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  • Cell Line  (9)
  • Recombinant Fusion Proteins/metabolism  (8)
  • American Association for the Advancement of Science (AAAS)  (16)
  • American Geophysical Union (AGU)
  • American Meteorological Society
  • National Academy of Sciences
  • Nature Publishing Group
  • 2015-2019
  • 2000-2004  (16)
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  • American Association for the Advancement of Science (AAAS)  (16)
  • American Geophysical Union (AGU)
  • American Meteorological Society
  • National Academy of Sciences
  • Nature Publishing Group
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  • 1
    Publikationsdatum: 2000-12-09
    Beschreibung: Genetic engineering of non-beta cells to release insulin upon feeding could be a therapeutic modality for patients with diabetes. A tumor-derived K-cell line was induced to produce human insulin by providing the cells with the human insulin gene linked to the 5'-regulatory region of the gene encoding glucose-dependent insulinotropic polypeptide (GIP). Mice expressing this transgene produced human insulin specifically in gut K cells. This insulin protected the mice from developing diabetes and maintained glucose tolerance after destruction of the native insulin-producing beta cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheung, A T -- Dayanandan, B -- Lewis, J T -- Korbutt, G S -- Rajotte, R V -- Bryer-Ash, M -- Boylan, M O -- Wolfe, M M -- Kieffer, T J -- New York, N.Y. -- Science. 2000 Dec 8;290(5498):1959-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Alberta, Edmonton, AB T6G 2S2, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11110661" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Blood Glucose/metabolism ; Cell Line ; Cloning, Molecular ; Diabetes Mellitus, Experimental/metabolism/*therapy ; Enteroendocrine Cells/*cytology/*metabolism ; Gastric Inhibitory Polypeptide/biosynthesis/genetics ; Gene Expression ; Genetic Engineering ; *Genetic Therapy ; Glucose/administration & dosage/*metabolism ; Glucose Tolerance Test ; Humans ; Insulin/biosynthesis/genetics/*metabolism ; Mice ; Mice, Transgenic ; Proinsulin/genetics ; Promoter Regions, Genetic ; Protein Precursors/genetics ; Stem Cells/cytology/metabolism ; Streptozocin ; Transfection ; Transgenes ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Publikationsdatum: 2002-05-23
    Beschreibung: Mechanical and thermal cues stimulate a specialized group of sensory neurons that terminate in the skin. Three members of the transient receptor potential (TRP) family of channels are expressed in subsets of these neurons and are activated at distinct physiological temperatures. Here, we describe the cloning and characterization of a novel thermosensitive TRP channel. TRPV3 has a unique threshold: It is activated at innocuous (warm) temperatures and shows an increased response at noxious temperatures. TRPV3 is specifically expressed in keratinocytes; hence, skin cells are capable of detecting heat via molecules similar to those in heat-sensing neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peier, Andrea M -- Reeve, Alison J -- Andersson, David A -- Moqrich, Aziz -- Earley, Taryn J -- Hergarden, Anne C -- Story, Gina M -- Colley, Sian -- Hogenesch, John B -- McIntyre, Peter -- Bevan, Stuart -- Patapoutian, Ardem -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2046-9. Epub 2002 May 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomics Institute of the Novartis Research Foundation, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12016205" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Animals, Newborn ; Blotting, Northern ; CHO Cells ; Capsaicin/*analogs & derivatives/pharmacology ; *Cation Transport Proteins ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Cricetinae ; Epidermis/cytology/innervation/metabolism ; Ganglia, Spinal/metabolism ; *Hot Temperature ; Humans ; In Situ Hybridization ; Ion Channels/chemistry/genetics/*metabolism ; Keratinocytes/*metabolism ; Membrane Potentials ; Mice ; Molecular Sequence Data ; Nerve Endings/physiology ; Neurons/physiology ; Patch-Clamp Techniques ; RNA, Messenger/genetics/metabolism ; Ruthenium Red/pharmacology ; Signal Transduction ; Spinal Cord/metabolism ; TRPV Cation Channels ; Temperature
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Publikationsdatum: 2000-11-04
