Date: 2001-09-08
    Description: Recently we reported that antibodies can generate hydrogen peroxide (H2O2) from singlet molecular oxygen (1O2*). We now show that this process is catalytic, and we identify the electron source for a quasi-unlimited generation of H2O2. Antibodies produce up to 500 mole equivalents of H2O2 from 1O2*, without a reduction in rate, and we have excluded metals or Cl- as the electron source. On the basis of isotope incorporation experiments and kinetic data, we propose that antibodies use H2O as an electron source, facilitating its addition to 1O2* to form H2O3 as the first intermediate in a reaction cascade that eventually leads to H2O2. X-ray crystallographic studies with xenon point to putative conserved oxygen binding sites within the antibody fold where this chemistry could be initiated. Our findings suggest a protective function of immunoglobulins against 1O2* and raise the question of whether the need to detoxify 1O2* has played a decisive role in the evolution of the immunoglobulin fold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wentworth , P Jr -- Jones, L H -- Wentworth, A D -- Zhu, X -- Larsen, N A -- Wilson, I A -- Xu, X -- Goddard , W A 3rd -- Janda, K D -- Eschenmoser, A -- Lerner, R A -- CA27489/CA/NCI NIH HHS/ -- GM43858/GM/NIGMS NIH HHS/ -- HD 36385/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1806-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, 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/11546867" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Catalytic/chemistry/*metabolism ; Binding Sites ; Catalysis ; Conserved Sequence ; Crystallography, X-Ray ; Humans ; Hydrogen Peroxide/*metabolism ; Kinetics ; Models, Molecular ; Oxidants/chemistry/*metabolism ; Oxidation-Reduction ; Oxygen/*metabolism ; Protein Conformation ; Singlet Oxygen ; Spectrometry, Mass, Electrospray Ionization ; Thermodynamics ; Tryptophan/metabolism ; Ultraviolet Rays ; Water/*chemistry/*metabolism ; Xenon/metabolism
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-11-03
    Description: Highly orchestrated molecular rearrangements are required for two membranes to fuse, as happens, for example, during neurotransmitter release into the synapse. In an elegant Perspective, Scales et al. discuss two studies (Schoch et al., Wang et al.) that shed new light on the protein interactions involved in membrane fusion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scales, S J -- Finley, M F -- Scheller, R H -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1015-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genentech Inc., South San Francisco, CA 94080, USA. sscales@gene.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691976" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Calcium Signaling ; *Calcium-Binding Proteins ; Catecholamines/metabolism ; Cell Membrane/metabolism ; Cells, Cultured ; Electrophysiology ; *Membrane Fusion ; Membrane Glycoproteins/*physiology ; Membrane Proteins/*physiology ; Mice ; Nerve Tissue Proteins/*physiology ; Neurotransmitter Agents/metabolism ; PC12 Cells ; Phospholipids/metabolism ; Protein Isoforms ; R-SNARE Proteins ; Rats ; SNARE Proteins ; Secretory Vesicles/*metabolism ; Synapses/physiology ; Synaptic Transmission ; Synaptic Vesicles/*metabolism ; Synaptotagmins ; *Vesicular Transport Proteins
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  • 62
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garelik, Glenn -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1702-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459565" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; DNA/genetics ; Developed Countries ; Developing Countries ; Drug Resistance, Microbial ; Fungicides, Industrial ; Genes ; Genes, Plant ; Genetic Engineering ; Genome ; Mutation ; *Phytophthora/genetics/pathogenicity/physiology ; *Plant Diseases ; Sequence Analysis, DNA ; Solanum tuberosum/genetics/*microbiology ; Spores/physiology ; Virulence/genetics
    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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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-03
    Description: The gastric pathogen Helicobacter pylori is known to be able to use molecular hydrogen as a respiratory substrate when grown in the laboratory. We found that hydrogen is available in the gastric mucosa of mice and that its use greatly increased the stomach colonization by H. pylori. Hydrogenase activity in H. pylori is constitutive but increased fivefold upon incubation with hydrogen. Hydrogen concentrations measured in the stomachs of live mice were found to be 10 to 50 times as high as the H. pylori affinity for hydrogen. A hydrogenase mutant strain is much less efficient in its colonization of mice. Therefore, hydrogen present in animals as a consequence of normal colonic flora is an energy-yielding substrate that can facilitate the maintenance of a pathogenic bacterium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, Jonathan W -- Maier, Robert J -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1788-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Georgia, Athens, GA 30602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459589" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catechol 2,3-Dioxygenase ; Colon/metabolism/microbiology ; *Dioxygenases ; Energy Metabolism ; Fermentation ; Gastric Mucosa/*metabolism/*microbiology ; Gene Expression Regulation, Bacterial ; Genes, Reporter ; Helicobacter pylori/growth & development/*metabolism ; Hydrogen/*metabolism ; Hydrogenase/genetics/*metabolism ; Kinetics ; Mice ; Mutation ; Oxidation-Reduction ; Oxygenases/genetics/metabolism ; Transcription, Genetic
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  • 64
    Publication Date: 2001-07-07
