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  • Articles  (444)
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  • American Association for the Advancement of Science (AAAS)  (444)
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  • 1
    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
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    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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  • 3
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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
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  • 4
    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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  • 5
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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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  • 6
    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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  • 7
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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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  • 8
    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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  • 9
    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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  • 10
    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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  • 11
    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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  • 12
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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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  • 13
    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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  • 14
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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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  • 15
    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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  • 16
    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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  • 17
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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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  • 18
    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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  • 19
    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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  • 20
    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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  • 21
    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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  • 22
    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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  • 23
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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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  • 24
    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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  • 25
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    Unknown
    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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  • 26
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    Unknown
    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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  • 27
    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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  • 28
    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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  • 29
    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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  • 30
    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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  • 31
    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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  • 32
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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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  • 33
    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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  • 34
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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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  • 35
    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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  • 36
    Publication Date: 2000-06-02
    Description: The mechanism by which a signal recognition particle (SRP) and its receptor mediate protein targeting to the endoplasmic reticulum or to the bacterial plasma membrane is evolutionarily conserved. In Escherichia coli, this reaction is mediated by the Ffh/4.5S RNA ribonucleoprotein complex (Ffh/4.5S RNP; the SRP) and the FtsY protein (the SRP receptor). We have quantified the effects of 4.5S RNA on Ffh-FtsY complex formation by monitoring changes in tryptophan fluorescence. Surprisingly, 4.5S RNA facilitates both assembly and disassembly of the Ffh-FtsY complex to a similar extent. These results provide an example of an RNA molecule facilitating protein-protein interactions in a catalytic fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peluso, P -- Herschlag, D -- Nock, S -- Freymann, D M -- Johnson, A E -- Walter, P -- GM 26494/GM/NIGMS NIH HHS/ -- GM 32384/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 2;288(5471):1640-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10834842" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/chemistry/*metabolism ; Catalysis ; Escherichia coli/metabolism ; *Escherichia coli Proteins ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Guanylyl Imidodiphosphate/metabolism ; Kinetics ; Models, Chemical ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; RNA, Bacterial/chemistry/*metabolism ; Receptors, Cytoplasmic and Nuclear/chemistry/*metabolism ; Ribonucleoproteins/chemistry/metabolism ; Signal Recognition Particle/chemistry/*metabolism ; Spectrometry, Fluorescence ; Thermodynamics ; Tryptophan
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  • 37
    Publication Date: 2000-01-22
    Description: Complement is a component of natural immunity. Its regulation is needed to protect tissues from inflammation, but mice with a disrupted gene for the complement regulator decay accelerating factor were normal. Mice that were deficient in another murine complement regulator, Crry, were generated to investigate its role in vivo. Survival of Crry-/- embryos was compromised because of complement deposition and concomitant placenta inflammation. Complement activation at the fetomaternal interface caused the fetal loss because breeding to C3-/- mice rescued Crry-/- mice from lethality. Thus, the regulation of complement is critical in fetal control of maternal processes that mediate tissue damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, C -- Mao, D -- Holers, V M -- Palanca, B -- Cheng, A M -- Molina, H -- R01 AI40576-01/AI/NIAID NIH HHS/ -- R01 AI44912-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Jan 21;287(5452):498-501.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, 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/10642554" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Complement Activation ; Complement C3/analysis/immunology ; Embryo, Mammalian/*immunology/metabolism ; *Embryonic and Fetal Development ; Female ; Gene Targeting ; *Immune Tolerance ; Mice ; Neutrophil Infiltration ; Pregnancy ; Receptors, Complement/genetics/*physiology ; Trophoblasts/immunology/metabolism
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  • 38
    Publication Date: 2000-02-26
    Description: Many protein enzymes use general acid-base catalysis as a way to increase reaction rates. The amino acid histidine is optimized for this function because it has a pK(a) (where K(a) is the acid dissociation constant) near physiological pH. The RNA enzyme (ribozyme) from hepatitis delta virus catalyzes self-cleavage of a phosphodiester bond. Reactivity-pH profiles in monovalent or divalent cations, as well as distance to the leaving-group oxygen, implicate cytosine 75 (C75) of the ribozyme as the general acid and ribozyme-bound hydrated metal hydroxide as the general base in the self-cleavage reaction. Moreover, C75 has a pK(a) perturbed to neutrality, making it "histidine-like." Anticooperative interaction is observed between protonated C75 and a metal ion, which serves to modulate the pK(a) of C75. General acid-base catalysis expands the catalytic repertoire of RNA and may provide improved rate acceleration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakano, S -- Chadalavada, D M -- Bevilacqua, P C -- GM58709/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Feb 25;287(5457):1493-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10688799" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Binding Sites ; Calcium/metabolism ; Catalysis ; Cobalt/metabolism ; Crystallography, X-Ray ; Hepatitis Delta Virus/*chemistry/enzymology ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Kinetics ; Magnesium/metabolism ; Metals/metabolism ; Models, Chemical ; Models, Molecular ; Nucleic Acid Conformation ; Protons ; RNA, Catalytic/chemistry/*metabolism ; RNA, Viral/chemistry/metabolism ; Static Electricity ; Thermodynamics
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  • 39
    Publication Date: 2000-07-07
    Description: Hypertension and pregnancy-related hypertension are major public health problems of largely unknown causes. We describe a mutation in the mineralocorticoid receptor (MR), S810L, that causes early-onset hypertension that is markedly exacerbated in pregnancy. This mutation results in constitutive MR activity and alters receptor specificity, with progesterone and other steroids lacking 21-hydroxyl groups, normally MR antagonists, becoming potent agonists. Structural and biochemical studies indicate that the mutation results in the gain of a van der Waals interaction between helix 5 and helix 3 that substitutes for interaction of the steroid 21-hydroxyl group with helix 3 in the wild-type receptor. This helix 5-helix 3 interaction is highly conserved among diverse nuclear hormone receptors, suggesting its general role in receptor activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geller, D S -- Farhi, A -- Pinkerton, N -- Fradley, M -- Moritz, M -- Spitzer, A -- Meinke, G -- Tsai, F T -- Sigler, P B -- Lifton, R P -- New York, N.Y. -- Science. 2000 Jul 7;289(5476):119-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Genetics, Yale University School of Medicine, Boyer Center for Molecular Medicine, Room 154, 295 Congress Avenue, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10884226" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Aldosterone/*metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Base Sequence ; Binding, Competitive ; Dimerization ; Female ; Heterozygote ; Humans ; Hypertension/etiology/*genetics/metabolism ; Male ; Models, Molecular ; Molecular Sequence Data ; Pedigree ; Point Mutation ; Pregnancy ; *Pregnancy Complications, Cardiovascular/etiology/metabolism ; Progesterone/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Receptors, Mineralocorticoid/chemistry/*genetics/*metabolism ; Receptors, Steroid/chemistry/metabolism ; Steroids/metabolism
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-15
