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  • 1
    Publication Date: 2018-10-10
    Description: Loss of pyruvate kinase M2 limits growth and triggers innate immune signaling in endothelial cells Loss of pyruvate kinase M2 limits growth and triggers innate immune signaling in endothelial cells, Published online: 09 October 2018; doi:10.1038/s41467-018-06406-8 The glycolytic enzyme pyruvate kinase M2 (PKM2) is required for nucleotide synthesis and cell proliferation. Using gene expression and metabolomics analyses, the authors here show that PKM2 regulates methionine metabolism and DNA methylation in endothelial cells.
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 2
    Publication Date: 2014-06-28
    Description: Dynamin superfamily molecular motors use guanosine triphosphate (GTP) as a source of energy for membrane-remodeling events. We found that knockdown of nucleoside diphosphate kinases (NDPKs) NM23-H1/H2, which produce GTP through adenosine triphosphate (ATP)-driven conversion of guanosine diphosphate (GDP), inhibited dynamin-mediated endocytosis. NM23-H1/H2 localized at clathrin-coated pits and interacted with the proline-rich domain of dynamin. In vitro, NM23-H1/H2 were recruited to dynamin-induced tubules, stimulated GTP-loading on dynamin, and triggered fission in the presence of ATP and GDP. NM23-H4, a mitochondria-specific NDPK, colocalized with mitochondrial dynamin-like OPA1 involved in mitochondria inner membrane fusion and increased GTP-loading on OPA1. Like OPA1 loss of function, silencing of NM23-H4 but not NM23-H1/H2 resulted in mitochondrial fragmentation, reflecting fusion defects. Thus, NDPKs interact with and provide GTP to dynamins, allowing these motor proteins to work with high thermodynamic efficiency.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4601533/" 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/PMC4601533/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boissan, Mathieu -- Montagnac, Guillaume -- Shen, Qinfang -- Griparic, Lorena -- Guitton, Jerome -- Romao, Maryse -- Sauvonnet, Nathalie -- Lagache, Thibault -- Lascu, Ioan -- Raposo, Graca -- Desbourdes, Celine -- Schlattner, Uwe -- Lacombe, Marie-Lise -- Polo, Simona -- van der Bliek, Alexander M -- Roux, Aurelien -- Chavrier, Philippe -- 311536/European Research Council/International -- New York, N.Y. -- Science. 2014 Jun 27;344(6191):1510-5. doi: 10.1126/science.1253768.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut Curie, Research Center, Paris, France. Membrane and Cytoskeleton Dynamics, CNRS UMR 144, Paris, France. Universite Pierre et Marie Curie, University Paris 06, Paris, France. Saint-Antoine Research Center, INSERM UMR-S 938, Paris, France. mathieu.boissan@inserm.fr philippe.chavrier@curie.fr. ; Institut Curie, Research Center, Paris, France. Membrane and Cytoskeleton Dynamics, CNRS UMR 144, Paris, France. ; Department of Biological Chemistry, David Geffen School of Medicine at University of California, Los Angeles, Los Angeles, CA, USA. ; Hospices Civils de Lyon, Pierre Benite, France. Universite de Lyon, Lyon, France. ; Institut Curie, Research Center, Paris, France. Structure and Membrane Compartments, CNRS UMR 144, Paris, France. ; Institut Pasteur, Unite de Biologie des Interactions Cellulaires, Paris, France. ; Quantitative Image Analysis Unit, Institut Pasteur, Paris, France. ; Institut de Biochimie et Genetique Cellulaires-CNRS, Universite Bordeaux 2, Bordeaux, France. ; Universite Grenoble Alpes, Laboratory of Fundamental and Applied Bioenergetics, Grenoble, France. Inserm, U1055, Grenoble, France. ; Universite Pierre et Marie Curie, University Paris 06, Paris, France. Saint-Antoine Research Center, INSERM UMR-S 938, Paris, France. ; IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, Milan, Italy. Dipartimento di Scienze della Salute, Universita' degli Studi di Milano, Milan, Italy. ; Biochemistry Department, University of Geneva, & Swiss National Center for Competence in Research Program Chemical Biology, Geneva, Switzerland. ; Institut Curie, Research Center, Paris, France. Membrane and Cytoskeleton Dynamics, CNRS UMR 144, Paris, France. mathieu.boissan@inserm.fr philippe.chavrier@curie.fr.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24970086" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Cell Line ; Cell Membrane/*metabolism ; Coated Pits, Cell-Membrane/metabolism ; Dynamins/*metabolism ; Endocytosis ; GTP Phosphohydrolases/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/*metabolism ; Humans ; Intracellular Membranes/metabolism ; Membrane Fusion ; Mitochondria/metabolism ; NM23 Nucleoside Diphosphate Kinases/genetics/*metabolism ; Nucleoside Diphosphate Kinase D/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2015-02-07
    Description: Article Activation of purinergic P2X 7 receptors is important for phagocytosis and bacterial killing. Here the authors show that a phospholipid scramblase, Anoctamin 6, is activated downstream of P2X 7 R and is a critical mediator of bacterial internalization and killing by macrophages. Nature Communications doi: 10.1038/ncomms7245 Authors: Jiraporn Ousingsawat, Podchanart Wanitchakool, Arthur Kmit, Ana M. Romao, Walailak Jantarajit, Rainer Schreiber, Karl Kunzelmann