    Description: Cloning by nuclear transfer (NT) is an inefficient process in which most clones die before birth and survivors often display growth abnormalities. In an effort to correlate gene expression with survival and fetal overgrowth, we have examined imprinted gene expression in both mice cloned by nuclear transfer and in the embryonic stem (ES) cell donor populations from which they were derived. The epigenetic state of the ES cell genome was found to be extremely unstable. Similarly, variation in imprinted gene expression was observed in most cloned mice, even in those derived from ES cells of the same subclone. Many of the animals survived to adulthood despite widespread gene dysregulation, indicating that mammalian development may be rather tolerant to epigenetic aberrations of the genome. These data imply that even apparently normal cloned animals may have subtle abnormalities in gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Humpherys, D -- Eggan, K -- Akutsu, H -- Hochedlinger, K -- Rideout , W M 3rd -- Biniszkiewicz, D -- Yanagimachi, R -- Jaenisch, R -- 5-R35-CA44339/CA/NCI NIH HHS/ -- R01-CA84198/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jul 6;293(5527):95-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, 9 Cambridge Center, Cambridge MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11441181" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Birth Weight ; Cell Nucleus/*genetics ; Cesarean Section ; *Cloning, Organism/methods ; Congenital Abnormalities/genetics ; DNA Methylation ; Embryo Loss/genetics ; Embryo Transfer ; Embryo, Mammalian/*cytology/metabolism ; Female ; Fetal Death/genetics ; *Gene Expression Regulation, Developmental ; Gene Silencing ; Genomic Imprinting/*genetics ; Mice ; Oocytes/metabolism ; Placenta/metabolism ; Placentation ; Polyploidy ; Pregnancy ; RNA, Messenger/genetics/metabolism ; Respiration ; Stem Cells/*cytology/*metabolism ; Survival Rate
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  • 65
    Publication Date: 2001-04-21
    Description: As growing retinotectal axons navigate from the eye to the tectum, they sense guidance molecules distributed along the optic pathway. Mutations in the zebrafish astray gene severely disrupt retinal axon guidance, causing anterior-posterior pathfinding defects, excessive midline crossing, and defasciculation of the retinal projection. Eye transplantation experiments show that astray function is required in the eye. We identify astray as zebrafish robo2, a member of the Roundabout family of axon guidance receptors. Retinal ganglion cells express robo2 as they extend axons. Thus, robo2 is required for multiple axon guidance decisions during establishment of the vertebrate visual projection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fricke, C -- Lee, J S -- Geiger-Rudolph, S -- Bonhoeffer, F -- Chien, C B -- R01-EY12873/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2001 Apr 20;292(5516):507-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Anatomy, University of Utah Medical Center, 50 North Medical Drive, Salt Lake City, UT 84132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11313496" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Axons/*physiology ; Body Patterning ; Chromosome Mapping ; Crosses, Genetic ; Eye/embryology/transplantation ; Female ; Gene Expression Regulation, Developmental ; Genes ; In Situ Hybridization ; Male ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Phenotype ; Receptors, Immunologic/*genetics/*physiology ; Retina/embryology/metabolism ; Retinal Ganglion Cells/metabolism/*physiology ; Superior Colliculi/cytology/*embryology ; Visual Pathways/embryology ; Zebrafish/embryology/genetics ; Zebrafish Proteins
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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-06-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, Jennifer -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2167-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077397" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Birth Weight ; Diabetes Mellitus, Type 2/epidemiology/etiology/physiopathology ; Diet ; *Disease Susceptibility ; Embryo Implantation ; Embryonic and Fetal Development ; Female ; Heart Diseases/epidemiology/etiology/physiopathology ; Humans ; Hydrocortisone/metabolism ; Hypertension/epidemiology/etiology/physiopathology ; *Infant, Low Birth Weight ; Infant, Newborn ; Placenta/physiology ; Pregnancy ; Pregnancy Complications/physiopathology ; *Prenatal Exposure Delayed Effects ; Risk Factors ; Stress, Physiological/physiopathology
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  • 67
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ivell, Richard -- New York, N.Y. -- Science. 2002 Jan 25;295(5555):637-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Hormone and Fertility Research, University of Hamburg, Grandweg 64, 22529 Hamburg, Germany. ivell@ihf.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11809958" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cyclic AMP/metabolism ; Endometrium/metabolism ; Endothelial Growth Factors/metabolism ; Female ; Humans ; Insulin ; Leydig Cells/metabolism ; Lymphokines/metabolism ; Male ; *Membrane Proteins ; Neovascularization, Physiologic ; Ovary/metabolism ; Pregnancy ; Proteins/chemistry/physiology ; Receptors, Cell Surface/chemistry/*physiology ; *Receptors, G-Protein-Coupled ; Receptors, Peptide/chemistry/*physiology ; Relaxin/blood/*physiology ; Reproduction ; Signal Transduction ; Testis/physiology ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors ; Vasodilation
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  • 68
    Publication Date: 2002-05-11
    Description: Aneuploidy (trisomy or monosomy) is the leading genetic cause of pregnancy loss in humans and results from errors in meiotic chromosome segregation. Here, we show that the absence of synaptonemal complex protein 3 (SCP3) promotes aneuploidy in murine oocytes by inducing defective meiotic chromosome segregation. The abnormal oocyte karyotype is inherited by embryos, which die in utero at an early stage of development. In addition, embryo death in SCP3-deficient females increases with advancing maternal age. We found that SCP3 is required for chiasmata formation and for the structural integrity of meiotic chromosomes, suggesting that altered chromosomal structure triggers nondisjunction. SCP3 is thus linked to inherited aneuploidy in female germ cells and provides a model system for studying age-dependent degeneration in oocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuan, Li -- Liu, Jian-Guo -- Hoja, Mary-Rose -- Wilbertz, Johannes -- Nordqvist, Katarina -- Hoog, Christer -- New York, N.Y. -- Science. 2002 May 10;296(5570):1115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Genomics and Bioinformatics and Department of Cell and Molecular Biology, Karolinska Institutet, SE-171 77 Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004129" target="_blank"〉PubMed〈/a〉
    Keywords: *Aneuploidy ; Animals ; Chromosome Segregation ; Chromosomes/*physiology/ultrastructure ; Crossing Over, Genetic ; *Embryo Loss ; Female ; Karyotyping ; Litter Size ; Male ; Maternal Age ; *Meiosis ; Mice ; Mice, Inbred C57BL ; Mutation ; Nondisjunction, Genetic ; Nuclear Proteins/genetics/*physiology ; Oocytes/*physiology ; Pregnancy ; Recombination, Genetic ; Synaptonemal Complex/physiology/ultrastructure