    Description: At the Chris Hani Baragwanath Hospital here, where HIV infects more than 20% of the 17,000 pregnant women who give birth here each year, pediatrician Glenda Gray and obstetrician James McIntyre aggressively try to help HIV-infected pregnant women stop the virus from infecting their babies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 2000 Jun 23;288(5474):2163.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10896602" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/therapeutic use ; Female ; HIV Infections/diagnosis/drug therapy/prevention & control/*transmission ; History, 20th Century ; Humans ; *Infectious Disease Transmission, Vertical ; Pregnancy ; Pregnancy Complications, Infectious/diagnosis/*drug therapy ; South Africa
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  • 41
    Publication Date: 2000-03-31
    Description: Using an optical-trap/flow-control video microscopy technique, we followed transcription by single molecules of Escherichia coli RNA polymerase in real time over long template distances. These studies reveal that RNA polymerase molecules possess different intrinsic transcription rates and different propensities to pause and stop. The data also show that reversible pausing is a kinetic intermediate between normal elongation and the arrested state. The conformational metastability of RNA polymerase revealed by this single-molecule study of transcription has direct implications for the mechanisms of gene regulation in both bacteria and eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davenport, R J -- Wuite, G J -- Landick, R -- Bustamante, C -- GM-32543/GM/NIGMS NIH HHS/ -- GM-38660/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 31;287(5462):2497-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10741971" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Bacterial/genetics/*metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Escherichia coli/enzymology/*genetics ; Kinetics ; Microscopy, Video ; Models, Genetic ; Optics and Photonics ; RNA, Bacterial/genetics ; RNA, Messenger/*genetics ; Templates, Genetic ; *Transcription, Genetic
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  • 42
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagmann, M -- New York, N.Y. -- Science. 2000 Jan 21;287(5452):408.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10671158" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Complement Activation ; Complement System Proteins/*immunology ; Embryo, Mammalian/*immunology ; Female ; Humans ; *Immune Tolerance ; Immunity, Innate ; Mice ; Mice, Knockout ; Pregnancy ; Receptors, Complement/genetics/*physiology ; Trophoblasts/immunology
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Will, C L -- Luhrmann, R -- New York, N.Y. -- Science. 2001 Mar 9;291(5510):1916-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany. cwill1@gwdg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11245200" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Anhydride Hydrolases/*metabolism ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; DEAD-box RNA Helicases ; Fungal Proteins/metabolism ; Kinetics ; Nucleoside-Triphosphatase ; RNA Nucleotidyltransferases/metabolism ; RNA Precursors/metabolism ; RNA, Double-Stranded/*metabolism ; RNA, Small Nuclear/*metabolism ; *RNA-Binding Proteins ; Ribonucleoprotein, U1 Small Nuclear/*metabolism ; Ribonucleoproteins/metabolism ; Ribonucleoproteins, Small Nuclear/*metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Spliceosomes/*metabolism ; Vaccinia virus/genetics/metabolism
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  • 44
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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〉Vogel, G -- New York, N.Y. -- Science. 2001 Nov 9;294(5545):1271-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11701910" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Zoo/anatomy & histology/physiology ; Conservation of Natural Resources ; Cryopreservation ; *Elephants/anatomy & histology/physiology ; Female ; Genitalia, Female/*ultrasonography ; Insemination, Artificial/*veterinary ; Male ; Pregnancy ; Semen Preservation ; Ultrasonography/*veterinary
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  • 45
    Publication Date: 2001-06-26
    Description: The temporal pattern and relative timing of action potentials among neocortical neurons may carry important information. However, how cortical circuits detect or generate coherent activity remains unclear. Using paired recordings in rat neocortical slices, we found that the firing of fast-spiking cells can reflect the spiking pattern of single-axon pyramidal inputs. Moreover, this property allowed groups of fast-spiking cells interconnected by electrical and gamma-aminobutyric acid (GABA)-releasing (GABAergic) synapses to detect the relative timing of their excitatory inputs. These results indicate that networks of fast-spiking cells may play a role in the detection and promotion of synchronous activity within the neocortex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galarreta, M -- Hestrin, S -- EY09120/EY/NEI NIH HHS/ -- EY12114/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 22;292(5525):2295-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Comparative Medicine, Department of Neurology and Neurological Sciences, Stanford University School of Medicine, Stanford, CA 94305, USA. galarreta@stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423653" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Axons/physiology ; Excitatory Postsynaptic Potentials ; Female ; In Vitro Techniques ; Interneurons/*physiology ; Kinetics ; Male ; Neocortex/cytology/*physiology ; Nerve Net/*physiology ; Pyramidal Cells/*physiology ; Rats ; Rats, Sprague-Dawley ; Synapses/physiology ; *Synaptic Transmission ; Time Factors ; gamma-Aminobutyric Acid/*metabolism
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  • 46
    Publication Date: 2001-12-26
    Description: The transfer of a hydrogen atom-a proton and an electron-is a fundamental process in chemistry and biology. A variety of hydrogen atom transfer reactions, involving iron complexes, phenols, hydroxylamines, tBuOOH, toluene, and related radicals, are shown to follow the Marcus cross relation. Thus, the Marcus theory formalism based on ground-state energetics and self-exchange rates, originally developed for electron transfer processes, is also valuable for hydrogen atom transfer. Compounds that undergo slow proton transfer (C-H bonds) or slow electron transfer (cobalt complexes) also undergo slow hydrogen atom transfer. Limitations of this approach are also discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roth, J P -- Yoder, J C -- Won, T J -- Mayer, J M -- 1 F32 GM63383-01/GM/NIGMS NIH HHS/ -- 2 R01 GM50422-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2524-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752572" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Cobalt/chemistry ; Cyclic N-Oxides/chemistry ; Electrons ; Ferric Compounds/chemistry ; Ferrous Compounds/chemistry ; Free Radicals ; Hydrogen/*chemistry ; Imidazoles/chemistry ; Kinetics ; Magnetic Resonance Spectroscopy ; Mathematics ; Oxidation-Reduction ; Physicochemical Phenomena ; Protons ; Pyrimidines/chemistry ; Thermodynamics
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  • 47
    Publication Date: 2002-02-09
    Description: Light synchronizes mammalian circadian rhythms with environmental time by modulating retinal input to the circadian pacemaker-the suprachiasmatic nucleus (SCN) of the hypothalamus. Such photic entrainment requires neither rods nor cones, the only known retinal photoreceptors. Here, we show that retinal ganglion cells innervating the SCN are intrinsically photosensitive. Unlike other ganglion cells, they depolarized in response to light even when all synaptic input from rods and cones was blocked. The sensitivity, spectral tuning, and slow kinetics of this light response matched those of the photic entrainment mechanism, suggesting that these ganglion cells may be the primary photoreceptors for this system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berson, David M -- Dunn, Felice A -- Takao, Motoharu -- EY12793/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1070-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Brown University, Providence, RI, 02912 USA. David_Berson@brown.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834835" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/ultrastructure ; *Biological Clocks ; *Circadian Rhythm ; Dendrites/ultrastructure ; Isoquinolines ; Kinetics ; Light ; *Light Signal Transduction ; Patch-Clamp Techniques ; Rats ; Rats, Sprague-Dawley ; Retinal Ganglion Cells/chemistry/cytology/*physiology ; Rod Opsins/analysis/physiology ; Suprachiasmatic Nucleus/cytology/*physiology
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  • 48
    Publication Date: 2002-08-24
    Description: Insulin secretion from intact mouse pancreatic islets was investigated with two-photon excitation imaging. Insulin granule exocytosis occurred mainly toward the interstitial space, away from blood vessels. The fusion pore was unusually stable with a lifetime of 1.8 seconds. Opening of the 1.4-nanometer-diameter pore was preceded by unrestricted lateral diffusion of lipids along the inner wall of the pore, supporting the idea that this structure is composed of membrane lipids. When the pore dilated to 12 nanometers, the granules rapidly flattened and discharged their contents. Thus, our methodology reveals fusion pore dynamics in intact tissues at nanometer resolution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takahashi, Noriko -- Kishimoto, Takuya -- Nemoto, Tomomi -- Kadowaki, Takashi -- Kasai, Haruo -- New York, N.Y. -- Science. 2002 Aug 23;297(5585):1349-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Physiology, National Institute for Physiological Sciences, and the Graduate University of Advanced Studies, Myodaiji, Okazaki 444-8585, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12193788" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/physiology/*ultrastructure ; Cell Polarity ; Colforsin/pharmacology ; Diffusion ; *Exocytosis ; Extracellular Space ; Fluorescence ; Glucose/pharmacology ; Guinea Pigs ; Image Processing, Computer-Assisted ; Insulin/*secretion ; Intracellular Membranes/physiology/ultrastructure ; Islets of Langerhans/blood supply/*physiology/secretion/*ultrastructure ; Kinetics ; Membrane Fusion ; Membrane Lipids/physiology ; Mice ; Mice, Inbred ICR ; Permeability ; Pyridinium Compounds ; Quaternary Ammonium Compounds ; Rhodamines ; Secretory Vesicles/physiology/*ultrastructure
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  • 49
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-12-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Vlas, Sake J -- Nagelkerke, Nico J D -- Jha, Prabhat -- Plummer, Frank A -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12481779" target="_blank"〉PubMed〈/a〉
    Keywords: Anti-HIV Agents/economics/*therapeutic use ; Child ; Developing Countries ; Drug Costs ; Drug Resistance, Viral ; Female ; HIV/drug effects/physiology ; HIV Infections/drug therapy/prevention & control/*transmission/virology ; Humans ; Infant ; Infant, Newborn ; Infectious Disease Transmission, Vertical/*prevention & control ; Pregnancy ; Pregnancy Complications, Infectious/drug therapy ; Viral Load
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  • 50
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-06
    Description: Often left out of news reports of cloned animals is the fact that for every 100 attempts, just two or three live offspring typically result. Now many researchers are going back to the lab to attempt to find out why. They are probing fundamental questions of cell biology, as well as trying to figure out whether there is something inherently flawed in "asexual" reproduction in mammals, or whether some problem lies in the in vitro component of the process. For now, the serious obstacles suggest that human cloning may be a long way off.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- Vogel, G -- New York, N.Y. -- Science. 2000 Jun 9;288(5472):1722-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10877684" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Domestic/embryology/genetics ; Animals, Genetically Modified ; Bioethics ; Cell Differentiation ; Cell Division ; *Cloning, Organism/adverse effects/economics/methods ; Embryo Transfer ; Embryo, Mammalian/cytology ; Female ; Gene Targeting ; Gene Transfer Techniques ; Humans ; Mice/embryology/genetics ; Nuclear Transfer Techniques ; Pregnancy ; Primates/embryology/genetics
