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  • Articles  (3)
  • Substrate Specificity  (3)
  • 550 - Earth sciences
  • DATE/TIME; Date/time end; Elevation, maximum; Elevation, minimum; GLAC; Glaciers Austria; Kesselwandferner; Kesselwandferner, Ötztaler Alpen, Austria; KWF; Mass balance, total of the altitude zone; Sampling/measurements on glacier; Specific mass balance of the altitude zone; Total area of the altitude zone
  • 2005-2009  (3)
  • Physics  (3)
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  • Articles  (3)
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  • 1
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    Innate immune and chemically triggered oxidative stress modifies translational fidelity (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-11-27
    Description: Translational fidelity, essential for protein and cell function, requires accurate transfer RNA (tRNA) aminoacylation. Purified aminoacyl-tRNA synthetases exhibit a fidelity of one error per 10,000 to 100,000 couplings. The accuracy of tRNA aminoacylation in vivo is uncertain, however, and might be considerably lower. Here we show that in mammalian cells, approximately 1% of methionine (Met) residues used in protein synthesis are aminoacylated to non-methionyl-tRNAs. Remarkably, Met-misacylation increases up to tenfold upon exposing cells to live or non-infectious viruses, toll-like receptor ligands or chemically induced oxidative stress. Met is misacylated to specific non-methionyl-tRNA families, and these Met-misacylated tRNAs are used in translation. Met-misacylation is blocked by an inhibitor of cellular oxidases, implicating reactive oxygen species (ROS) as the misacylation trigger. Among six amino acids tested, tRNA misacylation occurs exclusively with Met. As Met residues are known to protect proteins against ROS-mediated damage, we propose that Met-misacylation functions adaptively to increase Met incorporation into proteins to protect cells against oxidative stress. In demonstrating an unexpected conditional aspect of decoding mRNA, our findings illustrate the importance of considering alternative iterations of the genetic code.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2785853/" 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/PMC2785853/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Netzer, Nir -- Goodenbour, Jeffrey M -- David, Alexandre -- Dittmar, Kimberly A -- Jones, Richard B -- Schneider, Jeffrey R -- Boone, David -- Eves, Eva M -- Rosner, Marsha R -- Gibbs, James S -- Embry, Alan -- Dolan, Brian -- Das, Suman -- Hickman, Heather D -- Berglund, Peter -- Bennink, Jack R -- Yewdell, Jonathan W -- Pan, Tao -- Z01 AI000542-20/Intramural NIH HHS/ -- Z01 AI000653-16/Intramural NIH HHS/ -- Z01 AI000658-16/Intramural NIH HHS/ -- Z01 AI001014-01/Intramural NIH HHS/ -- England -- Nature. 2009 Nov 26;462(7272):522-6. doi: 10.1038/nature08576.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19940929" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/physiology ; Animals ; Genetic Code ; HeLa Cells ; Humans ; *Immunity, Innate ; Ligands ; Methionine/genetics/*metabolism ; Mice ; Models, Genetic ; NADPH Oxidase/metabolism ; Orthomyxoviridae/physiology ; Oxidative Stress/drug effects/genetics/*physiology ; RNA, Transfer, Met/genetics/metabolism ; Reactive Oxygen Species/metabolism ; Substrate Specificity ; Toll-Like Receptors/immunology/metabolism ; Transfer RNA Aminoacylation/drug effects/*physiology
    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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  • 2
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    Neisseria meningitidis recruits factor H using protein mimicry of host carbohydrates (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-02-20
    Description: The complement system is an essential component of the innate and acquired immune system, and consists of a series of proteolytic cascades that are initiated by the presence of microorganisms. In health, activation of complement is precisely controlled through membrane-bound and soluble plasma-regulatory proteins including complement factor H (fH; ref. 2), a 155 kDa protein composed of 20 domains (termed complement control protein repeats). Many pathogens have evolved the ability to avoid immune-killing by recruiting host complement regulators and several pathogens have adapted to avoid complement-mediated killing by sequestering fH to their surface. Here we present the structure of a complement regulator in complex with its pathogen surface-protein ligand. This reveals how the important human pathogen Neisseria meningitidis subverts immune responses by mimicking the host, using protein instead of charged-carbohydrate chemistry to recruit the host complement regulator, fH. The structure also indicates the molecular basis of the host-specificity of the interaction between fH and the meningococcus, and informs attempts to develop novel therapeutics and vaccines.