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 42 (1994), S. 391-395 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Medium-chain fatty acids (C6 to C12), produced by yeast metabolism during alcoholic fermentation, are known to be inhibitory to lactic acid bacteria. The purpose of this work was to clarify the effect of both ethanol and decanoic and dodecanoic acids on the growth and malolactic activity of a Leuconostoc oenos strain isolated from Portuguese red wine. Ethanol in concentrations up to 12% had no significant effect on malolactic activity but strongly inhibited cell growth. The fatty acids decanoic acid, in concentrations up to 12.5 mg l-1, and, dodecanoic acid up to 2.5 mg l-1 seemed to act as growth factors stimulating also malolactic activity; at higher concentrations they exerted an inhibitory effect. We found clear pH dependence between pH 3.0 and pH 6.0, between decanoic acid concentration and its effect on malolactic activity, indicating that the undissociated molecule is the active form. At pH 3.0 the results can be explained by considering that fatty acids enter the cell as protonated molecules and dissociate in the cytoplasm due to the higher internal pH, leading to increased intracellular hydrogenous concentration. This may be the basis of two different effects that contribute to the observed inhibition: decrease in the intracellular pH and dissipation of the transmembrane proton gradient, thus inhibiting intracellular enzymes and ΔpH-dependent transport systems.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Cytochrome c6, a plastocyanin functionally interchangeable electron carrier between the chlorophyll molecule P700 of photosystem I and cytochrome f from cytochrome b6f complex, has been isolated from the green alga Monoraphidium braunii and crystallized by the vapour-diffusion technique in sodium citrate. Crystals belong to space group R3, with cell dimensions a = b = 51.93 (5) and c = 80.5 (1) Å (hexagonal axes), with one molecule per asymmetric unit. They diffract beyond 1.9 Å under a Cu Kα rotating-anode source, with an anomalous signal that allows the positioning of the heme Fe atom in the unit cell.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Organometallics 3 (1984), S. 936-937 
    ISSN: 1520-6041
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 29 (1996), S. 311-317 
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The densities of protein crystals have been determined by crystal-volume measurement and amino-acid analysis. For this purpose, protein crystals were freely mounted under humidity control by means of air-stream-crystal-regulated humidity. With a video system (charge-coupled-device camera) the two-dimensional shadow projections of crystals are recorded and by the method of back projection the crystal shape is reconstructed and the volume determined. It is shown that the method is independent of the crystal morphology by the consistency of the results from a number of different crystals and materials.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 24 (2000), S. 256-261 
    ISSN: 1476-5535
    Keywords: Keywords: Chrysonilia sitophila; cork stoppers; cork taint; 2,4,6-trichloroanisole
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The contribution of Chrysonilia sitophila in cork stopper manufacture was studied and a simulation of the industrial processing of cork stoppers was performed. Stoppers cut from slabs where mold development was inhibited were compared with others cut from slabs colonized by C. sitophila alone or with several molds, in terms of physical properties and chemical taints. C. sitophila does not produce 2,4,6-trichloroanisole, guaiacol, or 1-octene-3-ol on cork slabs incubated for 66 days. Since some chlorophenol-related compounds contaminate cork slabs during the production processes, metabolic tests were performed to investigate the capability of molds to produce 2,4,6-trichloroanisole by methylation of 2,4,6-trichlorophenol. Degradation of 2,4,6-trichlorophenol by C. sitophila resulted in a very high level of degradation without production of 2,4,6-trichloroanisole. C. sitophila restricted growth of other molds on maturing slabs for at least 30 days. These results show that C. sitophila can be exploited by industrial producers of cork stoppers since it is able to inhibit the development of other molds and it does not produce the compounds responsible for ‘cork-taint’, even in the presence of chlorophenols. Journal of Industrial Microbiology & Biotechnology (2000) 24, 256–261.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 42 (1986), S. 1404-1408 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-1327
    Keywords: Key words X-ray crystal structure ; Cytochrome c' ; Electron transfer protein ; Rhodocyclus gelatinosus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  Cytochromes c' are heme proteins found in photosynthetic and denitrifying bacteria, where they are presumably involved in electron transport. The cytochrome c' isolated from the bacterium Rhodocyclus gelatinosus (RGCP) forms a homodimer with each polypeptide containing 129 residues. It has been crystallised in ammonium sulfate at pH 6. Crystals belong to space group P3121 with cell parameters a = 70.2 Å and c = 126.8 Å, which corresponds to a dimer in the asymmetric unit (VM = 3.5 Å3 / Da). The crystal structure of RGCP was solved by the molecular replacement method and refined using data to 2.5-Å resolution. The final crystallographic R factor was 17.9% for all reflections (above 2 σ) in the resolution range 27.4 to 2.5 Å. The refined model includes 1876 non-hydrogen protein atoms and 56 water molecules. As typical of c–type cytochromes, the heme group is covalently bound to Cys-X-Y-Cys-His through thio-ether bonds, and His123 occupies the fifth axial coordination position. On the vacant "distal" site, Phe16 blocks the direct access to the sixth coordination site, which is in a predominantly hydrophobic environment. In spite of the low sequence homology among cytochromes c' the overall fold is similar. The monomer structure consists of 4 anti-parallel α-helices and has random coils in the loops between the helices, and at the N- and C-termini. The subunits cross each other to form an X shape.
    Type of Medium: Electronic Resource
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