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  • 51
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-09-02
    Description: Low success rates and unpredictable results have plagued cloning researchers, particularly those trying to clone pigs. Now, on page 1188, Japanese researchers offer the first scientific report of a cloned pig, named Xena, raising hopes that pigs could one day provide an unlimited supply of organs for transplantation thanks to their close physiological relationship to humans. But this week those hopes were dealt a blow by more evidence suggesting that pig retroviruses can infect human cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- Normile, D -- New York, N.Y. -- Science. 2000 Aug 18;289(5482):1118-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10970216" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Organism/*methods ; Embryo Transfer ; Female ; Fibroblasts/ultrastructure ; Japan ; Microinjections ; Nuclear Transfer Techniques ; Pregnancy ; *Swine/embryology/genetics ; Transplantation, Heterologous
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  • 52
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-08-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickelgren, I -- New York, N.Y. -- Science. 2000 Jul 7;289(5476):23-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10928921" target="_blank"〉PubMed〈/a〉
    Keywords: Aldosterone/metabolism ; Female ; Humans ; Hypertension/etiology/*genetics/metabolism ; Kidney/metabolism ; Male ; *Point Mutation ; Pregnancy ; Pregnancy Complications, Cardiovascular/etiology/metabolism ; Progesterone/*metabolism ; Protein Structure, Secondary ; Receptors, Mineralocorticoid/chemistry/*genetics/*metabolism ; Sodium Chloride/metabolism
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  • 53
    Publication Date: 2000-02-11
    Description: The deleterious effects of ethanol on the developing human brain are poorly understood. Here it is reported that ethanol, acting by a dual mechanism [blockade of N-methyl-D-aspartate (NMDA) glutamate receptors and excessive activation of GABA(A) receptors], triggers widespread apoptotic neurodegeneration in the developing rat forebrain. Vulnerability coincides with the period of synaptogenesis, which in humans extends from the sixth month of gestation to several years after birth. During this period, transient ethanol exposure can delete millions of neurons from the developing brain. This can explain the reduced brain mass and neurobehavioral disturbances associated with human fetal alcohol syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ikonomidou, C -- Bittigau, P -- Ishimaru, M J -- Wozniak, D F -- Koch, C -- Genz, K -- Price, M T -- Stefovska, V -- Horster, F -- Tenkova, T -- Dikranian, K -- Olney, J W -- AG 11355/AG/NIA NIH HHS/ -- DA 05072/DA/NIDA NIH HHS/ -- MH 38894/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1056-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatric Neurology, Charite, Virchow Clinics, Humboldt University, Augustenburger Platz 1, 13353 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669420" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Benzodiazepines/pharmacology ; Dose-Response Relationship, Drug ; Ethanol/administration & dosage/blood/*toxicity ; Female ; Fetal Alcohol Spectrum Disorders/*pathology ; GABA Modulators/pharmacology ; Humans ; *Nerve Degeneration ; Neurons/cytology/pathology ; Organ Size/drug effects ; Pregnancy ; Prosencephalon/cytology/*drug effects/embryology/growth & development ; Rats ; Rats, Sprague-Dawley ; Receptors, GABA-A/*drug effects/metabolism ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/*drug effects/metabolism ; Synapses/drug effects/physiology
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  • 54
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-07
    Description: In Neurospora crassa, white collar 1 (WC-1), a transcriptional activator and positive clock element, is rhythmically expressed from a nonrhythmic steady-state pool of wc-1 transcript, consistent with posttranscriptional regulation of rhythmicity. Mutations in frq influence both the level and periodicity of WC-1 expression, and driven FRQ expression not only depresses its own endogenous levels, but positively regulates WC-1 synthesis with a lag of about 8 hours, a delay similar to that seen in the wild-type clock. FRQ thus plays dual roles in the Neurospora clock and thereby, with WC-1, forms a second feedback loop that would promote robustness and stability in this circadian system. The existence also of interlocked loops in Drosophila melanogaster and mouse clocks suggests that such interlocked loops may be a conserved aspect of circadian timing systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, K -- Loros, J J -- Dunlap, J C -- MH44651/MH/NIMH NIH HHS/ -- R37-GM 34985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 7;289(5476):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Dartmouth Medical School, Hanover, NH 03755-3844, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10884222" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Circadian Rhythm ; DNA-Binding Proteins/biosynthesis/chemistry/genetics/*metabolism ; Darkness ; Feedback ; Fungal Proteins/genetics/*metabolism ; Gene Expression Regulation, Fungal ; Humans ; Kinetics ; Light ; Molecular Sequence Data ; Mutation ; Neurospora crassa/genetics/metabolism/*physiology ; Phosphorylation ; RNA, Fungal/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Sequence Alignment ; Signal Transduction ; Transcription Factors/biosynthesis/chemistry/genetics/*metabolism
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  • 55
    Publication Date: 2000-01-15
    Description: Primates that are identical in both nuclear and cytoplasmic components have not been produced by current cloning strategies, yet such identicals represent the ideal model for investigations of human diseases. Here, genetically identical nonhuman embryos were produced as twin and larger sets by separation and reaggregation of blastomeres of cleavage-stage embryos. A total of 368 multiples were created by the splitting of 107 rhesus embryos with four pregnancies established after 13 embryo transfers (31% versus 53% in vitro fertilization controls). The birth of Tetra, a healthy female cloned from a quarter of an embryo, proves that this approach can result in live offspring.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, A W -- Dominko, T -- Luetjens, C M -- Neuber, E -- Martinovich, C -- Hewitson, L -- Simerly, C R -- Schatten, G P -- New York, N.Y. -- Science. 2000 Jan 14;287(5451):317-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oregon Regional Primate Research Center, Beaverton, OR 97006, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10634789" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Blastocyst/physiology ; Blastomeres/*physiology ; Cleavage Stage, Ovum/*physiology ; Cloning, Organism/*methods ; Embryo Transfer ; *Embryonic and Fetal Development ; Female ; Macaca mulatta/*embryology ; Pregnancy ; Twins, Monozygotic ; Zona Pellucida/physiology
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  • 56
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ross, J A -- New York, N.Y. -- Science. 2000 Jan 21;287(5452):427.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10671164" target="_blank"〉PubMed〈/a〉
    Keywords: Child ; Data Collection ; Environmental Exposure/adverse effects ; Female ; Genetic Predisposition to Disease ; Humans ; Interviews as Topic ; Leukemia/etiology/genetics ; Neoplasms/*etiology/genetics ; Pregnancy ; Prenatal Exposure Delayed Effects
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  • 57
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-15
    Description: AIDS researchers are finding cheaper and simpler ways to slow the spread of HIV from mother to child, and more pregnant women, even in the poorest countries, have access to anti-HIV drugs and formula--thanks to the largesse of donors, discounts from industry, new trade laws, and the tenacity of individual clinicians. But just as researchers offer ways to clear one enormous hurdle--drug availability--they run smack into other ones, ranging from social stigmas that discourage testing to disinterest on the part of cash-strapped health authorities to a deeply ingrained culture of breast-feeding--often supported by government policy for otherwise sound health reasons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 2000 Jun 23;288(5474):2160-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10896599" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Serodiagnosis ; Africa South of the Sahara ; Anti-HIV Agents/*therapeutic use ; Breast Feeding/*adverse effects ; Clinical Trials as Topic ; Female ; HIV Infections/drug therapy/*prevention & control/*transmission ; Humans ; Infant, Newborn ; *Infectious Disease Transmission, Vertical ; Nevirapine/therapeutic use ; Pregnancy ; Pregnancy Complications, Infectious/*drug therapy ; Social Conditions ; Zidovudine/therapeutic use
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  • 58
    Publication Date: 2000-08-26
    Description: Prion proteins can serve as genetic elements by adopting distinct physical and functional states that are self-perpetuating and heritable. The critical region of one prion protein, Sup35, is initially unstructured in solution and then forms self-seeded amyloid fibers. We examined in vitro the mechanism by which this state is attained and replicated. Structurally fluid oligomeric complexes appear to be crucial intermediates in de novo amyloid nucleus formation. Rapid assembly ensues when these complexes conformationally convert upon association with nuclei. This model for replicating protein-based genetic information, nucleated conformational conversion, may be applicable to other protein assembly processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Serio, T R -- Cashikar, A G -- Kowal, A S -- Sawicki, G J -- Moslehi, J J -- Serpell, L -- Arnsdorf, M F -- Lindquist, S L -- GM025874/GM/NIGMS NIH HHS/ -- GM57840/GM/NIGMS NIH HHS/ -- P41-RR017777/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1317-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Cell Biology, Howard Hughes Medical Institute, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958771" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*chemistry ; Biopolymers/chemistry ; Centrifugation, Density Gradient ; Circular Dichroism ; Electrophoresis, Polyacrylamide Gel ; Endopeptidases/metabolism ; Fungal Proteins/*chemistry/metabolism/ultrastructure ; Kinetics ; Light ; Micelles ; Microscopy, Atomic Force ; Microscopy, Electron ; Models, Chemical ; Peptide Termination Factors ; Prions/*chemistry/metabolism/ultrastructure ; Protein Conformation ; Protein Folding ; *Saccharomyces cerevisiae Proteins ; Scattering, Radiation ; Solubility ; Sonication
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  • 59
    Publication Date: 2001-03-10
    Description: Assessing the energy costs of development in extreme environments is important for understanding how organisms can exist at the margins of the biosphere. Macromolecular turnover rates of RNA and protein were measured at -1.5 degrees C during early development of an Antarctic sea urchin. Contrary to expectations of low synthesis with low metabolism at low temperatures, protein and RNA synthesis rates exhibited temperature compensation and were equivalent to rates in temperate sea urchin embryos. High protein metabolism with a low metabolic rate is energetically possible in this Antarctic sea urchin because the energy cost of protein turnover, 0.45 joules per milligram of protein, is 1/25th the values reported for other animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marsh, A G -- Maxson , R E Jr -- Manahan, D T -- New York, N.Y. -- Science. 2001 Mar 9;291(5510):1950-2. Epub 2001 Feb 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11239152" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antarctic Regions ; Blastocyst/metabolism ; Cold Temperature ; Embryo, Nonmammalian/metabolism ; Energy Metabolism ; Half-Life ; Kinetics ; *Oxygen Consumption ; *Protein Biosynthesis ; Proteins/metabolism ; RNA/*biosynthesis/metabolism ; RNA, Messenger/biosynthesis/metabolism ; Sea Urchins/*embryology/growth & development/*metabolism ; Temperature
