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  • Kinetics  (4)
  • American Association for the Advancement of Science (AAAS)  (4)
  • American Association for the Advancement of Science
  • American Chemical Society
  • American Physical Society (APS)
  • 2005-2009  (1)
  • 2000-2004  (1)
  • 1980-1984  (2)
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  • 1935-1939
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  • American Association for the Advancement of Science (AAAS)  (4)
  • American Association for the Advancement of Science
  • American Chemical Society
  • American Physical Society (APS)
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Year
  • 1
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    Parallel single-cell monitoring of receptor-triggered membrane translocation of a calcium-sensing protein module (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Time courses of translocation of fluorescently conjugated proteins to the plasma membrane were simultaneously measured in thousands of individual rat basophilic leukemia cells. We found that the C2 domain---a calcium-sensing, lipid-binding protein module that is an essential regulator of protein kinase C and numerous other proteins---targeted proteins to the plasma membrane transiently if calcium was released from internal stores, and persistently in response to entry of extracellular calcium across the plasma membrane. The C2 domain translocation time courses of stimulated cells clustered into only two primary modes. Hence, the reversible recruitment of families of signaling proteins from one cellular compartment to another is a rapid bifurcation mechanism for inducing discrete states of cellular signaling networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teruel, Mary N -- Meyer, Tobias -- CA83229/CA/NCI NIH HHS/ -- GM062144/GM/NIGMS NIH HHS/ -- HG00057/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1910-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Stanford University Medical School, 269 Campus Drive, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884760" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins ; Calcium/*metabolism ; *Calcium Signaling ; Cell Membrane/*metabolism ; Cytosol/metabolism ; Fluorescence ; Fluorescent Dyes ; Isoenzymes/chemistry/*metabolism ; Kinetics ; Luminescent Proteins ; Platelet Activating Factor/pharmacology ; Protein Binding ; Protein Kinase C/chemistry/*metabolism ; Protein Structure, Tertiary ; *Protein Transport ; Rats ; Receptors, Cell Surface/*metabolism ; Recombinant Fusion Proteins/metabolism ; Software ; Thapsigargin/pharmacology ; Transfection ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-11
    Description: Many signaling, cytoskeletal, and transport proteins have to be localized to the plasma membrane (PM) in order to carry out their function. We surveyed PM-targeting mechanisms by imaging the subcellular localization of 125 fluorescent protein-conjugated Ras, Rab, Arf, and Rho proteins. Out of 48 proteins that were PM-localized, 37 contained clusters of positively charged amino acids. To test whether these polybasic clusters bind negatively charged phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] lipids, we developed a chemical phosphatase activation method to deplete PM PI(4,5)P2. Unexpectedly, proteins with polybasic clusters dissociated from the PM only when both PI(4,5)P2 and phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] were depleted, arguing that both lipid second messengers jointly regulate PM targeting.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3579512/" 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/PMC3579512/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heo, Won Do -- Inoue, Takanari -- Park, Wei Sun -- Kim, Man Lyang -- Park, Byung Ouk -- Wandless, Thomas J -- Meyer, Tobias -- R01 GM030179/GM/NIGMS NIH HHS/ -- R01 GM030179-24A1/GM/NIGMS NIH HHS/ -- R01 GM030179-25/GM/NIGMS NIH HHS/ -- R01 GM063702/GM/NIGMS NIH HHS/ -- R01 MH064801/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1458-61. Epub 2006 Nov 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, 318 Campus Drive, Clark Building, Stanford University Medical School, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17095657" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors/chemistry/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Membrane/*metabolism ; GTP Phosphohydrolases/chemistry/*metabolism ; HeLa Cells ; Humans ; Hydrophobic and Hydrophilic Interactions ; Kinetics ; Mice ; Molecular Sequence Data ; NIH 3T3 Cells ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphatidylinositol Phosphates/*metabolism ; Second Messenger Systems ; Signal Transduction ; Static Electricity ; rab GTP-Binding Proteins/chemistry/metabolism ; ras Proteins/chemistry/metabolism ; rho GTP-Binding Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    High-affinity choline transport in proteoliposomes derived from rat cortical synaptosomes (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-08-27
    Description: Functional high- and low-affinity choline transport processes from rat cortical plasma membranes were reconstituted in phosphatidylcholine bilayer liposomes. The high-affinity choline transporter demonstrated a pharmacological profile and ion dependency that were identical to those of intact synaptosomes. This preparation may be used to further characterize choline transport and, with appropriate supplementation, to investigate the release of acetylcholine in the absence of synaptic vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer, E M -- Cooper, J R -- NS 09836/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):843-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7100928" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Animals ; Biological Transport ; Cell Membrane/metabolism ; Chlorides/metabolism ; Choline/*metabolism ; Kinetics ; Lipid Bilayers/metabolism ; Liposomes/*metabolism ; Phosphatidylcholines/metabolism ; Rats ; Sodium/metabolism ; Synaptosomes/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Virus-induced corticosterone in hypophysectomized mice: a possible lymphoid adrenal axis (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-12-24
    Description: Infection of hypophysectomized mice with Newcastle disease virus caused a time-dependent increase in corticosterone and interferon production. Prior treatment with dexamethasone completely inhibited the virus-induced elevation in corticosterone concentration, but did not significantly alter the interferon response. Lymphocytes appear to be the most likely source of an adrenocorticotropin-like substance that is responsible for the increased corticosterone, since spleen cells from the virus-infected, but not from control or dexamethasone-treated, hypophysectomized mice showed positive immunofluorescence with antibody to adrenocorticotropin-(1-13 amide). Thus the adrenocorticotropin-like material and interferon appear to be coordinately induced the differentially controlled products of different genes. These findings strongly suggest the existence of a lymphoid-adrenal axis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, E M -- Meyer, W J -- Blalock, J E -- AM30046/AM/NIADDK NIH HHS/ -- HL20201/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1982 Dec 24;218(4579):1311-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6183748" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/*physiology ; Animals ; Corticosterone/*biosynthesis ; Dexamethasone/pharmacology ; *Hypophysectomy ; Interferons/biosynthesis ; Kinetics ; Lymph Nodes/*physiology ; Mice ; Newcastle Disease/*metabolism ; Time Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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