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  • 69
    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
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  • 70
    Publication Date: 2002-09-14
    Description: We report a photoactivatable variant of the Aequorea victoria green fluorescent protein (GFP) that, after intense irradiation with 413-nanometer light, increases fluorescence 100 times when excited by 488-nanometer light and remains stable for days under aerobic conditions. These characteristics offer a new tool for exploring intracellular protein dynamics by tracking photoactivated molecules that are the only visible GFPs in the cell. Here, we use the photoactivatable GFP both as a free protein to measure protein diffusion across the nuclear envelope and as a chimera with a lysosomal membrane protein to demonstrate rapid interlysosomal membrane exchange.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Patterson, George H -- Lippincott-Schwartz, Jennifer -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1873-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228718" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Amino Acid Substitution ; Antigens, CD/metabolism ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; *Fluorescence ; Green Fluorescent Proteins ; Intracellular Membranes/metabolism ; Kinetics ; *Light ; Luminescent Proteins/*chemistry/genetics/isolation & purification/*metabolism ; Lysosome-Associated Membrane Glycoproteins ; Lysosomes/*metabolism ; Membrane Glycoproteins/metabolism ; Nuclear Envelope/metabolism ; Protein Engineering ; Protein Transport ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Spectrometry, Fluorescence
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  • 71
    Publication Date: 2002-09-28
    Description: It has been known since 1986 that CD8 T lymphocytes from certain HIV-1-infected individuals who are immunologically stable secrete a soluble factor, termed CAF, that suppresses HIV-1 replication. However, the identity of CAF remained elusive despite an extensive search. By means of a protein-chip technology, we identified a cluster of proteins that were secreted when CD8 T cells from long-term nonprogressors with HIV-1 infection were stimulated. These proteins were identified as alpha-defensin 1, 2, and 3 on the basis of specific antibody recognition and amino acid sequencing. CAF activity was eliminated or neutralized by an antibody specific for human alpha-defensins. Synthetic and purified preparations of alpha-defensins also inhibited the replication of HIV-1 isolates in vitro. Taken together, our results indicate that alpha-defensin 1, 2, and 3 collectively account for much of the anti-HIV-1 activity of CAF that is not attributable to beta-chemokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Linqi -- Yu, Wenjie -- He, Tian -- Yu, Jian -- Caffrey, Rebecca E -- Dalmasso, Enrique A -- Fu, Siyu -- Pham, Thang -- Mei, Jianfeng -- Ho, Jaclyn J -- Zhang, Wenyong -- Lopez, Peter -- Ho, David D -- AI-42848/AI/NIAID NIH HHS/ -- M01-RR00102/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):995-1000. Epub 2002 Sep 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Aaron Diamond AIDS Research Center, The Rockefeller University, 455 First Avenue, New York, NY 10016, USA. lzhang@adarc.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12351674" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Antiviral Agents/chemistry/isolation & purification/*pharmacology ; CD8-Positive T-Lymphocytes/chemistry/*immunology ; Cells, Cultured ; Chemokines, CC/immunology/physiology ; HIV Infections/*immunology/virology ; HIV Long-Term Survivors ; HIV-1/drug effects/*physiology ; Humans ; Mass Spectrometry ; Molecular Sequence Data ; Neutrophils/chemistry/immunology ; Protein Array Analysis ; Virus Replication ; alpha-Defensins/chemistry/isolation & purification/pharmacology/*physiology
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  • 72
    Publication Date: 2002-05-23
    Description: Mechanical and thermal cues stimulate a specialized group of sensory neurons that terminate in the skin. Three members of the transient receptor potential (TRP) family of channels are expressed in subsets of these neurons and are activated at distinct physiological temperatures. Here, we describe the cloning and characterization of a novel thermosensitive TRP channel. TRPV3 has a unique threshold: It is activated at innocuous (warm) temperatures and shows an increased response at noxious temperatures. TRPV3 is specifically expressed in keratinocytes; hence, skin cells are capable of detecting heat via molecules similar to those in heat-sensing neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peier, Andrea M -- Reeve, Alison J -- Andersson, David A -- Moqrich, Aziz -- Earley, Taryn J -- Hergarden, Anne C -- Story, Gina M -- Colley, Sian -- Hogenesch, John B -- McIntyre, Peter -- Bevan, Stuart -- Patapoutian, Ardem -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2046-9. Epub 2002 May 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016205" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Newborn ; Blotting, Northern ; CHO Cells ; Capsaicin/*analogs & derivatives/pharmacology ; *Cation Transport Proteins ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Cricetinae ; Epidermis/cytology/innervation/metabolism ; Ganglia, Spinal/metabolism ; *Hot Temperature ; Humans ; In Situ Hybridization ; Ion Channels/chemistry/genetics/*metabolism ; Keratinocytes/*metabolism ; Membrane Potentials ; Mice ; Molecular Sequence Data ; Nerve Endings/physiology ; Neurons/physiology ; Patch-Clamp Techniques ; RNA, Messenger/genetics/metabolism ; Ruthenium Red/pharmacology ; Signal Transduction ; Spinal Cord/metabolism ; TRPV Cation Channels ; Temperature
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  • 73
    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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 74
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    American Association for the Advancement of Science (AAAS)
    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
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  • 75
    Publication Date: 2002-12-03