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  • 60
    Publication Date: 2001-07-07
    Description: The existence of a large number of receptors coupled to heterotrimeric guanine nucleotide binding proteins (G proteins) raises the question of how a particular receptor selectively regulates specific targets. We provide insight into this question by identifying a prototypical macromolecular signaling complex. The beta(2) adrenergic receptor was found to be directly associated with one of its ultimate effectors, the class C L-type calcium channel Ca(v)1.2. This complex also contained a G protein, an adenylyl cyclase, cyclic adenosine monophosphate-dependent protein kinase, and the counterbalancing phosphatase PP2A. Our electrophysiological recordings from hippocampal neurons demonstrate highly localized signal transduction from the receptor to the channel. The assembly of this signaling complex provides a mechanism that ensures specific and rapid signaling by a G protein-coupled receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davare, M A -- Avdonin, V -- Hall, D D -- Peden, E M -- Burette, A -- Weinberg, R J -- Horne, M C -- Hoshi, T -- Hell, J W -- AG00213/AG/NIA NIH HHS/ -- AG17502/AG/NIA NIH HHS/ -- GM08688/GM/NIGMS NIH HHS/ -- GM56900/GM/NIGMS NIH HHS/ -- HL61645/HL/NHLBI NIH HHS/ -- NS35563/NS/NINDS NIH HHS/ -- NS39444/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jul 6;293(5527):98-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11441182" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Adrenergic beta-2 Receptor Agonists ; Albuterol/pharmacology ; Animals ; Calcium Channels, L-Type/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Electric Conductivity ; Fluorescent Antibody Technique ; Heterotrimeric GTP-Binding Proteins/metabolism ; Humans ; Isoproterenol/pharmacology ; Kinetics ; Macromolecular Substances ; Neurons/cytology/drug effects/enzymology/metabolism ; Phosphoprotein Phosphatases/metabolism ; Precipitin Tests ; Prosencephalon/cytology/metabolism ; Protein Binding ; Pyramidal Cells/cytology/drug effects/enzymology/metabolism ; Rats ; Receptors, Adrenergic, beta-2/genetics/*metabolism ; *Signal Transduction ; Substrate Specificity
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  • 61
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-02-07
    Description: We describe a heptameric protein pore that has been engineered to accommodate two different cyclodextrin adapters simultaneously within the lumen of a transmembrane beta barrel. The volume between the adapters is a cavity of approximately 4400 cubic angstroms. Analysis of single-channel recordings reveals that individual charged organic molecules can be pulled into the cavity by an electrical potential. Once trapped, an organic molecule shuttles back and forth between the adapters for hundreds of milliseconds. Such self-assembling nanostructures are of interest for the fabrication of multianalyte sensors and could provide a means to control chemical reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gu, L Q -- Cheley, S -- Bayley, H -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):636-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Biochemistry and Genetics, Texas A&M University System Health Science Center, College Station, TX 77843, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158673" target="_blank"〉PubMed〈/a〉
    Keywords: Adamantane/*analogs & derivatives/*chemistry/metabolism ; Bacterial Toxins/*chemistry/metabolism ; Binding Sites ; Cyclodextrins/*chemistry/metabolism ; Dicarboxylic Acids/*chemistry/metabolism ; Electric Conductivity ; Hemolysin Proteins/*chemistry/metabolism ; Kinetics ; Membrane Potentials ; Models, Molecular ; Mutagenesis, Site-Directed ; Protein Conformation ; *Protein Engineering ; Thermodynamics ; *beta-Cyclodextrins
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  • 62
    Publication Date: 2001-10-27
    Description: Single-molecule imaging techniques were used to reveal the binding of individual cyclic adenosine 3',5'-monophosphate molecules to heterotrimeric guanine nucleotide-binding protein coupled receptors on the surface of living Dictyostelium discoideum cells. The binding sites were uniformly distributed and diffused rapidly in the plane of the membrane. The probabilities of individual association and dissociation events were greater for receptors at the anterior end of the cell. Agonist-induced receptor phosphorylation had little effect on any of the monitored properties, whereas G protein coupling influenced the binding kinetics. These observations illustrate the dynamic properties of receptors involved in gradient sensing and suggest that these may be polarized in chemotactic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ueda, M -- Sako, Y -- Tanaka, T -- Devreotes, P -- Yanagida, T -- New York, N.Y. -- Science. 2001 Oct 26;294(5543):864-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Recognition and Formation, Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Corporation (JST)., Osaka 562-0035, Japan. ueda@phys1.med.osaka-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11679673" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbocyanines/metabolism ; Cell Membrane/metabolism ; *Chemotaxis ; Cyclic AMP/*metabolism ; Dictyostelium/cytology/genetics/metabolism/*physiology ; Diffusion ; Guanosine Diphosphate/pharmacology ; Guanosine Triphosphate/pharmacology ; Heterotrimeric GTP-Binding Proteins/genetics/*metabolism ; Kinetics ; Microscopy, Fluorescence ; Mutation ; Phosphorylation ; Pseudopodia/metabolism ; Receptors, Cyclic AMP/*metabolism ; *Signal Transduction
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  • 63
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-01-06
    Description: Neurons encode information and communicate via action potentials, which are generated following the summation of synaptic events. It is commonly assumed that action potentials reset the membrane potential completely, allowing another round of synaptic integration to begin. We show here that the conductances underlying the action potential act instead as a variable reset of synaptic integration. The strength of this reset is cell type-specific and depends on the kinetics, location, and timing of the synaptic input. As a consequence, distal synapses, as well as inputs mediated by N-methyl-d-aspartate receptor activation, can contribute disproportionately to synaptic integration during action potential firing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hausser, M -- Major, G -- Stuart, G J -- New York, N.Y. -- Science. 2001 Jan 5;291(5501):138-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University College London, Gower Street, London WC1E 6BT, UK. m.hausser@ucl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11141567" target="_blank"〉PubMed〈/a〉
    Keywords: *Action Potentials/drug effects ; Animals ; Computer Simulation ; Dendrites/drug effects/physiology ; Electric Stimulation ; *Excitatory Postsynaptic Potentials/drug effects ; Kinetics ; Magnesium/pharmacology ; Models, Neurological ; Neocortex/cytology/physiology ; Patch-Clamp Techniques ; Purkinje Cells/*physiology ; Pyramidal Cells/*physiology ; Rats ; Receptors, AMPA/physiology ; Receptors, N-Methyl-D-Aspartate/physiology ; Synapses/physiology ; *Synaptic Transmission ; Tetrodotoxin/pharmacology
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  • 64
    Publication Date: 2001-04-28
    Description: Here we use mechanical force to induce the unfolding and refolding of single RNA molecules: a simple RNA hairpin, a molecule containing a three-helix junction, and the P5abc domain of the Tetrahymena thermophila ribozyme. All three molecules (P5abc only in the absence of Mg2+) can be mechanically unfolded at equilibrium, and when kept at constant force within a critical force range, are bi-stable and hop between folded and unfolded states. We determine the force-dependent equilibrium constants for folding/unfolding these single RNA molecules and the positions of their transition states along the reaction coordinate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liphardt, J -- Onoa, B -- Smith, S B -- Tinoco, I Jr -- Bustamante, C -- GM-10840/GM/NIGMS NIH HHS/ -- GM-32543/GM/NIGMS NIH HHS/ -- R01 GM010840/GM/NIGMS NIH HHS/ -- R01 GM010840-42/GM/NIGMS NIH HHS/ -- R01 GM010840-43/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Apr 27;292(5517):733-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA. jliphard@alice.berkeley.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11326101" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Edetic Acid ; Kinetics ; Magnesium ; Microspheres ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Polystyrenes ; RNA/*chemistry ; RNA Stability ; RNA, Catalytic/*chemistry ; Stress, Mechanical ; Tetrahymena thermophila ; Thermodynamics
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  • 65
    Publication Date: 2001-12-12
    Description: Calcium (Ca2+) influx through Ca2+-permeable ion channels plays a pivotal role in a variety of neuronal signaling processes, and negative-feedback control of this influx by Ca2+ itself is often equally important for modulation of such signaling. Negative modulation by Ca2+ through calmodulin (CaM) on cyclic nucleotide-gated (CNG) channels underlies the adaptation of olfactory receptor neurons to odorants. We show that this feedback requires two additional subunits of the native olfactory channel, CNGA4 and CNGB1b, even though the machinery for CaM binding and modulation is present in the principal subunit CNGA2. This provides a rationale for the presence of three distinct subunits in the native olfactory channel and underscores the subtle link between the molecular make-up of an ion channel and the physiological function it subserves.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradley, J -- Reuter, D -- Frings, S -- New York, N.Y. -- Science. 2001 Dec 7;294(5549):2176-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Biologische Informationsverarbeitung, Forschungszentrum Julich, 52425 Julich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11739960" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Physiological ; Animals ; Calcium/metabolism/pharmacology ; Calcium Signaling ; Calmodulin/*metabolism/pharmacology ; Cell Line ; Cyclic AMP/*metabolism ; Cyclic Nucleotide-Gated Cation Channels ; Feedback, Physiological ; Humans ; Ion Channel Gating ; Ion Channels/metabolism/*physiology ; Kinetics ; *Odors ; Olfactory Receptor Neurons/*physiology ; Patch-Clamp Techniques ; Photolysis ; Protein Subunits ; Rats ; Recombinant Proteins/metabolism
    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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  • 66
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-09-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duffy, P E -- Fried, M -- New York, N.Y. -- Science. 2001 Sep 14;293(5537):2009-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Seattle Biomedical Research Institute, Seattle, WA 98109, USA. pduffy@sbri.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11557864" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Protozoan/immunology ; Cell Adhesion ; Chondroitin Sulfates/metabolism ; Erythrocytes/metabolism/*parasitology ; Female ; Humans ; Hyaluronic Acid/metabolism ; Immunoglobulin G/immunology/*metabolism ; Malaria Vaccines ; Malaria, Falciparum/immunology/*parasitology/prevention & control ; Placenta/metabolism/parasitology ; Placenta Diseases/immunology/parasitology ; Plasmodium falciparum/immunology ; Pregnancy ; Pregnancy Complications, Parasitic/immunology/*parasitology/prevention & control ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry/immunology/*metabolism ; Receptors, Fc/*metabolism ; Trophoblasts/immunology/metabolism/parasitology