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2670278/" 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/PMC2670278/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, Muriel C -- Prosser, Beverly E -- Caesar, Joseph J E -- Kugelberg, Elisabeth -- Li, Su -- Zhang, Qian -- Quoraishi, Sadik -- Lovett, Janet E -- Deane, Janet E -- Sim, Robert B -- Roversi, Pietro -- Johnson, Steven -- Tang, Christoph M -- Lea, Susan M -- 083599/Wellcome Trust/United Kingdom -- G0400775/Medical Research Council/United Kingdom -- G0400775(71657)/Medical Research Council/United Kingdom -- G0500367/Medical Research Council/United Kingdom -- G0601195/Medical Research Council/United Kingdom -- G0601195(79743)/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- England -- Nature. 2009 Apr 16;458(7240):890-3. doi: 10.1038/nature07769. Epub 2009 Feb 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre for Molecular Microbiology and Infection, Imperial College, London SW7 2AZ, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19225461" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Bacterial/*chemistry/*metabolism ; Bacterial Proteins/*chemistry/*metabolism ; Binding Sites ; Carbohydrates/*chemistry ; Complement Factor H/*chemistry/immunology/*metabolism ; Crystallography, X-Ray ; Ligands ; Models, Molecular ; *Molecular Mimicry ; Neisseria meningitidis/chemistry/immunology/*metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; Substrate Specificity
    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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  • 3
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    Inhibitors selective for mycobacterial versus human proteasomes (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-09-18
    Description: Many anti-infectives inhibit the synthesis of bacterial proteins, but none selectively inhibits their degradation. Most anti-infectives kill replicating pathogens, but few preferentially kill pathogens that have been forced into a non-replicating state by conditions in the host. To explore these alternative approaches we sought selective inhibitors of the proteasome of Mycobacterium tuberculosis. Given that the proteasome structure is extensively conserved, it is not surprising that inhibitors of all chemical classes tested have blocked both eukaryotic and prokaryotic proteasomes, and no inhibitor has proved substantially more potent on proteasomes of pathogens than of their hosts. Here we show that certain oxathiazol-2-one compounds kill non-replicating M. tuberculosis and act as selective suicide-substrate inhibitors of the M. tuberculosis proteasome by cyclocarbonylating its active site threonine. Major conformational changes protect the inhibitor-enzyme intermediate from hydrolysis, allowing formation of an oxazolidin-2-one and preventing regeneration of active protease. Residues outside the active site whose hydrogen bonds stabilize the critical loop before and after it moves are extensively non-conserved. This may account for the ability of oxathiazol-2-one compounds to inhibit the mycobacterial proteasome potently and irreversibly while largely sparing the human homologue.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3172082/" 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/PMC3172082/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Gang -- Li, Dongyang -- de Carvalho, Luiz Pedro Sorio -- Deng, Haiteng -- Tao, Hui -- Vogt, Guillaume -- Wu, Kangyun -- Schneider, Jean -- Chidawanyika, Tamutenda -- Warren, J David -- Li, Huilin -- Nathan, Carl -- P01 AI056293/AI/NIAID NIH HHS/ -- P01 AI056293-05/AI/NIAID NIH HHS/ -- P01-AI056293/AI/NIAID NIH HHS/ -- R01 AI055549/AI/NIAID NIH HHS/ -- R01 AI055549-01/AI/NIAID NIH HHS/ -- R01AI070285/AI/NIAID NIH HHS/ -- England -- Nature. 2009 Oct 1;461(7264):621-6. doi: 10.1038/nature08357. Epub 2009 Sep 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Weill Cornell Medical College, New York, New York 10065, USA. gal2005@med.cornell.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19759536" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain/drug effects ; Humans ; Hydrogen Bonding ; Kinetics ; Models, Molecular ; Mycobacterium tuberculosis/*drug effects/*enzymology/growth & development ; Oxazolidinones/metabolism/pharmacology ; Protease Inhibitors/chemistry/*pharmacology ; Proteasome Endopeptidase Complex/chemistry/metabolism ; *Proteasome Inhibitors ; Protein Carbonylation/drug effects ; Protein Conformation/drug effects ; Protein Subunits ; Substrate Specificity ; Thiazoles/pharmacology ; Threonine/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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