    Description: The Survival of Motor Neurons (SMN) protein, the product of the spinal muscular atrophy-determining gene, is part of a large macromolecular complex (SMN complex) that functions in the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs). Using cell extracts and purified components, we demonstrated that the SMN complex is necessary and sufficient to mediate the ATP-dependent assembly of the core of seven Sm proteins on uridine-rich, small nuclear ribonucleic acids (U snRNAs). In vitro experiments revealed strict requirements for ordered binding of the Sm proteins and the U snRNAs to the SMN complex. Importantly, the SMN complex is necessary to ensure that Sm cores assemble only on correct RNA targets and prevent their otherwise promiscuous association with other RNAs. Thus, the SMN complex functions as a specificity factor essential for the efficient assembly of Sm proteins on U snRNAs and likely protects cells from illicit, and potentially deleterious, nonspecific binding of Sm proteins to RNAs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pellizzoni, Livio -- Yong, Jeongsik -- Dreyfuss, Gideon -- New York, N.Y. -- Science. 2002 Nov 29;298(5599):1775-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12459587" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Carrier Proteins/metabolism ; Cell Extracts ; Cyclic AMP Response Element-Binding Protein ; DEAD Box Protein 20 ; DEAD-box RNA Helicases ; HeLa Cells ; Humans ; Kinetics ; Models, Biological ; Nerve Tissue Proteins/isolation & purification/*metabolism ; Nuclear Proteins/metabolism ; Oligoribonucleotides/metabolism ; Protein Binding ; RNA Helicases/metabolism ; RNA, Small Nuclear/*metabolism ; RNA-Binding Proteins ; Ribonucleoproteins, Small Nuclear/isolation & purification/*metabolism ; SMN Complex Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 76
    Publication Date: 2002-01-19
    Description: Blood vessels express estrogen receptors, but their role in cardiovascular physiology is not well understood. We show that vascular smooth muscle cells and blood vessels from estrogen receptor beta (ERbeta)-deficient mice exhibit multiple functional abnormalities. In wild-type mouse blood vessels, estrogen attenuates vasoconstriction by an ERbeta-mediated increase in inducible nitric oxide synthase expression. In contrast, estrogen augments vasoconstriction in blood vessels from ERbeta-deficient mice. Vascular smooth muscle cells isolated from ERbeta-deficient mice show multiple abnormalities of ion channel function. Furthermore, ERbeta-deficient mice develop sustained systolic and diastolic hypertension as they age. These data support an essential role for ERbeta in the regulation of vascular function and blood pressure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, Yan -- Bian, Zhao -- Lu, Ping -- Karas, Richard H -- Bao, Lin -- Cox, Daniel -- Hodgin, Jeffrey -- Shaul, Philip W -- Thoren, Peter -- Smithies, Oliver -- Gustafsson, Jan-Ake -- Mendelsohn, Michael E -- GM20069/GM/NIGMS NIH HHS/ -- HD30276/HD/NICHD NIH HHS/ -- HL53546/HL/NHLBI NIH HHS/ -- HL56235/HL/NHLBI NIH HHS/ -- P50 HL63494/HL/NHLBI NIH HHS/ -- R01 HL55309/HL/NHLBI NIH HHS/ -- R01 HL56069/HL/NHLBI NIH HHS/ -- R01 HL61298/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):505-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Cardiology Research Institute, New England Medical Center and Department of Medicine, Tufts University School of Medicine, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799247" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic alpha-Agonists/pharmacology ; Animals ; Aorta ; Blood Pressure ; Cells, Cultured ; Estradiol/*analogs & derivatives/pharmacology ; Estrogen Antagonists/pharmacology ; Estrogen Receptor alpha ; Estrogen Receptor beta ; Guanidines/pharmacology ; Humans ; Hypertension/*physiopathology ; In Vitro Techniques ; Male ; Mice ; Mice, Knockout ; Muscle, Smooth, Vascular/*physiology ; Nitric Oxide Synthase/genetics/metabolism ; Nitric Oxide Synthase Type II ; Nitroarginine/pharmacology ; Patch-Clamp Techniques ; Phenylephrine/pharmacology ; Potassium Channels/metabolism ; Receptors, Estrogen/genetics/*physiology ; *Vasoconstriction/drug effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, Timothy Trengove -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2015.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11898821" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/*therapeutic use ; Drug Industry/legislation & jurisprudence ; Female ; HIV Infections/*drug therapy/prevention & control/transmission ; Humans ; Infant ; Infectious Disease Transmission, Vertical/*prevention & control ; Jurisprudence ; Nevirapine/therapeutic use ; *Politics ; Pregnancy ; Preventive Health Services/*legislation & jurisprudence ; South Africa
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  • 78
    Publication Date: 2002-05-04
    Description: Neurofibromatosis type 1 (NF1) is one of the most prevalent dominantly inherited genetic diseases of the nervous system. NF1 encodes a tumor suppressor whose functional loss results in the development of benign neurofibromas that can progress to malignancy. Neurofibromas are complex tumors composed of axonal processes, Schwann cells, fibroblasts, perineurial cells, and mast cells. Through use of a conditional (cre/lox) allele, we show that loss of NF1 in the Schwann cell lineage is sufficient to generate tumors. In addition, complete NF1-mediated tumorigenicity requires both a loss of NF1 in cells destined to become neoplastic as well as heterozygosity in non-neoplastic cells. The requirement for a permissive haploinsufficient environment to allow tumorigenesis may have therapeutic implications for NF1 and other familial cancers.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3024710/" 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/PMC3024710/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, Yuan -- Ghosh, Pritam -- Charnay, Patrick -- Burns, Dennis K -- Parada, Luis F -- R01 NS034296/NS/NINDS NIH HHS/ -- R01 NS034296-06/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):920-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Developmental Biology, Department of Pathology, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75390-9133, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988578" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Axons/ultrastructure ; Cell Lineage ; Cell Transformation, Neoplastic ; Cells, Cultured ; Cranial Nerves/pathology ; Culture Techniques ; Female ; *Genes, Neurofibromatosis 1 ; Genotype ; Heterozygote ; Hyperplasia ; Loss of Heterozygosity ; Male ; Mast Cells/chemistry/pathology ; Mice ; Mice, Transgenic ; Neurofibroma/genetics/*pathology ; Neurofibromatosis 1/genetics/*pathology ; Peripheral Nerves/pathology ; Schwann Cells/chemistry/*pathology ; Spinal Nerves/pathology