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  • 67
    Publication Date: 2001-12-12
    Description: Heteromultimeric cyclic nucleotide-gated (CNG) channels play a central role in the transduction of odorant signals and subsequent adaptation. The contributions of individual subunits to native channel function in olfactory receptor neurons remain unclear. Here, we show that the targeted deletion of the mouse CNGA4 gene, which encodes a modulatory CNG subunit, results in a defect in odorant-dependent adaptation. Channels in excised membrane patches from the CNGA4 null mouse exhibited slower Ca2+-calmodulin-mediated channel desensitization. Thus, the CNGA4 subunit accelerates the Ca2+-mediated negative feedback in olfactory signaling and allows rapid adaptation in this sensory system.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885906/" 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/PMC2885906/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Munger, S D -- Lane, A P -- Zhong, H -- Leinders-Zufall, T -- Yau, K W -- Zufall, F -- Reed, R R -- R37 EY006837/EY/NEI NIH HHS/ -- R37 EY006837-13/EY/NEI NIH HHS/ -- R37 EY006837-14/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2001 Dec 7;294(5549):2172-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11739959" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; *Adaptation, Physiological ; Animals ; Calcium/*metabolism ; Calcium Signaling ; Calmodulin/*metabolism ; Cyclic AMP/metabolism ; Cyclic Nucleotide-Gated Cation Channels ; Cyclohexanols/pharmacology ; Electrophysiology ; Gene Targeting ; Ion Channel Gating ; Ion Channels/*genetics/*physiology ; Kinetics ; Mice ; Mice, Inbred C57BL ; *Monoterpenes ; *Odors ; Olfactory Bulb/physiology ; Olfactory Mucosa/physiology ; Olfactory Receptor Neurons/metabolism/*physiology ; Protein Subunits ; Terpenes/pharmacology
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  • 68
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vogel, G -- New York, N.Y. -- Science. 2001 Jan 12;291(5502):226.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11253205" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Genetically Modified ; Embryo Transfer ; Female ; Gene Expression ; Gene Transfer Techniques ; Gene Transfer, Horizontal ; Green Fluorescent Proteins ; Luminescent Proteins/*genetics ; Macaca mulatta/*genetics ; Male ; Pregnancy ; Sperm Injections, Intracytoplasmic
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  • 69
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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〉Couzin, Jennifer -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1538.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12446883" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/*metabolism ; Computer Simulation ; Fluorescent Dyes ; Genes ; Kinetics ; Microscopy ; Models, Genetic ; Pol1 Transcription Initiation Complex Proteins/metabolism ; RNA Polymerase I/*metabolism ; RNA Polymerase II/metabolism ; *Transcription, Genetic
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  • 70
    Publication Date: 2002-01-05
    Description: The presence of galactose alpha-1,3-galactose residues on the surface of pig cells is a major obstacle to successful xenotransplantation. Here, we report the production of four live pigs in which one allele of the alpha-1,3-galactosyltransferase locus has been knocked out. These pigs were produced by nuclear transfer technology; clonal fetal fibroblast cell lines were used as nuclear donors for embryos reconstructed with enucleated pig oocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lai, Liangxue -- Kolber-Simonds, Donna -- Park, Kwang-Wook -- Cheong, Hee-Tae -- Greenstein, Julia L -- Im, Gi-Sun -- Samuel, Melissa -- Bonk, Aaron -- Rieke, August -- Day, Billy N -- Murphy, Clifton N -- Carter, David B -- Hawley, Robert J -- Prather, Randall S -- R44 RR15198/RR/NCRR NIH HHS/ -- T32 RR07004/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1089-92. Epub 2002 Jan 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Science, University of Missouri, Columbia, MO 65211, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778012" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; *Animals, Genetically Modified ; Cell Line ; *Cloning, Organism ; Embryo Transfer ; Female ; Fetus ; Fibroblasts ; Galactosyltransferases/*genetics ; *Gene Targeting ; Genetic Vectors ; Male ; Mutagenesis, Insertional ; Nuclear Transfer Techniques ; Pregnancy ; Recombination, Genetic ; Swine ; Swine, Miniature/embryology/*genetics ; Transfection
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  • 71
    Publication Date: 2002-03-16
    Description: We analyzed the technical basis for a major global program to reduce disease among the poor. Effective interventions exist against the few diseases which most account for excess mortality among the poor. Achieving high coverage of effective interventions requires a well-functioning health system, as well as overcoming a set of financial and nonfinancial constraints. The annual incremental cost would be between $40 billion and $52 billion by 2015 in 83 low-income and sub-Saharan African countries. Such a program is feasible and would avoid millions of child, maternal, and adult deaths annually in poor countries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jha, Prabhat -- Mills, Anne -- Hanson, Kara -- Kumaranayake, Lilani -- Conteh, Lesong -- Kurowski, Christoph -- Nguyen, Son Nam -- Cruz, Valeria Oliveira -- Ranson, Kent -- Vaz, Lara M E -- Yu, Shengchao -- Morton, Oliver -- Sachs, Jeffrey D -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2036-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉World Health Organization (WHO), Geneva 01220, Switzerland. jhap@who.int〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896266" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Child ; *Delivery of Health Care/economics ; Female ; *Global Health ; Government ; Health Care Costs ; *Health Expenditures ; Health Services Accessibility ; *Health Status ; Humans ; Immunization Programs/economics ; *Medically Underserved Area ; *Poverty ; Pregnancy ; Preventive Health Services/economics ; Public Policy
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  • 72
    Publication Date: 2002-04-16
    Description: A practical, inexpensive, green chemical process for degrading environmental pollutants is greatly needed, especially for persistent chlorinated pollutants. Here we describe the activation of hydrogen peroxide by tetraamidomacrocylic ligand (TAML) iron catalysts, to destroy the priority pollutants pentachlorophenol (PCP) and 2,4,6-trichlorophenol (TCP). In water, in minutes, under ambient conditions of temperature and pressure, PCP and TCP are completely destroyed at catalyst:substrate ratios of 1:715 and 1:2000, respectively. The fate of about 90% of the carbon and about 99% of the chlorine has been determined in each case. Neither dioxins nor any other toxic compounds are detectable products, and the catalysts themselves show low toxicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gupta, Sayam Sen -- Stadler, Matthew -- Noser, Christopher A -- Ghosh, Anindya -- Steinhoff, Bradley -- Lenoir, Dieter -- Horwitz, Colin P -- Schramm, Karl-Werner -- Collins, Terrence J -- GM44867-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):326-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA 15213, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11951040" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Chlorine Compounds/chemistry ; Chlorophenols/*chemistry ; Dioxins/chemistry ; Environmental Pollutants ; Ferric Compounds/*chemistry/toxicity ; Gas Chromatography-Mass Spectrometry ; Heterocyclic Compounds with 4 or More Rings/*chemistry/toxicity ; Hydrogen Peroxide/*chemistry ; Hydrogen-Ion Concentration ; Kinetics ; Magnetic Resonance Spectroscopy ; Oxidation-Reduction ; Pentachlorophenol/*chemistry ; Pressure ; Spectrometry, Mass, Electrospray Ionization ; Temperature
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  • 73
    Publication Date: 2002-11-26
    Description: We have analyzed the kinetics of assembly and elongation of the mammalian RNA polymerase I complex on endogenous ribosomal genes in the nuclei of living cells with the use of in vivo microscopy. We show that components of the RNA polymerase I machinery are brought to ribosomal genes as distinct subunits and that assembly occurs via metastable intermediates. With the use of computational modeling of imaging data, we have determined the in vivo elongation time of the polymerase, and measurements of recruitment and incorporation frequencies show that incorporation of components into the assembling polymerase is inefficient. Our data provide a kinetic and mechanistic framework for the function of a mammalian RNA polymerase in living cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dundr, Miroslav -- Hoffmann-Rohrer, Urs -- Hu, Qiyue -- Grummt, Ingrid -- Rothblum, Lawrence I -- Phair, Robert D -- Misteli, Tom -- New York, N.Y. -- Science. 2002 Nov 22;298(5598):1623-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute (NCI), 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/12446911" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalytic Domain ; Cell Line ; Cell Nucleolus/metabolism ; Cell Nucleus/*metabolism ; Computer Simulation ; DNA, Ribosomal/genetics ; Fluorescence ; Fluorescence Recovery After Photobleaching ; Fluorescent Dyes ; Green Fluorescent Proteins ; Haplorhini ; Humans ; In Situ Hybridization, Fluorescence ; Kinetics ; Least-Squares Analysis ; Luminescent Proteins ; Microscopy ; Pol1 Transcription Initiation Complex Proteins/metabolism ; Probability ; Promoter Regions, Genetic ; Protein Subunits ; RNA Polymerase I/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Transcription, Genetic ; Transfection
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  • 74
    Publication Date: 2002-08-31
    Description: The latitudinal gradient of increasing biodiversity from poles to equator is one of the most prominent but least understood features of life on Earth. Here we show that species diversity can be predicted from the biochemical kinetics of metabolism. We first demonstrate that the average energy flux of populations is temperature invariant. We then derive a model that quantitatively predicts how species diversity increases with environmental temperature. Predictions are supported by data for terrestrial, freshwater, and marine taxa along latitudinal and elevational gradients. These results establish a thermodynamic basis for the regulation of species diversity and the organization of ecological communities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allen, Andrew P -- Brown, James H -- Gillooly, James F -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1545-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of New Mexico, Albuquerque, NM 87131, USA. drewa@unm.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202828" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Constitution ; *Ecosystem ; Kinetics ; *Models, Biological ; Plants ; Temperature ; Thermodynamics
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  • 75
    Publication Date: 2002-01-19
