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  • 1
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    Mitochondrial reactive oxygen species enable proinflammatory signaling through disulfide linkage of NEMO (2019)
    The American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2019
    Description: 〈p〉A major function of macrophages during infection is initiation of the proinflammatory response, leading to the secretion of cytokines that help to orchestrate the immune response. Here, we identify reactive oxygen species (ROS) as crucial mediators of proinflammatory signaling leading to cytokine secretion in 〈i〉Listeria monocytogenes–〈/i〉infected macrophages. ROS produced by NADPH oxidases (Noxes), such as Nox2, are key components of the macrophage response to invading pathogens; however, our data show that the ROS that mediated proinflammatory signaling were produced by mitochondria (mtROS). We identified the inhibitor of B (IB) kinase (IKK) complex regulatory subunit NEMO [nuclear factor B (NF-B) essential modulator] as a target for mtROS. Specifically, mtROS induced intermolecular covalent linkage of NEMO through disulfide bonds formed by Cys〈sup〉54〈/sup〉 and Cys〈sup〉347〈/sup〉, which was essential for activation of the IKK complex and subsequent signaling through the extracellular signal–regulated protein kinases 1 and 2 (ERK1/2) and NF-B pathways that eventually led to the secretion of proinflammatory cytokines. We thus identify mtROS-dependent disulfide linkage of NEMO as an essential regulatory step of the proinflammatory response of macrophages to bacterial infection.〈/p〉
    Print ISSN: 1945-0877
    Electronic ISSN: 1937-9145
    Topics: Biology , Medicine
    Published by The American Association for the Advancement of Science (AAAS)
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  • 2
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    Intrinsic Instability of Aberration-Corrected Electron Microscopes (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-10-16
    Description: Author(s): S. M. Schramm, S. J. van der Molen, and R. M. Tromp Aberration-corrected microscopes with subatomic resolution will impact broad areas of science and technology. However, the experimentally observed lifetime of the corrected state is just a few minutes. Here we show that the corrected state is intrinsically unstable; the higher its quality, the more ... [Phys. Rev. Lett. 109, 163901] Published Mon Oct 15, 2012
    Keywords: Nonlinear Dynamics, Fluid Dynamics, Classical Optics, etc.
    Print ISSN: 0031-9007
    Electronic ISSN: 1079-7114
    Topics: Physics
    Published by American Physical Society (APS)
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  • 3
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    Riboflavin kinase couples TNF receptor 1 to NADPH oxidase (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-07-31
    Description: Reactive oxygen species (ROS) produced by NADPH oxidase function as defence and signalling molecules related to innate immunity and various cellular responses. The activation of NADPH oxidase in response to plasma membrane receptor activation depends on the phosphorylation of cytoplasmic oxidase subunits, their translocation to membranes and the assembly of all NADPH oxidase components. Tumour necrosis factor (TNF) is a prominent stimulus of ROS production, but the molecular mechanisms by which TNF activates NADPH oxidase are poorly understood. Here we identify riboflavin kinase (RFK, formerly known as flavokinase) as a previously unrecognized TNF-receptor-1 (TNFR1)-binding protein that physically and functionally couples TNFR1 to NADPH oxidase. In mouse and human cells, RFK binds to both the TNFR1-death domain and to p22(phox), the common subunit of NADPH oxidase isoforms. RFK-mediated bridging of TNFR1 and p22(phox) is a prerequisite for TNF-induced but not for Toll-like-receptor-induced ROS production. Exogenous flavin mononucleotide or FAD was able to substitute fully for TNF stimulation of NADPH oxidase in RFK-deficient cells. RFK is rate-limiting in the synthesis of FAD, an essential prosthetic group of NADPH oxidase. The results suggest that TNF, through the activation of RFK, enhances the incorporation of FAD in NADPH oxidase enzymes, a critical step for the assembly and activation of NADPH oxidase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yazdanpanah, Benjamin -- Wiegmann, Katja -- Tchikov, Vladimir -- Krut, Oleg -- Pongratz, Carola -- Schramm, Michael -- Kleinridders, Andre -- Wunderlich, Thomas -- Kashkar, Hamid -- Utermohlen, Olaf -- Bruning, Jens C -- Schutze, Stefan -- Kronke, Martin -- England -- Nature. 2009 Aug 27;460(7259):1159-63. doi: 10.1038/nature08206. Epub 2009 Jul 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Medical Microbiology, Immunology and Hygiene, University of Cologne, Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19641494" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cytochrome b Group/metabolism ; Enzyme Activation ; Fibroblasts ; Flavin Mononucleotide/metabolism ; Flavin-Adenine Dinucleotide/biosynthesis/metabolism ; HeLa Cells ; Humans ; Isoenzymes/chemistry/metabolism ; Membrane Glycoproteins/metabolism ; Mice ; NADH, NADPH Oxidoreductases/metabolism ; NADPH Oxidase/chemistry/*metabolism ; Phosphotransferases (Alcohol Group Acceptor)/deficiency/genetics/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; Reactive Oxygen Species/metabolism ; Receptors, Tumor Necrosis Factor, Type I/chemistry/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    Message transmission: receptor controlled adenylate cyclase system (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-21