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  • 79
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2111-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481111" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Cellulose/biosynthesis ; Ciona intestinalis/anatomy & histology/classification/*genetics/physiology ; Computational Biology ; Gene Dosage ; Gene Transfer, Horizontal ; Genes ; *Genome ; Humans ; *Sequence Analysis, DNA ; Species Specificity ; Vertebrates/classification/genetics
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  • 80
    Publication Date: 2002-09-21
    Description: Persons with the autosomal recessive disorder Bloom syndrome are predisposed to cancers of many types due to loss-of-function mutations in the BLM gene, which encodes a recQ-like helicase. Here we show that mice heterozygous for a targeted null mutation of Blm, the murine homolog of BLM, develop lymphoma earlier than wild-type littermates in response to challenge with murine leukemia virus and develop twice the number of intestinal tumors when crossed with mice carrying a mutation in the Apc tumor suppressor. These observations indicate that Blm is a modifier of tumor formation in the mouse and that Blm haploinsufficiency is associated with tumor predisposition, a finding with important implications for cancer risk in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goss, Kathleen Heppner -- Risinger, Mary A -- Kordich, Jennifer J -- Sanz, Maureen M -- Straughen, Joel E -- Slovek, Lisa E -- Capobianco, Anthony J -- German, James -- Boivin, Gregory P -- Groden, Joanna -- CA63507/CA/NCI NIH HHS/ -- CA84291/CA/NCI NIH HHS/ -- CA88460/CA/NCI NIH HHS/ -- ES06096/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 20;297(5589):2051-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Department of Molecular Genetics, University of Cincinnati College of Medicine, 231 Albert Sabin Way, Cincinnati, OH 45267, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12242442" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoma/genetics/pathology ; Adenosine Triphosphatases/*genetics ; Alleles ; Animals ; Bloom Syndrome/*genetics ; Cells, Cultured ; Crosses, Genetic ; DNA Helicases/*genetics ; Female ; Gene Targeting ; Genes, APC ; *Genetic Predisposition to Disease ; *Heterozygote ; Humans ; Intestinal Neoplasms/*genetics/pathology ; Leukemia Virus, Murine ; Loss of Heterozygosity ; Lymphoma, T-Cell/*genetics/virology ; Male ; Mice ; Mice, Inbred C57BL ; Mutation ; RecQ Helicases ; Sister Chromatid Exchange
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  • 81
    Publication Date: 2002-05-25
    Description: We have studied the correlation between structural dynamics and function of the hairpin ribozyme. The enzyme-substrate complex exists in either docked (active) or undocked (inactive) conformations. Using single-molecule fluorescence methods, we found complex structural dynamics with four docked states of distinct stabilities and a strong memory effect where each molecule rarely switches between different docked states. We also found substrate cleavage to be rate-limited by a combination of conformational transitions and reversible chemistry equilibrium. The complex structural dynamics quantitatively explain the heterogeneous cleavage kinetics common to many catalytic RNAs. The intimate coupling of structural dynamics and function is likely a general phenomenon for RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhuang, Xiaowei -- Kim, Harold -- Pereira, Miguel J B -- Babcock, Hazen P -- Walter, Nils G -- Chu, Steven -- GM62357/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 May 24;296(5572):1473-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029135" target="_blank"〉PubMed〈/a〉
    Keywords: Carbocyanines/metabolism ; Catalysis ; Enzymes, Immobilized ; Fluorescence ; Hydrogen Bonding ; Kinetics ; Nepovirus/genetics ; Nucleic Acid Conformation ; RNA, Catalytic/*chemistry/*metabolism ; RNA, Satellite ; RNA, Viral/*chemistry/*metabolism ; Spectrometry, Fluorescence ; Thermodynamics
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  • 82
    Publication Date: 2002-08-24
    Description: The mammalian ovarian follicle consists of a multilayered complex of somatic cells that surround the oocyte. A signal from the follicle cells keeps the oocyte cell cycle arrested at prophase of meiosis I until luteinizing hormone from the pituitary acts on the follicle cells to release the arrest, causing meiosis to continue. Here we show that meiotic arrest can be released in mice by microinjecting the oocyte within the follicle with an antibody that inhibits the stimulatory heterotrimeric GTP-binding protein Gs. This indicates that Gs activity in the oocyte is required to maintain meiotic arrest within the ovarian follicle and suggests that the follicle may keep the cell cycle arrested by activating Gs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mehlmann, Lisa M -- Jones, Teresa L Z -- Jaffe, Laurinda A -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1343-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Connecticut Health Center, Farmington, CT 06032, USA. lmehlman@neuron.uchc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193786" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/immunology ; Cells, Cultured ; Cyclic AMP/metabolism ; Female ; GTP-Binding Protein alpha Subunits, Gi-Go/immunology/physiology ; GTP-Binding Protein alpha Subunits, Gs/antagonists & ; inhibitors/immunology/*physiology ; Hypoxanthine/pharmacology ; *Meiosis ; Mice ; Oocytes/drug effects/metabolism/*physiology ; Ovarian Follicle/*physiology ; Signal Transduction
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1863-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471226" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Chromosomes, Human, Pair 21/genetics ; Conserved Sequence ; Gene Expression ; Gene Expression Profiling ; Genes ; *Genome ; *Genome, Human ; Humans ; Mice/*genetics ; Rats/genetics ; *Sequence Analysis, DNA ; Species Specificity
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-11-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, Elizabeth -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1540-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446885" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Domestic/anatomy & histology/classification/genetics ; *Behavior, Animal ; Biological Evolution ; Body Constitution ; Breeding ; Cues ; DNA, Mitochondrial/genetics ; *Dogs/anatomy & histology/classification/genetics ; Fossils ; Genes ; Genetic Variation ; Genome ; Humans ; Phylogeny ; Selection, Genetic ; Sequence Analysis, DNA ; Wolves/genetics
