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    Optogenetics. Engineering of a light-gated potassium channel (2015)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2015-05-09
    Description: The present palette of opsin-based optogenetic tools lacks a light-gated potassium (K(+)) channel desirable for silencing of excitable cells. Here, we describe the construction of a blue-light-induced K(+) channel 1 (BLINK1) engineered by fusing the plant LOV2-Jalpha photosensory module to the small viral K(+) channel Kcv. BLINK1 exhibits biophysical features of Kcv, including K(+) selectivity and high single-channel conductance but reversibly photoactivates in blue light. Opening of BLINK1 channels hyperpolarizes the cell to the K(+) equilibrium potential. Ectopic expression of BLINK1 reversibly inhibits the escape response in light-exposed zebrafish larvae. BLINK1 therefore provides a single-component optogenetic tool that can establish prolonged, physiological hyperpolarization of cells at low light intensities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cosentino, Cristian -- Alberio, Laura -- Gazzarrini, Sabrina -- Aquila, Marco -- Romano, Edoardo -- Cermenati, Solei -- Zuccolini, Paolo -- Petersen, Jan -- Beltrame, Monica -- Van Etten, James L -- Christie, John M -- Thiel, Gerhard -- Moroni, Anna -- BB/J016047/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- BB/M002128/Biotechnology and Biological Sciences Research Council/United Kingdom -- New York, N.Y. -- Science. 2015 May 8;348(6235):707-10. doi: 10.1126/science.aaa2787. Epub 2015 May 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biosciences, University of Milano, Italy. ; Institute of Molecular, Cell and Systems Biology, University of Glasgow, UK. ; Department of Plant Pathology and Nebraska Center for Virology, University of Nebraska-Lincoln, Lincoln, NE 68583-0900, USA. ; Membrane Biophysics, Technical University of Darmstadt, Darmstadt, Germany. ; Department of Biosciences, University of Milano, Italy. anna.moroni@unimi.it.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25954011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avena/metabolism ; Biophysical Processes ; HEK293 Cells ; Humans ; Larva ; Light ; *Optogenetics ; Phototropins/chemistry/genetics ; Potassium Channels/chemistry/genetics ; Protein Conformation/radiation effects ; Protein Engineering ; Recombinant Fusion Proteins/chemistry/genetics/*radiation effects ; Viral Proteins/chemistry/genetics ; Zebrafish
    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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    Surface expression and functional characterization of α-granule factor V in human platelets: effects of ionophore A23187, thrombin, collagen, and convulxin (2000)
    American Society of Hematology
    Details
    Publication Date: 2000-03-01
    Description: Factor V (FV) present in platelet -granules has a significant but incompletely understood role in hemostasis. This report demonstrates that a fraction of platelets express very high levels of surface-bound, -granule FV on simultaneous activation with 2 agonists, thrombin and convulxin, an activator of the collagen receptor glycoprotein VI. This subpopulation of activated platelets represents 30.7% ± 4.7% of the total population and is referred to as convulxin and thrombin–induced-FV (COAT-FV) platelets. COAT-FV platelets are also observed on activation with thrombin plus collagen types I, V, or VI, but not with type III. No single agonist examined was able to produce COAT-FV platelets, although ionophore A23187 in conjunction with either thrombin or convulxin did generate this population. COAT-FV platelets bound annexin-V, indicating exposure of aminophospholipids and were enriched in young platelets as identified by the binding of thiazole orange. The functional significance of COAT-FV platelets was investigated by demonstrating that factor Xa preferentially bound to COAT-FV platelets, that COAT-FV platelets had more FV activity than either thrombin or A23187–activated platelets, and that COAT-FV platelets were capable of generating more prothrombinase activity than any other physiologic agonist examined. Microparticle production by dual stimulation with thrombin and convulxin was less than that observed with A23187, indicating that microparticles were not responsible for all the activities observed. These data demonstrate a new procoagulant component produced from dual stimulation of platelets with thrombin and collagen. COAT-FV platelets may explain the unique role of -granule FV and the hemostatic effectiveness of young platelets.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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