    Beschreibung: The Agrobacterium VirB/D4 transport system mediates the transfer of a nucleoprotein T complex into plant cells, leading to crown gall disease. In addition, several Virulence proteins must somehow be transported to fulfill a function in planta. Here, we used fusions between Cre recombinase and VirE2 or VirF to directly demonstrate protein translocation into plant cells. Transport of the proteins was monitored by a Cre-mediated in planta recombination event resulting in a selectable phenotype and depended on the VirB/D4 transport system but did not require transferred DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vergunst, A C -- Schrammeijer, B -- den Dulk-Ras, A -- de Vlaam, C M -- Regensburg-Tuink, T J -- Hooykaas, P J -- New York, N.Y. -- Science. 2000 Nov 3;290(5493):979-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Plant Sciences, Leiden University, Clusius Laboratory, Wassenaarseweg 64, 2333 AL, Leiden, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11062129" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Agrobacterium tumefaciens/genetics/*metabolism/pathogenicity ; Arabidopsis/genetics/*metabolism/microbiology ; Bacterial Proteins/*metabolism ; DNA, Bacterial/genetics/metabolism ; DNA-Binding Proteins/*metabolism ; Drug Resistance ; Integrases/genetics/*metabolism ; *Ion Channels ; Kanamycin/pharmacology ; Plant Roots/metabolism ; Plants, Genetically Modified ; Plasmids ; Polymerase Chain Reaction ; *Protein Transport ; Recombinant Fusion Proteins/metabolism ; *Viral Proteins ; Virulence ; *Virulence Factors
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Publikationsdatum: 2001-05-26
    Beschreibung: Dysfunction of the tubby protein results in maturity-onset obesity in mice. Tubby has been implicated as a transcription regulator, but details of the molecular mechanism underlying its function remain unclear. Here we show that tubby functions in signal transduction from heterotrimeric GTP-binding protein (G protein)-coupled receptors. Tubby localizes to the plasma membrane by binding phosphatidylinositol 4,5-bisphosphate through its carboxyl terminal "tubby domain." X-ray crystallography reveals the atomic-level basis of this interaction and implicates tubby domains as phosphorylated-phosphatidyl- inositol binding factors. Receptor-mediated activation of G protein alphaq (Galphaq) releases tubby from the plasma membrane through the action of phospholipase C-beta, triggering translocation of tubby to the cell nucleus. The localization of tubby-like protein 3 (TULP3) is similarly regulated. These data suggest that tubby proteins function as membrane-bound transcription regulators that translocate to the nucleus in response to phosphoinositide hydrolysis, providing a direct link between G-protein signaling and the regulation of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santagata, S -- Boggon, T J -- Baird, C L -- Gomez, C A -- Zhao, J -- Shan, W S -- Myszka, D G -- Shapiro, L -- New York, N.Y. -- Science. 2001 Jun 15;292(5524):2041-50. Epub 2001 May 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ruttenberg Cancer Center, Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine of New York University, 1425 Madison Avenue New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11375483" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Active Transport, Cell Nucleus ; Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Cell Membrane/metabolism ; Cell Nucleus/*metabolism ; Cells, Cultured ; Crystallography, X-Ray ; GTP-Binding Protein alpha Subunits, Gq-G11 ; Gene Expression Regulation ; Heterotrimeric GTP-Binding Proteins/*metabolism ; Humans ; Isoenzymes/*metabolism ; Membrane Lipids/metabolism ; Mice ; Models, Biological ; Molecular Sequence Data ; Nuclear Localization Signals ; Obesity/genetics/metabolism ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phospholipase C beta ; Phosphorylation ; Protein Structure, Tertiary ; Proteins/chemistry/genetics/*metabolism ; Receptor, Serotonin, 5-HT2C ; Receptors, Muscarinic/metabolism ; Receptors, Serotonin/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transcription Factors/chemistry/genetics/*metabolism ; Type C Phospholipases/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Publikationsdatum: 2001-03-07
    Beschreibung: The ability of intestinal mucosa to absorb dietary ferric iron is attributed to the presence of a brush-border membrane reductase activity that displays adaptive responses to iron status. We have isolated a complementary DNA, Dcytb (for duodenal cytochrome b), which encoded a putative plasma membrane di-heme protein in mouse duodenal mucosa. Dcytb shared between 45 and 50% similarity to the cytochrome b561 family of plasma membrane reductases, was highly expressed in the brush-border membrane of duodenal enterocytes, and induced ferric reductase activity when expressed in Xenopus oocytes and cultured cells. Duodenal expression levels of Dcytb messenger RNA and protein were regulated by changes in physiological modulators of iron absorption. Thus, Dcytb provides an important element in the iron absorption pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McKie, A T -- Barrow, D -- Latunde-Dada, G O -- Rolfs, A -- Sager, G -- Mudaly, E -- Mudaly, M -- Richardson, C -- Barlow, D -- Bomford, A -- Peters, T J -- Raja, K B -- Shirali, S -- Hediger, M A -- Farzaneh, F -- Simpson, R J -- New York, N.Y. -- Science. 