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  • 85
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-06-22
    Description: The recently developed testis cell transplantation method provides a powerful approach to studying the biology of the male germline stem cell and its microenvironment, the stem cell niche. The technique also is being used to examine spermatogenic defects, correct male infertility, and generate transgenic animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brinster, Ralph L -- 36504/PHS HHS/ -- New York, N.Y. -- Science. 2002 Jun 21;296(5576):2174-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, 3850 Baltimore Avenue, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12077400" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Separation ; Cells, Cultured ; Cryopreservation ; Humans ; Male ; Seminiferous Tubules/cytology ; Sertoli Cells/physiology ; *Spermatogenesis ; Spermatogonia/*cytology/physiology ; *Stem Cell Transplantation ; Stem Cells/physiology ; Testis/*cytology ; Transduction, Genetic ; *Transgenes ; Transplantation, Heterologous
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  • 86
    Publication Date: 2002-03-02
    Description: When bound by extracellular ligands, receptor tyrosine kinases (RTKs) on the cell surface transmit critical signals to the cell interior. Although signal termination is less well understood, protein tyrosine phosphatase-1B (PTP1B) is implicated in the dephosphorylation and inactivation of several RTKs. However, PTP1B resides on the cytoplasmic surface of the endoplasmic reticulum (ER), so how and when it accesses RTKs has been unclear. Using fluorescence resonance energy transfer (FRET) methods, we monitored interactions between the epidermal- and platelet-derived growth factor receptors and PTP1B. PTP1B-catalyzed dephosphorylation required endocytosis of the receptors and occurred at specific sites on the surface of the ER. Most of the RTKs activated at the cell surface showed interaction with PTP1B after internalization, establishing that RTK activation and inactivation are spatially and temporally partitioned within cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haj, Fawaz G -- Verveer, Peter J -- Squire, Anthony -- Neel, Benjamin G -- Bastiaens, Philippe I H -- R01 CA49152/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1708-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Biology Program, Division of Hematology-Oncology, Department of Medicine, Beth Israel-Deaconess Medical Center, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872838" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Catalytic Domain ; Cell Membrane/enzymology ; Cells, Cultured ; *Endocytosis ; Endoplasmic Reticulum/*enzymology ; Energy Transfer ; Epidermal Growth Factor/metabolism/pharmacology ; Fluorescence ; Mice ; Microscopy, Confocal ; Microscopy, Fluorescence ; Phosphorylation ; Platelet-Derived Growth Factor/metabolism/pharmacology ; Protein Transport ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 ; Protein Tyrosine Phosphatases/chemistry/genetics/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Receptors, Platelet-Derived Growth Factor/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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  • 87
    Publication Date: 2002-12-14
    Description: The first chordates appear in the fossil record at the time of the Cambrian explosion, nearly 550 million years ago. The modern ascidian tadpole represents a plausible approximation to these ancestral chordates. To illuminate the origins of chordate and vertebrates, we generated a draft of the protein-coding portion of the genome of the most studied ascidian, Ciona intestinalis. The Ciona genome contains approximately 16,000 protein-coding genes, similar to the number in other invertebrates, but only half that found in vertebrates. Vertebrate gene families are typically found in simplified form in Ciona, suggesting that ascidians contain the basic ancestral complement of genes involved in cell signaling and development. The ascidian genome has also acquired a number of lineage-specific innovations, including a group of genes engaged in cellulose metabolism that are related to those in bacteria and fungi.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dehal, Paramvir -- Satou, Yutaka -- Campbell, Robert K -- Chapman, Jarrod -- Degnan, Bernard -- De Tomaso, Anthony -- Davidson, Brad -- Di Gregorio, Anna -- Gelpke, Maarten -- Goodstein, David M -- Harafuji, Naoe -- Hastings, Kenneth E M -- Ho, Isaac -- Hotta, Kohji -- Huang, Wayne -- Kawashima, Takeshi -- Lemaire, Patrick -- Martinez, Diego -- Meinertzhagen, Ian A -- Necula, Simona -- Nonaka, Masaru -- Putnam, Nik -- Rash, Sam -- Saiga, Hidetoshi -- Satake, Masanobu -- Terry, Astrid -- Yamada, Lixy -- Wang, Hong-Gang -- Awazu, Satoko -- Azumi, Kaoru -- Boore, Jeffrey -- Branno, Margherita -- Chin-Bow, Stephen -- DeSantis, Rosaria -- Doyle, Sharon -- Francino, Pilar -- Keys, David N -- Haga, Shinobu -- Hayashi, Hiroko -- Hino, Kyosuke -- Imai, Kaoru S -- Inaba, Kazuo -- Kano, Shungo -- Kobayashi, Kenji -- Kobayashi, Mari -- Lee, Byung-In -- Makabe, Kazuhiro W -- Manohar, Chitra -- Matassi, Giorgio -- Medina, Monica -- Mochizuki, Yasuaki -- Mount, Steve -- Morishita, Tomomi -- Miura, Sachiko -- Nakayama, Akie -- Nishizaka, Satoko -- Nomoto, Hisayo -- Ohta, Fumiko -- Oishi, Kazuko -- Rigoutsos, Isidore -- Sano, Masako -- Sasaki, Akane -- Sasakura, Yasunori -- Shoguchi, Eiichi -- Shin-i, Tadasu -- Spagnuolo, Antoinetta -- Stainier, Didier -- Suzuki, Miho M -- Tassy, Olivier -- Takatori, Naohito -- Tokuoka, Miki -- Yagi, Kasumi -- Yoshizaki, Fumiko -- Wada, Shuichi -- Zhang, Cindy -- Hyatt, P Douglas -- Larimer, Frank -- Detter, Chris -- Doggett, Norman -- Glavina, Tijana -- Hawkins, Trevor -- Richardson, Paul -- Lucas, Susan -- Kohara, Yuji -- Levine, Michael -- Satoh, Nori -- Rokhsar, Daniel S -- HD-37105/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2157-67.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U.S. Department of Energy Joint Genome Institute, 2800 Mitchell Drive, Walnut Creek, CA 94598, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481130" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Apoptosis ; Base Sequence ; Cellulose/metabolism ; Central Nervous System/physiology ; Ciona intestinalis/anatomy & histology/classification/*genetics/physiology ; Computational Biology ; Endocrine System/physiology ; Gene Dosage ; Gene Duplication ; Genes ; Genes, Homeobox ; *Genome ; Heart/embryology/physiology ; Immunity/genetics ; Molecular Sequence Data ; Multigene Family ; Muscle Proteins/genetics ; Organizers, Embryonic/physiology ; Phylogeny ; Polymorphism, Genetic ; Proteins/genetics/physiology ; *Sequence Analysis, DNA ; Sequence Homology, Nucleic Acid ; Species Specificity ; Thyroid Gland/physiology ; Urochordata/genetics ; Vertebrates/anatomy & histology/classification/genetics/physiology