    Description: The separate components of nucleocytoplasmic transport have been well characterized, including the key regulatory role of Ran, a guanine nucleotide triphosphatase. However, the overall system behavior in intact cells is difficult to analyze because the dynamics of these components are interdependent. We used a combined experimental and computational approach to study Ran transport in vivo. The resulting model provides the first quantitative picture of Ran flux between the nuclear and cytoplasmic compartments in eukaryotic cells. The model predicts that the Ran exchange factor RCC1, and not the flux capacity of the nuclear pore complex (NPC), is the crucial regulator of steady-state flux across the NPC. Moreover, it provides the first estimate of the total in vivo flux (520 molecules per NPC per second and predicts that the transport system is robust.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, Alicia E -- Slepchenko, Boris M -- Schaff, James C -- Loew, Leslie M -- Macara, Ian G -- GM-50526/GM/NIGMS NIH HHS/ -- NCRR-RR13186/RR/NCRR NIH HHS/ -- NIH-GM-20438/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):488-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cell Signaling, Department of Pharmacology, University of Virginia, Charlottesville, VA 22908, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799242" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; *Cell Cycle Proteins ; Cell Line ; Cell Nucleus/metabolism ; *Computer Simulation ; Cricetinae ; Cytoplasm/metabolism ; Diffusion ; Fluorescence ; Guanine Nucleotide Exchange Factors/metabolism ; Guanosine Triphosphate/metabolism ; Kinetics ; Mathematics ; *Models, Biological ; Mutation ; Nuclear Pore/*metabolism ; *Nuclear Proteins ; Nucleocytoplasmic Transport Proteins/metabolism ; Recombinant Proteins/metabolism ; Temperature ; ran GTP-Binding Protein/genetics/*metabolism
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  • 76
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-09-01
    Description: The vomeronasal organ (VNO) of mammals plays an essential role in the detection of pheromones. We obtained simultaneous recordings of action potentials from large subsets of VNO neurons. These cells responded to components of urine by increasing their firing rate. This chemosensory activation required phospholipase C function. Unlike most other sensory neurons, VNO neurons did not adapt under prolonged stimulus exposure. The full time course of the VNO spiking response is captured by a simple quantitative model of ligand binding. Many individual VNO neurons were strongly selective for either male or female mouse urine, with the effective concentrations differing as much as a thousandfold. These results establish a framework for understanding sensory coding in the vomeronasal system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holy, T E -- Dulac, C -- Meister, M -- New York, N.Y. -- Science. 2000 Sep 1;289(5484):1569-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA. timholy@mcb.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10968796" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Chemoreceptor Cells/metabolism ; Female ; Kinetics ; Ligands ; Male ; Mice ; Mice, Inbred DBA ; Models, Biological ; Neurons, Afferent/*physiology ; Pheromones/physiology/*urine ; Potassium/pharmacology ; Signal Transduction ; Type C Phospholipases/antagonists & inhibitors/metabolism ; Urine ; Vomeronasal Organ/*physiology
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  • 77
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-06
    Description: Diatoms are a key component of marine ecosystems and are extremely important for the biogeochemical cycling of silica and as contributors to global fixed carbon. However, the answers to fundamental questions such as what diatoms can sense in their environment, how they respond to external signals, and what factors control their life strategies are largely unknown. We generated transgenic diatom cells containing the calcium-sensitive photoprotein aequorin to determine whether changes in calcium homeostasis are used to respond to relevant environmental stimuli. Our results reveal sensing systems for detecting and responding to fluid motion (shear stress), osmotic stress, and iron, a key nutrient that controls diatom abundance in the ocean.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Falciatore, A -- d'Alcala, M R -- Croot, P -- Bowler, C -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories of Molecular Plant Biology and Biological Oceanography, Stazione Zoologica Anton Dohrn, Villa Comunale, I-80121 Naples, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875921" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptation, Physiological ; Aequorin/genetics/metabolism ; Biological Transport ; Calcium/*metabolism ; *Calcium Signaling ; Chlorides ; Culture Media ; Diatoms/genetics/*physiology ; Ferric Compounds/metabolism ; Homeostasis ; Hydrogen-Ion Concentration ; Iron/metabolism ; Kinetics ; Osmolar Concentration ; Osmotic Pressure ; Seawater ; Stress, Mechanical ; Transformation, Genetic ; Transgenes
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 78
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2000-07-06
    Description: In 1998, an anonymous millionaire, hoping to clone his pet dog Missy, awarded a Texas A&M University animal scientist $2.3 million to develop the necessary techniques. Now several companies are cashing in on the boom in frozen-tissue storage of pets for future cloning.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 2000 Jun 9;288(5472):1726.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10877685" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cats/embryology/genetics ; Cloning, Organism/*economics/methods ; Costs and Cost Analysis ; *Dogs/embryology/genetics ; Female ; Pregnancy ; Tissue Preservation
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  • 79
    Publication Date: 2000-09-16
    Description: In excitable cells, small-conductance Ca2+-activated potassium channels (SK channels) are responsible for the slow after-hyperpolarization that often follows an action potential. Three SK channel subunits have been molecularly characterized. The SK3 gene was targeted by homologous recombination for the insertion of a gene switch that permitted experimental regulation of SK3 expression while retaining normal SK3 promoter function. An absence of SK3 did not present overt phenotypic consequences. However, SK3 overexpression induced abnormal respiratory responses to hypoxia and compromised parturition. Both conditions were corrected by silencing the gene. The results implicate SK3 channels as potential therapeutic targets for disorders such as sleep apnea or sudden infant death syndrome and for regulating uterine contractions during labor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bond, C T -- Sprengel, R -- Bissonnette, J M -- Kaufmann, W A -- Pribnow, D -- Neelands, T -- Storck, T -- Baetscher, M -- Jerecic, J -- Maylie, J -- Knaus, H G -- Seeburg, P H -- Adelman, J P -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1942-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Department of Obstetrics and Gynecology, Oregon Health Sciences University, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10988076" target="_blank"〉PubMed〈/a〉
    Keywords: 5' Untranslated Regions ; Action Potentials ; Animals ; Anoxia/metabolism ; Brain/metabolism ; Crosses, Genetic ; Culture Techniques ; Doxycycline/pharmacology ; Female ; Gene Expression ; Gene Expression Regulation/drug effects ; Gene Targeting ; Labor, Obstetric/*physiology ; Male ; Mice ; Mice, Inbred C57BL ; Muscle, Skeletal/metabolism ; Potassium Channels/genetics/*physiology ; *Potassium Channels, Calcium-Activated ; Pregnancy ; *Respiratory Physiological Phenomena ; Small-Conductance Calcium-Activated Potassium Channels
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  • 80
    Publication Date: 2000-02-05
    Description: A system for direct pharmacologic control of protein secretion was developed to allow rapid and pulsatile delivery of therapeutic proteins. A protein was engineered so that it accumulated as aggregates in the endoplasmic reticulum. Secretion was then stimulated by a synthetic small-molecule drug that induces protein disaggregation. Rapid and transient secretion of growth hormone and insulin was achieved in vitro and in vivo. A regulated pulse of insulin secretion resulted in a transient correction of serum glucose concentrations in a mouse model of hyperglycemia. This approach may make gene therapy a viable method for delivery of polypeptides that require rapid and regulated delivery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rivera, V M -- Wang, X -- Wardwell, S -- Courage, N L -- Volchuk, A -- Keenan, T -- Holt, D A -- Gilman, M -- Orci, L -- Cerasoli, F Jr -- Rothman, J E -- Clackson, T -- New York, N.Y. -- Science. 2000 Feb 4;287(5454):826-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ARIAD Gene Therapeutics, 26 Landsdowne Street, Cambridge, MA 02139, USA. vrivera@ariad.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10657290" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Glucose/metabolism ; Cell Line ; Diabetes Mellitus, Experimental/drug therapy/metabolism ; Drug Delivery Systems ; Endoplasmic Reticulum/*metabolism/secretion ; Furin ; Genetic Therapy ; Golgi Apparatus/metabolism ; Human Growth Hormone/chemistry/metabolism/secretion ; Humans ; Immunophilins/chemistry/genetics/metabolism ; Insulin/secretion ; Kinetics ; Ligands ; Mice ; Proinsulin/chemistry/metabolism ; Protein Engineering ; Recombinant Fusion Proteins/*chemistry/*metabolism/secretion ; Subtilisins/metabolism ; Tacrolimus Binding Proteins ; Tumor Cells, Cultured
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  • 81
    Publication Date: 2000-06-17
    Description: Using fluorescence microscopy, we studied the catalysis by and folding of individual Tetrahymena thermophila ribozyme molecules. The dye-labeled and surface-immobilized ribozymes used were shown to be functionally indistinguishable from the unmodified free ribozyme in solution. A reversible local folding step in which a duplex docks and undocks from the ribozyme core was observed directly in single-molecule time trajectories, allowing the determination of the rate constants and characterization of the transition state. A rarely populated docked state, not measurable by ensemble methods, was observed. In the overall folding process, intermediate folding states and multiple folding pathways were observed. In addition to observing previously established folding pathways, a pathway with an observed folding rate constant of 1 per second was discovered. These results establish single-molecule fluorescence as a powerful tool for examining RNA folding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhuang, X -- Bartley, L E -- Babcock, H P -- Russell, R -- Ha, T -- Herschlag, D -- Chu, S -- GM49423/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jun 16;288(5473):2048-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Stanford University, Stanford, CA 94305-4060, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10856219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biotinylation ; Carbocyanines ; Catalysis ; Fluorescent Dyes ; Guanosine/metabolism ; Kinetics ; Microscopy, Fluorescence ; Models, Molecular ; *Nucleic Acid Conformation ; Oligoribonucleotides/metabolism ; RNA, Catalytic/*chemistry/*metabolism ; RNA, Protozoan/*chemistry/metabolism ; Tetrahymena thermophila
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  • 82
    Publication Date: 2001-05-12
    Description: In eukaryotic cells, microtubules and their associated motor proteins can be organized into various large-scale patterns. Using a simplified experimental system combined with computer simulations, we examined how the concentrations and kinetic parameters of the motors contribute to their collective behavior. We observed self-organization of generic steady-state structures such as asters, vortices, and a network of interconnected poles. We identified parameter combinations that determine the generation of each of these structures. In general, this approach may become useful for correlating the morphogenetic phenomena taking place in a biological system with the biophysical characteristics of its constituents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Surrey, T -- Nedelec, F -- Leibler, S -- Karsenti, E -- New York, N.Y. -- Science. 2001 May 11;292(5519):1167-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Biophysics Program, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11349149" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Antibodies ; Biopolymers/chemistry/metabolism ; *Computer Simulation ; *Drosophila Proteins ; Guanosine Triphosphate/metabolism ; Kinesin/chemistry/metabolism ; Kinetics ; Macromolecular Substances ; Microtubules/*chemistry/drug effects/*metabolism ; Models, Molecular ; Molecular Motor Proteins/*chemistry/*metabolism ; Paclitaxel/pharmacology ; Protein Structure, Quaternary/drug effects ; Tubulin/chemistry/metabolism ; Viscosity