    Description: The adenylate cyclase system is composed of an activating hormone or neurotransmitter (H), its receptor (R), the guanosine triphosphate (GTP) binding protein (Gs), and the catalytic unit (C). The activation of the receptor R involves a transient change in conformation, from a loose binding of the neurotransmitter H to an extremely tight interaction, termed locking. The system is regulated in the activation steps and also by three deactivation processes. A guanosine triphosphatase activity is built into the Gs protein so that the active GsGTP has only a limited lifetime during which it is able to activate C. In addition, the continued occupation of R by H causes desensitization of R. Finally, there are inhibitory receptors, such as alpha-adrenergic and opiate receptors, which inhibit the adenylate cyclase by way of a specific GTP binding protein (Gi). Yet to be determined are the conformational transformations of pure R on binding of an agonist or a partial agonist; the genes that code for the many different receptors that activate the adenylate cyclase, and the possibility that the G components interact with systems in the cell other than the adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schramm, M -- Selinger, Z -- AM10451/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1350-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6147897" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*metabolism ; Animals ; Cyclic AMP/*physiology ; Enzyme Activation ; GTP Phosphohydrolases/metabolism ; GTP-Binding Proteins ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Guanylyl Imidodiphosphate/metabolism ; Membrane Lipids/physiology ; Neurotransmitter Agents/physiology ; Protein Conformation ; Receptors, Cell Surface/metabolism ; *Synaptic Transmission
    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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  • 5
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    Regulation of measles virus gene expression by P protein coiled-coil properties (2019)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2019
    Description: 〈p〉The polymerase of negative-stranded RNA viruses consists of the large protein (L) and the phosphoprotein (P), the latter serving both as a chaperon and a cofactor for L. We mapped within measles virus (MeV) P the regions responsible for binding and stabilizing L and showed that the coiled-coil multimerization domain (MD) of P is required for gene expression. MeV MD is kinked as a result of the presence of a stammer. Both restoration of the heptad regularity and displacement of the stammer strongly decrease or abrogate activity in a minigenome assay. By contrast, P activity is rather tolerant of substitutions within the stammer. Single substitutions at the "a" or "d" hydrophobic anchor positions with residues of variable hydrophobicity revealed that P functionality requires a narrow range of cohesiveness of its MD. Results collectively indicate that, beyond merely ensuring P oligomerization, the MD finely tunes viral gene expression through its cohesiveness.〈/p〉
    Electronic ISSN: 2375-2548
    Topics: Natural Sciences in General
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
    Electronic Resource
    Electronic Resource
    Role of Hexose Phosphate in Synthesis of Cellulose by Acetobacter Xylinum (1957)
    [s.l.] : Nature Publishing Group
    Nature 179 (1957), S. 28-29 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] DISSIMILATION of carbohydrate may proceed JL/ in Acetobacter species largely via the pentose cycle1-2. Thus, in A. xylinum. where synthesis of cellulose depends on oxidation of carbohydrate3, the possibility is presented that energy for the synthesis might be derived from the operation of the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/179028a0
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Formation of Erythrose-4-phosphate and Acetyl Phosphate by a Phosphorolytic Cleavage of Fructose-6-phosphate (1957)
    [s.l.] : Nature Publishing Group
    Nature 179 (1957), S. 1349-1350 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The micro-organisms were grown at 30 with continuous shaking for 20-24 hr. The cells were harvested by centrifugation and washed several times with distilled water. Extracts were prepared in 0-05-M histidine buffer pH 6-5 containing 0-5 per cent potassium chloride with the aid of a Nossal shaker3. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/1791349a0
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  • 8
    Electronic Resource
    Electronic Resource
    Cold-induced leakage of amylase from the zymogen granule and sealing of its membrane by specific lipids
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 135 (1967), S. 44-52 
    Details
    ISSN: 0005-2736
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(67)90006-5
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  • 9
    Electronic Resource
    Electronic Resource
    The proteins of the content of the secretory granules of the rat parotid gland
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 382 (1975), S. 552-564 
    Details
    ISSN: 0005-2736
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90222-9
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  • 10
    Electronic Resource
    Electronic Resource
    Non-parallel transport of membrane proteins and content proteins during assembly of the secretory granule in rat parotid gland
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 375 (1975), S. 87-105 
    Details
    ISSN: 0005-2736
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(75)90074-7
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