2001 Mar 2;291(5509):1755-9. Epub 2001 Feb 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Medicine, Guy's, King's and St. Thomas' School of Medicine, King's College London, Rayne Institute, Denmark Hill Campus, 123 Coldharbour Lane, London SE5 9NU, UK. andrew.t.mckie@kcl.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11230685" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Anemia/enzymology ; Animals ; Anoxia ; Cell Line ; Cloning, Molecular ; Cytochrome b Group/chemistry/genetics/*metabolism ; DNA, Complementary ; Duodenum/enzymology/*metabolism ; Enterocytes/enzymology/metabolism ; Enzyme Induction ; Ferric Compounds/*metabolism ; *Intestinal Absorption ; Intestinal Mucosa/enzymology/*metabolism ; Iron, Dietary/administration & dosage/*metabolism ; Male ; Mice ; Microvilli/enzymology/metabolism ; Molecular Sequence Data ; Nitroblue Tetrazolium/metabolism ; Oocytes ; Oxidation-Reduction ; Oxidoreductases/chemistry/genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; Tetrazolium Salts/metabolism ; Thiazoles/metabolism ; *Transfection ; Up-Regulation ; Xenopus
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    Publikationsdatum: 2002-04-20
    Beschreibung: Recombinant proteins containing tetracysteine tags can be successively labeled in living cells with different colors of biarsenical fluorophores so that older and younger protein molecules can be sharply distinguished by both fluorescence and electron microscopy. Here we used this approach to show that newly synthesized connexin43 was transported predominantly in 100- to 150-nanometer vesicles to the plasma membrane and incorporated at the periphery of existing gap junctions, whereas older connexins were removed from the center of the plaques into pleiomorphic vesicles of widely varying sizes. Selective imaging by correlated optical and electron microscopy of protein molecules of known ages will clarify fundamental processes of protein trafficking in situ.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gaietta, Guido -- Deerinck, Thomas J -- Adams, Stephen R -- Bouwer, James -- Tour, Oded -- Laird, Dale W -- Sosinsky, Gina E -- Tsien, Roger Y -- Ellisman, Mark H -- DC03192/DC/NIDCD NIH HHS/ -- NS14718/NS/NINDS NIH HHS/ -- NS27177/NS/NINDS NIH HHS/ -- P01 DK54441/DK/NIDDK NIH HHS/ -- R01 GM065937/GM/NIGMS NIH HHS/ -- RR04050/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):503-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Microscopy and Imaging Research, Department of Neurosciences, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964472" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): 3,3'-Diaminobenzidine/chemistry ; Amino Acid Motifs ; Animals ; Arsenicals/metabolism ; Cell Line ; Cell Membrane/metabolism/ultrastructure ; Connexin 43/biosynthesis/*metabolism ; Cysteine/chemistry ; Endocytosis ; Exocytosis ; Fluoresceins/metabolism ; Fluorescence ; Fluorescent Dyes/metabolism ; Gap Junctions/*metabolism/ultrastructure ; HeLa Cells ; Humans ; Microscopy, Confocal ; Microscopy, Electron ; Microscopy, Immunoelectron ; Organometallic Compounds/metabolism ; Oxazines/metabolism ; Patch-Clamp Techniques ; Protein Transport ; Recombinant Proteins/metabolism ; Transport Vesicles/*metabolism/ultrastructure
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 7
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2002-02-09
    Beschreibung: Lamellipodia are thin, veil-like extensions at the edge of cells that contain a dynamic array of actin filaments. We describe an approach for analyzing spatial regulation of actin polymerization and depolymerization in vivo in which we tracked single molecules of actin fused to the green fluorescent protein. Polymerization and the lifetime of actin filaments in lamellipodia were measured with high spatial precision. Basal polymerization and depolymerization occurred throughout lamellipodia with largely constant kinetics, and polymerization was promoted within one micron of the lamellipodium tip. Most of the actin filaments in the lamellipodium were generated by polymerization away from the tip.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watanabe, Naoki -- Mitchison, Timothy J -- GM48027/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1083-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. naoki_watanabe@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834838" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Actin Cytoskeleton/drug effects/*metabolism/ultrastructure ; Actin-Related Protein 2 ; Actin-Related Protein 3 ; Actins/*metabolism ; Animals ; Biopolymers ; Cell Line ; *Cytoskeletal Proteins ; *Depsipeptides ; Fibroblasts ; Fluorescence ; Green Fluorescent Proteins ; Half-Life ; Luminescent Proteins ; Models, Biological ; Peptides, Cyclic/pharmacology ; Pseudopodia/*metabolism/ultrastructure ; Recombinant Fusion Proteins/metabolism ; Xenopus
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 8
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2003-06-14