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  • 83
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-03-28
    Description: The human genome encodes 30,000 to 40,000 proteins, and a major challenge is to understand how posttranslational events, such as glycosylation, affect the activities and functions of these proteins in health and disease. Glycosylated proteins are ubiquitous components of extracellular matrices and cellular surfaces where their oligosaccharide moieties are implicated in a wide range of cell-cell and cell-matrix recognition events. The power of ultrahigh-sensitivity mass spectrometric strategies for defining the primary structures of highly complex mixtures of glycoprotein glycoforms is set to revolutionize structural glycobiology in the coming postgenomic era.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dell, A -- Morris, H R -- New York, N.Y. -- Science. 2001 Mar 23;291(5512):2351-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, UK. a.dell@ic.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11269315" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbohydrate Metabolism, Inborn Errors/metabolism ; Female ; Glycoproteins/*chemistry/metabolism ; Glycosylation ; Humans ; *Mass Spectrometry/methods ; Mucins/chemistry ; Pregnancy ; Pregnancy Proteins/chemistry/metabolism ; Prions/chemistry/metabolism ; Protein Processing, Post-Translational ; Spectrometry, Mass, Electrospray Ionization ; Spectrometry, Mass, Fast Atom Bombardment ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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  • 84
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2001-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pickrell, J -- New York, N.Y. -- Science. 2001 Mar 16;291(5511):2061-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11256389" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cloning, Organism/adverse effects ; Female ; Humans ; Internationality ; Male ; Oligospermia ; Pregnancy ; Pregnancy Complications ; Surrogate Mothers
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  • 85
    Publication Date: 2001-02-07
    Description: The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5'-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5'-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kawaguchi, K -- Ishiwata, S -- New York, N.Y. -- Science. 2001 Jan 26;291(5504):667-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, School of Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11158681" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/*metabolism ; Adenosine Triphosphate/metabolism ; Adenylyl Imidodiphosphate/*metabolism ; Animals ; Cattle ; Elasticity ; Kinesin/*metabolism ; Kinetics ; Microtubules/metabolism ; Models, Biological ; Swine
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  • 86
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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〉Enserink, M -- New York, N.Y. -- Science. 2001 Dec 14;294(5550):2271.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11743176" target="_blank"〉PubMed〈/a〉
    Keywords: *Bedding and Linens ; Child ; Female ; Humans ; Infant ; *Insecticides ; Kenya ; Malaria/*prevention & control/*transmission ; Mosquito Control ; *Permethrin ; Placenta Diseases/parasitology/prevention & control ; Pregnancy ; Pregnancy Complications, Parasitic/prevention & control ; Randomized Controlled Trials as Topic
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  • 87
    Publication Date: 2001-10-06
    Description: Oligonucleotide microarrays were used to map the detailed topography of chromosome replication in the budding yeast Saccharomyces cerevisiae. The times of replication of thousands of sites across the genome were determined by hybridizing replicated and unreplicated DNAs, isolated at different times in S phase, to the microarrays. Origin activations take place continuously throughout S phase but with most firings near mid-S phase. Rates of replication fork movement vary greatly from region to region in the genome. The two ends of each of the 16 chromosomes are highly correlated in their times of replication. This microarray approach is readily applicable to other organisms, including humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raghuraman, M K -- Winzeler, E A -- Collingwood, D -- Hunt, S -- Wodicka, L -- Conway, A -- Lockhart, D J -- Davis, R W -- Brewer, B J -- Fangman, W L -- New York, N.Y. -- Science. 2001 Oct 5;294(5540):115-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Department of Mathematics, University of Washington, Seattle, WA 98195, USA. raghu@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11588253" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Base Sequence ; Centromere/metabolism ; Chromosomes, Fungal/genetics/*metabolism ; *DNA Replication ; DNA, Fungal/*biosynthesis/genetics/metabolism ; DNA, Intergenic ; Fourier Analysis ; *Genome, Fungal ; Kinetics ; Nucleic Acid Hybridization ; Oligonucleotide Array Sequence Analysis ; *Replication Origin ; *S Phase ; Saccharomyces cerevisiae/cytology/*genetics/metabolism ; Telomere/metabolism ; Transcription, Genetic
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  • 88
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2002-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, Jocelyn -- New York, N.Y. -- Science. 2002 Jan 4;295(5552):25-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11778016" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; *Cloning, Organism ; Embryo Transfer ; Female ; Galactosyltransferases/*genetics/immunology ; Genetic Vectors ; Graft Rejection/*prevention & control ; Humans ; Pregnancy ; Swine/*genetics ; *Transplantation, Heterologous
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  • 89
    Publication Date: 2002-08-06
    Description: The vibrational dynamics of the retinal chromophore all-trans-to-13-cis photoisomerization in bacteriorhodopsin has been studied with mid-infrared absorption spectroscopy at high time resolution (about 200 femtoseconds). After photoexcitation of light-adapted bacteriorhodopsin, the transient infrared absorption was probed in a broad spectral region, including vibrations with dominant C-C, C=C, and C=NH stretching mode amplitude. All photoproduct modes, especially those around 1190 reciprocal-centimeters that are indicative for a 13-cis configuration of the chromophore, rise with a time constant of approximately 0.5 picosecond. The results presented give direct vibrational-spectroscopic evidence for the isomerization taking place within 0.5 picosecond, as has been suggested by previous optical femtosecond time-resolved experiments but questioned recently by picosecond time-resolved vibrational spectroscopy experiments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herbst, Johannes -- Heyne, Karsten -- Diller, Rolf -- New York, N.Y. -- Science. 2002 Aug 2;297(5582):822-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Experimentalphysik, Freie Universitat Berlin, Arnimallee 14, 14195 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12161649" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriorhodopsins/*chemistry/*metabolism ; Binding Sites ; Isomerism ; Kinetics ; Light ; Photochemistry ; Retinaldehyde/*chemistry/*metabolism ; Spectrophotometry, Infrared/*methods ; Spectroscopy, Fourier Transform Infrared ; Time Factors ; Vibration
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  • 90
    Publication Date: 2002-05-25
    Description: Pyrrolysine is a lysine derivative encoded by the UAG codon in methylamine methyltransferase genes of Methanosarcina barkeri. Near a methyltransferase gene cluster is the pylT gene, which encodes an unusual transfer RNA (tRNA) with a CUA anticodon. The adjacent pylS gene encodes a class II aminoacyl-tRNA synthetase that charges the pylT-derived tRNA with lysine but is not closely related to known lysyl-tRNA synthetases. Homologs of pylS and pylT are found in a Gram-positive bacterium. Charging a tRNA(CUA) with lysine is a likely first step in translating UAG amber codons as pyrrolysine in certain methanogens. Our results indicate that pyrrolysine is the 22nd genetically encoded natural amino acid.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srinivasan, Gayathri -- James, Carey M -- Krzycki, Joseph A -- New York, N.Y. -- Science. 2002 May 24;296(5572):1459-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Ohio State University, Columbus, OH 43210, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12029131" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acyl-tRNA Synthetases/chemistry/*genetics/metabolism ; Anticodon ; Archaeal Proteins ; Base Sequence ; Catalytic Domain ; *Codon ; Codon, Terminator ; Kinetics ; Lysine/analogs & derivatives/chemistry/*genetics/metabolism ; Methanosarcina barkeri/chemistry/enzymology/*genetics ; Methyltransferases/genetics/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Biosynthesis ; RNA, Archaeal/chemistry/genetics/metabolism ; RNA, Transfer/chemistry/*genetics/metabolism ; Recombinant Proteins/metabolism ; Sequence Alignment
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  • 91
    Publication Date: 2003-03-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Renner, Rebecca -- New York, N.Y. -- Science. 2003 Mar 21;299(5614):1829.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12649455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/growth & development ; Female ; Humans ; Intelligence ; Maternal Exposure ; Maximum Allowable Concentration ; *Military Science ; *National Academy of Sciences (U.S.) ; *Perchlorates/adverse effects/toxicity ; Pregnancy ; *Sodium Compounds/adverse effects/toxicity ; Thyroid Gland/drug effects/metabolism ; Thyroid Hormones/metabolism ; United States ; United States Environmental Protection Agency ; United States Government Agencies ; *Water Pollutants, Chemical/adverse effects/toxicity ; *Water Supply
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  • 92
    Publication Date: 2003-03-01
    Description: The mechanisms that determine how folding attempts are interrupted to target folding-incompetent proteins for endoplasmic reticulum-associated degradation (ERAD) are poorly defined. Here the alpha-mannosidase I-like protein EDEM was shown to extract misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. EDEM overexpression resulted in faster release of folding-incompetent proteins from the calnexin cycle and earlier onset of degradation, whereas EDEM down-regulation prolonged folding attempts and delayed ERAD. Up-regulation of EDEM during ER stress may promote cell recovery by clearing the calnexin cycle and by accelerating ERAD of terminally misfolded polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molinari, Maurizio -- Calanca, Verena -- Galli, Carmela -- Lucca, Paola -- Paganetti, Paolo -- New York, N.Y. -- Science. 2003 Feb 28;299(5611):1397-400.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Research in Biomedicine, CH-6500 Bellinzona, Switzerland. Maurizio.molinari@irb.unisi.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12610306" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid Endopeptidases/chemistry/*metabolism ; Calnexin/*metabolism ; Cell Line ; Down-Regulation ; Electrophoresis, Polyacrylamide Gel ; Endoplasmic Reticulum/*metabolism ; Glycoproteins/chemistry/*metabolism ; Glycosylation ; Humans ; Kinetics ; Membrane Proteins/*metabolism ; Molecular Weight ; Polysaccharides/metabolism ; Protein Conformation ; Protein Folding ; RNA Interference ; Transfection ; Up-Regulation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