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  • 88
    Publication Date: 2002-03-30
    Description: Primary human cells in culture invariably stop dividing and enter a state of growth arrest called replicative senescence. This transition is induced by programmed telomere shortening, but the underlying mechanisms are unclear. Here, we report that overexpression of TRF2, a telomeric DNA binding protein, increased the rate of telomere shortening in primary cells without accelerating senescence. TRF2 reduced the senescence setpoint, defined as telomere length at senescence, from 7 to 4 kilobases. TRF2 protected critically short telomeres from fusion and repressed chromosome-end fusions in presenescent cultures, which explains the ability of TRF2 to delay senescence. Thus, replicative senescence is induced by a change in the protected status of shortened telomeres rather than by a complete loss of telomeric DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karlseder, Jan -- Smogorzewska, Agata -- de Lange, Titia -- AG16643/AG/NIA NIH HHS/ -- CA76027/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 29;295(5564):2446-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cell Biology and Genetics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11923537" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Polyomavirus Transforming/genetics/metabolism ; *Cell Aging ; *Cell Division ; Cell Line ; Cells, Cultured ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Humans ; Oncogene Proteins, Viral/genetics/metabolism ; Papillomavirus E7 Proteins ; *Repressor Proteins ; Retinoblastoma Protein/metabolism ; Retroviridae/genetics ; Telomere/metabolism/*physiology ; Telomeric Repeat Binding Protein 2 ; Transformation, Genetic ; Tumor Suppressor Protein p53/metabolism
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  • 89
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, Robert F -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):419-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799209" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biopolymers ; Cattle ; Cell Line ; Cricetinae ; Epithelial Cells/metabolism ; *Fibroins ; Genes ; Mechanics ; Molecular Weight ; *Protein Biosynthesis ; Proteins/chemistry/*genetics/isolation & purification ; Recombinant Proteins/biosynthesis/chemistry ; Spiders/*genetics
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  • 90
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, Virginia -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1816.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884728" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carotenoids/analysis ; Color ; *Feeding Behavior ; Female ; *Food Preferences ; Fruit/chemistry ; Genes ; Male ; *Pigmentation ; Poecilia/anatomy & histology/genetics/*physiology ; *Sexual Behavior, Animal
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  • 91
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-08-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Aug 2;297(5582):754-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12161624" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Biotechnology/*economics/legislation & jurisprudence ; Cloning, Organism/economics/legislation & jurisprudence ; *DNA/genetics ; Embryo, Mammalian/cytology ; Europe ; Genes ; Humans ; Patents as Topic/*legislation & jurisprudence ; *Stem Cells/metabolism ; United States
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  • 92
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-02-23
    Description: Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the reaction trajectory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisenmesser, Elan Zohar -- Bosco, Daryl A -- Akke, Mikael -- Kern, Dorothee -- GM62117/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1520-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Brandeis University, Waltham, MA 02454, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859194" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Isomerism ; Kinetics ; Mathematics ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation
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  • 93
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-07-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Jul 19;297(5580):328.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12130764" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Evolution ; Cell Count ; Cell Division ; Cells, Cultured ; Cerebral Cortex/cytology/*embryology ; Cytoskeletal Proteins/*genetics/physiology ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Homeodomain Proteins/*genetics/physiology ; Humans ; Mice ; Mice, Transgenic ; Mutation ; Neurons/cytology/physiology ; Pituitary Gland/*cytology/growth & development ; Retina/*cytology/growth & development ; Stem Cells/cytology/*physiology ; Trans-Activators/*genetics/physiology ; beta Catenin
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  • 94
    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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  • 95
    Publication Date: 2002-12-21