    Beschreibung: The SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) hypothesis suggests that pairs of proteins known as vesicle (v-) SNAREs and target membrane (t-) SNAREs interact specifically to control and mediate intracellular membrane fusion events. Here, cells expressing the interacting domains of v- and t-SNAREs on the cell surface were found to fuse spontaneously, demonstrating that SNAREs are sufficient to fuse biological membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, Chuan -- Ahmed, Mahiuddin -- Melia, Thomas J -- Sollner, Thomas H -- Mayer, Thomas -- Rothman, James E -- New York, N.Y. -- Science. 2003 Jun 13;300(5626):1745-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, Box 251, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12805548" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antigens, Surface/chemistry/*metabolism ; COS Cells ; *Cell Fusion ; Cell Membrane/*metabolism ; Cercopithecus aethiops ; Endoplasmic Reticulum/metabolism ; Glycosylation ; Membrane Fusion/physiology ; Membrane Proteins/chemistry/genetics/*metabolism ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; R-SNARE Proteins ; Recombinant Fusion Proteins/metabolism ; Synaptosomal-Associated Protein 25 ; Syntaxin 1 ; Transfection
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 9
    Publikationsdatum: 2002-03-02
    Beschreibung: Type III secreted "effector" proteins of bacterial pathogens play central roles in virulence, yet are notoriously difficult to identify. We used an in vivo genetic screen to identify 13 effectors secreted by the type III apparatus (called Hrp, for "hypersensitive response and pathogenicity") of the plant pathogen Pseudomonas syringae. Although sharing little overall homology, the amino-terminal regions of these effectors had strikingly similar amino acid compositions. This feature facilitated the bioinformatic prediction of 38 P. syringae effectors, including 15 previously unknown proteins. The secretion of two of these putative effectors was shown to be type III--dependent. Effectors showed high interstrain variation, supporting a role for some effectors in adaptation to different hosts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guttman, David S -- Vinatzer, Boris A -- Sarkar, Sara F -- Ranall, Max V -- Kettler, Gregory -- Greenberg, Jean T -- GM020024/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1722-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, University of Toronto, 25 Willcocks Street, Toronto, ON M5S 3B2, Canada. guttman@botany.utoronto.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872842" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Amino Acids/analysis ; Arabidopsis/genetics/metabolism/*microbiology ; *Arabidopsis Proteins ; Bacterial Proteins/chemistry/*genetics/*metabolism ; Computational Biology ; DNA Transposable Elements ; *Genes, Bacterial ; Genomics ; Molecular Sequence Data ; Plant Proteins/metabolism ; Promoter Regions, Genetic ; Proteome ; Pseudomonas/*genetics/*metabolism/pathogenicity ; Recombinant Fusion Proteins/metabolism ; Virulence
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 10
    facet.materialart.
    Unbekannt
    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2000-11-18
    Beschreibung: Histoplasma capsulatum is an effective intracellular parasite of macrophages and causes the most prevalent fungal respiratory disease in the United States. A "dimorphic" fungus, H. capsulatum exists as a saprophytic mold in soil and converts to the parasitic yeast form after inhalation. Only the yeasts secrete a calcium-binding protein (CBP) and can grow in calcium-limiting conditions. To probe the relation between calcium limitation and intracellular parasitism, we designed a strategy to disrupt CBP1 in H. capsulatum using a telomeric linear plasmid and a two-step genetic selection. The resultingcbp1 yeasts no longer grew when deprived of calcium, and they were also unable to destroy macrophages in vitro or proliferate in a mouse model of pulmonary infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sebghati, T S -- Engle, J T -- Goldman, W E -- A107172/PHS HHS/ -- AI25584/AI/NIAID NIH HHS/ -- HL07317/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 17;290(5495):1368-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Campus Box 8230, 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/11082066" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Alleles ; Animals ; Calcium/*metabolism ; Calcium-Binding Proteins/*genetics/*metabolism ; Cell Line ; Cell Survival ; Gene Targeting ; Genes, Fungal ; Genetic Complementation Test ; Histoplasma/genetics/growth & development/metabolism/*pathogenicity ; Histoplasmosis/*microbiology ; Lung Diseases, Fungal/microbiology ; Macrophages/*microbiology ; Mice ; Mutagenesis ; Phenotype ; Plasmids ; Recombination, Genetic ; Transformation, Genetic ; Virulence
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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