    Publication Date: 2003-03-08
    Description: Mutations in the cytochrome P450 family 1, subfamily B, polypeptide 1 (CYP1B1) gene are a common cause of human primary congenital glaucoma (PCG). Here we show that Cyp1b1-/- mice have ocular drainage structure abnormalities resembling those reported in human PCG patients. Using Cyp1b1-/- mice, we identified the tyrosinase gene (Tyr) as a modifier of the drainage structure phenotype, with Tyr deficiency increasing the magnitude of dysgenesis. The severe dysgenesis in eyes lacking both CYP1B1 and TYR was alleviated by administration of the tyrosinase product dihydroxyphenylalanine (l-dopa). Tyr also modified the drainage structure dysgenesis in mice with a mutant Foxc1 gene, which is also involved in PCG. These experiments raise the possibility that a tyrosinase/l-dopa pathway modifies human PCG, which could open new therapeutic avenues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Libby, Richard T -- Smith, Richard S -- Savinova, Olga V -- Zabaleta, Adriana -- Martin, Janice E -- Gonzalez, Frank J -- John, Simon W M -- CA34196/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Mar 7;299(5612):1578-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jackson Laboratory, Bar Harbor, ME 04609, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12624268" target="_blank"〉PubMed〈/a〉
    Keywords: Albinism, Ocular/genetics/pathology ; Animals ; Anterior Eye Segment/*abnormalities ; Aryl Hydrocarbon Hydroxylases/deficiency/genetics ; Cornea/abnormalities ; Cytochrome P-450 CYP1B1 ; *DNA-Binding Proteins ; Disease Models, Animal ; Female ; Forkhead Transcription Factors ; Glaucoma/*congenital/enzymology/*genetics/pathology ; Intraocular Pressure ; Iris/abnormalities ; Levodopa/administration & dosage/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Monophenol Monooxygenase/deficiency/*genetics/metabolism ; Mutation ; Phenotype ; Pregnancy ; Trabecular Meshwork/abnormalities ; Transcription Factors/genetics
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  • 94
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2003-06-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Molloy, Justin E -- Veigel, Claudia -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2045-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Physical Biochemistry, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK. jmolloy@nimr.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829773" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism/ultrastructure ; Actins/metabolism ; Adenosine Triphosphate/metabolism ; Binding Sites ; Fluorescent Dyes/metabolism ; Hydrolysis ; Kinetics ; Microscopy, Fluorescence ; Models, Biological ; Molecular Motor Proteins/chemistry/*metabolism ; Myosin Light Chains/chemistry/metabolism ; Myosin Type V/chemistry/*metabolism ; Protein Structure, Tertiary
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  • 95
    Publication Date: 2003-02-01
    Description: Genetic evidence suggests that inhibition of amyloid fibril formation by small molecules should be effective against amyloid diseases. Known amyloid inhibitors appear to function by shifting the aggregation equilibrium away from the amyloid state. Here, we describe a series of transthyretin amyloidosis inhibitors that functioned by increasing the kinetic barrier associated with misfolding, preventing amyloidogenesis by stabilizing the native state. The trans-suppressor mutation, threonine 119 --〉 methionine 119, which is known to ameliorate familial amyloid disease, also functioned through kinetic stabilization, implying that this small-molecule strategy should be effective in treating amyloid diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hammarstrom, Per -- Wiseman, R Luke -- Powers, Evan T -- Kelly, Jeffery W -- DK 46335/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):713-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12560553" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloidosis/metabolism/*prevention & control ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Prealbumin/*antagonists & inhibitors/*chemistry/genetics/metabolism ; Protein Denaturation ; *Protein Folding ; Protein Structure, Quaternary ; Protein Subunits ; Suppression, Genetic ; Thermodynamics
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  • 96
    Publication Date: 2003-06-14
    Description: We modeled how the charged levels of different transfer RNAs (tRNAs) that carry the same amino acid (isoacceptors) respond when this amino acid becomes growth-limiting. The charged levels will approach zero for some isoacceptors (such as tRNA2Leu) and remain high for others (such as tRNA4Leu), as determined by the concentrations of isoacceptors and how often their codons occur in protein synthesis. The theory accounts for (synonymous) codons for the same amino acid that are used in ribosome-mediated transcriptional attenuation, the choices of synonymous codons in trans-translating transfermessenger RNA, and the overrepresentation of rare codons in messenger RNAs for amino acid biosynthetic enzymes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elf, Johan -- Nilsson, Daniel -- Tenson, Tanel -- Ehrenberg, Mans -- New York, N.Y. -- Science. 2003 Jun 13;300(5626):1718-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, Box 596, 751 24 Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12805541" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*metabolism ; Amino Acyl-tRNA Synthetases/metabolism ; *Codon ; Escherichia coli/*genetics/growth & development/metabolism ; Escherichia coli Proteins/biosynthesis/genetics ; Frameshifting, Ribosomal ; Gene Expression Regulation, Bacterial ; Kinetics ; Mathematics ; Models, Genetic ; Operon ; *Protein Biosynthesis ; Pyrophosphatases/genetics/metabolism ; RNA, Bacterial/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Transfer/genetics/metabolism ; RNA, Transfer, Amino Acyl/genetics/*metabolism ; Ribosomes/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
    Publication Date: 2003-10-11
    Description: We prepared the primary adduct for the reaction of singlet dioxygen (1O2) with an arylphosphine by using the sterically hindered arylphosphine tris(o-methoxyphenyl)phosphine. The resulting phosphadioxirane has a dioxygen molecule triangularly bound to the phosphorus atom. Olefin trapping experiments show that the phosphadioxirane can undergo nonradical oxygen atom-transfer reactions. Under protic conditions, two different intermediates are formed during the reaction of singlet dioxygen with tris(o-methoxyphenyl)phosphine, namely, the corresponding hydroperoxy arylphosphine and a hydroxy phosphorane. Experiments with other arylphosphines possessing different electronic and steric properties demonstrate that the relative stability of the tris(o-methoxyphenyl)phosphadioxirane is due to both steric and electronic effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, David G -- Gao, Ruomei -- Celaje, Jeff -- Chung, Ha-Yong -- Selke, Matthias -- GM 08101/GM/NIGMS NIH HHS/ -- GM 64104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 10;302(5643):259-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, California State University, Los Angeles, Los Angeles, CA 90032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14551430" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Epoxy Compounds/*chemistry ; Heterocyclic Compounds, 1-Ring/*chemistry ; Kinetics ; Magnetic Resonance Spectroscopy ; Molecular Structure ; Organophosphorus Compounds/*chemistry ; Oxidation-Reduction ; Oxygen/chemistry ; Peroxides/*chemistry ; Phosphines/chemistry ; Phosphorus ; Physicochemical Phenomena ; Singlet Oxygen/chemistry ; Temperature
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  • 98
    Publication Date: 2003-06-07
    Description: Myosin V is a dimeric molecular motor that moves processively on actin, with the center of mass moving approximately 37 nanometers for each adenosine triphosphate hydrolyzed. We have labeled myosin V with a single fluorophore at different positions in the light-chain domain and measured the step size with a standard deviation of 〈1.5 nanometers, with 0.5-second temporal resolution, and observation times of minutes. The step size alternates between 37 + 2x nm and 37 - 2x, where x is the distance along the direction of motion between the dye and the midpoint between the two heads. These results strongly support a hand-over-hand model of motility, not an inchworm model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yildiz, Ahmet -- Forkey, Joseph N -- McKinney, Sean A -- Ha, Taekjip -- Goldman, Yale E -- Selvin, Paul R -- AR26846/AR/NIAMS NIH HHS/ -- AR44420/AR/NIAMS NIH HHS/ -- GM65367/GM/NIGMS NIH HHS/ -- PHS 5 T32 GM08276/PH/PHPPO CDC HHS/ -- R01 GM065367/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2061-5. Epub 2003 Jun 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biophysics and Computational Biology, University of Illinois, Urbana-Champaign, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791999" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism/ultrastructure ; Actins/metabolism ; Adenosine Triphosphate/metabolism ; Binding Sites ; Calmodulin ; Carbocyanines/metabolism ; Catalytic Domain ; Dna ; Fluorescence ; Fluorescent Dyes/metabolism ; Kinetics ; Mathematics ; Microscopy, Fluorescence ; *Models, Biological ; Molecular Motor Proteins/chemistry/*metabolism ; Myosin Light Chains/chemistry/metabolism ; Myosin Type V/chemistry/*metabolism ; Protein Structure, Tertiary ; Rhodamines/metabolism
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  • 99
    Publication Date: 2003-01-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Storch, David -- New York, N.Y. -- Science. 2003 Jan 17;299(5605):346; author reply 346.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biodiversity and Macroecology Group, Department of Animal and Plant Sciences, University of Sheffield, Sheffield S10 2TN, UK, and Center for Theoretical Study, Charles University, Jilska 1, 110 00 Prague, Czech Republic. storch@cts.cuni.cz〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12531999" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Constitution ; *Ecosystem ; Kinetics ; *Models, Biological ; Population Density ; Temperature ; Thermodynamics
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  • 100
    Publication Date: 2003-03-29
    Description: Acetyl-coenzyme A carboxylases (ACCs) are required for the biosynthesis and oxidation of long-chain fatty acids. They are targets for therapeutics against obesity and diabetes, and several herbicides function by inhibiting their carboxyltransferase (CT) domain. We determined the crystal structure of the free enzyme and the coenzyme A complex of yeast CT at 2.7 angstrom resolution and found that it comprises two domains, both belonging to the crotonase/ClpP superfamily. The active site is at the interface of a dimer. Mutagenesis and kinetic studies reveal the functional roles of conserved residues here. The herbicides target the active site of CT, providing a lead for inhibitor development against human ACCs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Hailong -- Yang, Zhiru -- Shen, Yang -- Tong, Liang -- New York, N.Y. -- Science. 2003 Mar 28;299(5615):2064-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12663926" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl-CoA Carboxylase/antagonists & inhibitors/*chemistry/genetics/metabolism ; Amino Acid Sequence ; Binding Sites ; Biotin/chemistry/metabolism ; Catalysis ; Coenzyme A/chemistry/metabolism ; Crystallography, X-Ray ; Dimerization ; Enzyme Inhibitors/metabolism/pharmacology ; Hydrogen Bonding ; Kinetics ; Molecular Sequence Data ; Mutagenesis ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pyridines/metabolism/pharmacology ; Saccharomyces cerevisiae/*enzymology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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