    Description: The immunoglobulin G (IgG)-containing B lymphocyte antigen receptor (IgG-BCR) transmits a signal distinct from that of IgM-BCR or IgD-BCR, although all three use the same signal-transducing component, Igalpha/Igbeta. Here we demonstrate that the inhibitory coreceptor CD22 down-modulates signaling through IgM-BCR and IgD-BCR, but not that through IgG-BCR, because of the IgG cytoplasmic tail, which prevents CD22 phosphorylation. These results suggest that the cytoplasmic tail of IgG specifically enhances IgG-BCR signaling by preventing CD22-mediated signal inhibition. Enhanced signaling through IgG-BCR may be involved in efficient IgG production, which is crucial for immunity to pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wakabayashi, Chisato -- Adachi, Takahiro -- Wienands, Jurgen -- Tsubata, Takeshi -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2392-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Medical Research Institute, Tokyo Medical and Dental University, 113-8510 Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493916" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/metabolism ; Antigens, Differentiation, B-Lymphocyte/metabolism ; B-Lymphocytes/immunology/metabolism ; Calcium/metabolism ; Calcium Signaling ; *Cell Adhesion Molecules ; Cells, Cultured ; Immunoglobulin D/immunology/metabolism ; Immunoglobulin G/chemistry/immunology/*metabolism ; Intracellular Signaling Peptides and Proteins ; Lectins/metabolism ; Mice ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/metabolism ; Receptors, Antigen, B-Cell/chemistry/immunology/*metabolism ; Sialic Acid Binding Ig-like Lectin 2 ; *Signal Transduction ; Transfection ; Tumor Cells, Cultured
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  • 96
    Publication Date: 2002-09-14
    Description: Antigen-presenting cells (APCs) can induce tolerance or immunity. We describe a subset of human APCs that express indoleamine 2,3-dioxygenase (IDO) and inhibit T cell proliferation in vitro. IDO-positive APCs constituted a discrete subset identified by coexpression of the cell-surface markers CD123 and CCR6. In the dendritic cell (DC) lineage, IDO-mediated suppressor activity was present in fully mature as well as immature CD123+ DCs. IDO+ DCs could also be readily detected in vivo, which suggests that these cells may represent a regulatory subset of APCs in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Munn, David H -- Sharma, Madhav D -- Lee, Jeffrey R -- Jhaver, Kanchan G -- Johnson, Theodore S -- Keskin, Derin B -- Marshall, Brendan -- Chandler, Phillip -- Antonia, Scott J -- Burgess, Russell -- Slingluff, Craig L Jr -- Mellor, Andrew L -- AI44219/AI/NIAID NIH HHS/ -- AI44759/AI/NIAID NIH HHS/ -- HL60137/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 13;297(5588):1867-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, GA 30912, USA. dmunn@mail.mcg.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228717" target="_blank"〉PubMed〈/a〉
    Keywords: Antigen-Presenting Cells/enzymology/immunology ; Antigens, CD/analysis ; Cell Adhesion ; Cell Lineage ; Cells, Cultured ; Dendritic Cells/*enzymology/*immunology ; Down-Regulation ; Enzyme Inhibitors/pharmacology ; Humans ; Indoleamine-Pyrrole 2,3,-Dioxygenase ; Interferon-gamma/pharmacology ; Interleukin-10/pharmacology ; Interleukin-3 Receptor alpha Subunit ; Lymphocyte Activation ; Lymphocyte Culture Test, Mixed ; Lymphoid Tissue/cytology/enzymology ; Macrophages/enzymology ; Receptors, CCR6 ; Receptors, Chemokine/analysis ; Receptors, Interleukin-3/analysis ; T-Lymphocytes/*immunology ; Tryptophan/*analogs & derivatives/pharmacology ; Tryptophan Oxygenase/antagonists & inhibitors/*metabolism
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  • 97
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-03-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, Gretchen -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):1989-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896242" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Culture Techniques ; *Cell Differentiation ; *Cell Fusion ; Cell Lineage ; Cells, Cultured ; Chromosome Aberrations ; Embryo, Mammalian/cytology ; Hybrid Cells/*physiology ; Mice ; Polyploidy ; Stem Cells/cytology/*physiology
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  • 98
    Publication Date: 2000-01-05
    Description: Mutations in copper, zinc superoxide dismutase (SOD) have been implicated in the selective death of motor neurons in 2 percent of amyotrophic lateral sclerosis (ALS) patients. The loss of zinc from either wild-type or ALS-mutant SODs was sufficient to induce apoptosis in cultured motor neurons. Toxicity required that copper be bound to SOD and depended on endogenous production of nitric oxide. When replete with zinc, neither ALS-mutant nor wild-type copper, zinc SODs were toxic, and both protected motor neurons from trophic factor withdrawal. Thus, zinc-deficient SOD may participate in both sporadic and familial ALS by an oxidative mechanism involving nitric oxide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Estevez, A G -- Crow, J P -- Sampson, J B -- Reiter, C -- Zhuang, Y -- Richardson, G J -- Tarpey, M M -- Barbeito, L -- Beckman, J S -- R01 HL58209/HL/NHLBI NIH HHS/ -- R01 NS33291/NS/NINDS NIH HHS/ -- R01 NS36761/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2498-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anesthesiology, University of Alabama at Birmingham, Birmingham, AL 35233, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617463" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/drug therapy/*enzymology/genetics/pathology ; Animals ; *Apoptosis ; Brain-Derived Neurotrophic Factor/pharmacology ; Cells, Cultured ; Chelating Agents/pharmacology ; Copper/metabolism ; Fluoresceins/metabolism ; Liposomes ; Motor Neurons/*cytology/metabolism ; Mutation ; Nitrates/metabolism ; Nitric Oxide/*metabolism ; Nitric Oxide Synthase/antagonists & inhibitors/metabolism ; Nitric Oxide Synthase Type I ; Oxidation-Reduction ; Rats ; Superoxide Dismutase/chemistry/genetics/*metabolism/toxicity ; Superoxides/metabolism ; Zinc/*metabolism
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  • 99
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-01-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Plotkin, S A -- Koprowski, H -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2450.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10636806" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Democratic Republic of the Congo ; History, 20th Century ; Humans ; Immunization Programs/history ; Pan troglodytes ; Poliovirus/growth & development ; Poliovirus Vaccine, Oral/*history ; Virus Cultivation
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  • 100
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 2000 Apr 28;288(5466):586-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10798984" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics ; Animals ; Bioethics ; Cattle/*genetics ; *Cell Aging/genetics ; Cell Division ; Cells, Cultured ; *Cloning, Organism ; Female ; Nuclear Transfer Techniques ; Oocytes/physiology ; Stem Cells ; Telomere/*ultrastructure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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