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  • 1
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    Cullin–RING ubiquitin E3 ligase regulation by the COP9 signalosome (2016)
    Springer Nature
    In: Nature
    Details
    Publication Date: 2016-03-31
    Description: Cullin–RING ubiquitin E3 ligase regulation by the COP9 signalosome Nature 531, 7596 (2016). doi:10.1038/nature17416 Authors: Simone Cavadini, Eric S. Fischer, Richard D. Bunker, Alessandro Potenza, Gondichatnahalli M. Lingaraju, Kenneth N. Goldie, Weaam I. Mohamed, Mahamadou Faty, Georg Petzold, Rohan E. J. Beckwith, Ritesh B. Tichkule, Ulrich Hassiepen, Wassim Abdulrahman, Radosav S. Pantelic, Syota Matsumoto, Kaoru Sugasawa, Henning Stahlberg & Nicolas H. Thomä The cullin–RING ubiquitin E3 ligase (CRL) family comprises over 200 members in humans. The COP9 signalosome complex (CSN) regulates CRLs by removing their ubiquitin-like activator NEDD8. The CUL4A–RBX1–DDB1–DDB2 complex (CRL4ADDB2) monitors the genome for ultraviolet-light-induced DNA damage. CRL4ADBB2 is inactive in
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 2
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    Late-stage C–H functionalization of complex alkaloids and drug molecules via intermolecular rhodium-carbenoid insertion (2015)
    Springer Nature
    Details
    Publication Date: 2015-01-14
    Description: Article The ability to functionalize a C–H bond is useful in complex organic syntheses, but the scope of this approach is sometimes limited by its sensitivity to basic amines. Here, the authors achieve functionalization of amine-containing natural products by site-selective rhodium-carbene-mediated C–H insertion. Nature Communications doi: 10.1038/ncomms6943 Authors: Jing He, Lawrence G. Hamann, Huw M. L. Davies, Rohan E. J. Beckwith
    Electronic ISSN: 2041-1723
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 3
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    Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-10-06
    Description: Pathways for the reduction of protein disulfide bonds are found in all organisms and are required for the reductive recycling of certain enzymes including the essential protein ribonucleotide reductase. An Escherichia coli strain that lacks both thioredoxin reductase and glutathione reductase grows extremely poorly. Here, we show that a mutation occurring at high frequencies in the gene ahpC, encoding a peroxiredoxin, restores normal growth to this strain. This mutation is the result of a reversible expansion of a triplet nucleotide repeat sequence, leading to the addition of one amino acid that converts the AhpC protein from a peroxidase to a disulfide reductase. The ready mutational interconversion between the two activities could provide an evolutionary advantage to E. coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ritz, D -- Lim, J -- Reynolds, C M -- Poole, L B -- Beckwith, J -- R001 GM55090/GM/NIGMS NIH HHS/ -- R01 GM050389/GM/NIGMS NIH HHS/ -- R01 GM50389/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Oct 5;294(5540):158-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, 200 Longwood Avenue, Harvard Medical School, Boston, MA, 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11588261" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Benzene Derivatives/pharmacology ; Binding Sites ; Biological Evolution ; *DNA-Binding Proteins ; Disulfides/*metabolism ; Dithionitrobenzoic Acid/metabolism ; Escherichia coli/enzymology/*genetics/growth & development/metabolism ; Escherichia coli Proteins ; Genes, Bacterial ; Glutathione/metabolism ; Hydrogen Peroxide/metabolism ; Molecular Sequence Data ; Mutation ; NAD/metabolism ; NADH, NADPH Oxidoreductases/*metabolism ; Operon ; Oxidation-Reduction ; Oxidative Stress ; Peroxidases/chemistry/*genetics/*metabolism ; Peroxides/metabolism ; Peroxiredoxins ; Phenotype ; Repressor Proteins/metabolism ; Suppression, Genetic ; Transcription Factors/metabolism ; Transformation, Bacterial ; *Trinucleotide Repeat Expansion
    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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    Structure of a bacterial homologue of vitamin K epoxide reductase (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-01-30
    Description: Vitamin K epoxide reductase (VKOR) generates vitamin K hydroquinone to sustain gamma-carboxylation of many blood coagulation factors. Here, we report the 3.6 A crystal structure of a bacterial homologue of VKOR from Synechococcus sp. The structure shows VKOR in complex with its naturally fused redox partner, a thioredoxin-like domain, and corresponds to an arrested state of electron transfer. The catalytic core of VKOR is a four transmembrane helix bundle that surrounds a quinone, connected through an additional transmembrane segment with the periplasmic thioredoxin-like domain. We propose a pathway for how VKOR uses electrons from cysteines of newly synthesized proteins to reduce a quinone, a mechanism confirmed by in vitro reconstitution of vitamin K-dependent disulphide bridge formation. Our results have implications for the mechanism of the mammalian VKOR and explain how mutations can cause resistance to the VKOR inhibitor warfarin, the most commonly used oral anticoagulant.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919313/" 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/PMC2919313/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Weikai -- Schulman, Sol -- Dutton, Rachel J -- Boyd, Dana -- Beckwith, Jon -- Rapoport, Tom A -- GMO41883/PHS HHS/ -- K99 HL097083/HL/NHLBI NIH HHS/ -- K99 HL097083-01/HL/NHLBI NIH HHS/ -- K991K99HL097083/HL/NHLBI NIH HHS/ -- R00 HL097083/HL/NHLBI NIH HHS/ -- R01 GM041883/GM/NIGMS NIH HHS/ -- T32 GM007753/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2010 Jan 28;463(7280):507-12. doi: 10.1038/nature08720.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA. weikai@crystal.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20110994" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anticoagulants ; Bacterial Proteins/chemistry ; Catalytic Domain ; Disulfides/chemistry ; Drug Resistance/genetics ; Electron Transport ; Humans ; Membrane Proteins/chemistry ; Mixed Function Oxygenases/*chemistry/genetics ; *Models, Molecular ; Protein Structure, Tertiary ; Synechococcus/*enzymology ; Vitamin K Epoxide Reductases ; Warfarin
    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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  • 5
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    A methyl transferase links the circadian clock to the regulation of alternative splicing (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-10-22
    Description: Circadian rhythms allow organisms to time biological processes to the most appropriate phases of the day-night cycle. Post-transcriptional regulation is emerging as an important component of circadian networks, but the molecular mechanisms linking the circadian clock to the control of RNA processing are largely unknown. Here we show that PROTEIN ARGININE METHYL TRANSFERASE 5 (PRMT5), which transfers methyl groups to arginine residues present in histones and Sm spliceosomal proteins, links the circadian clock to the control of alternative splicing in plants. Mutations in PRMT5 impair several circadian rhythms in Arabidopsis thaliana and this phenotype is caused, at least in part, by a strong alteration in alternative splicing of the core-clock gene PSEUDO RESPONSE REGULATOR 9 (PRR9). Furthermore, genome-wide studies show that PRMT5 contributes to the regulation of many pre-messenger-RNA splicing events, probably by modulating 5'-splice-site recognition. PRMT5 expression shows daily and circadian oscillations, and this contributes to the mediation of the circadian regulation of expression and alternative splicing of a subset of genes. Circadian rhythms in locomotor activity are also disrupted in dart5-1, a mutant affected in the Drosophila melanogaster PRMT5 homologue, and this is associated with alterations in splicing of the core-clock gene period and several clock-associated genes. Our results demonstrate a key role for PRMT5 in the regulation of alternative splicing and indicate that the interplay between the circadian clock and the regulation of alternative splicing by PRMT5 constitutes a common mechanism that helps organisms to synchronize physiological processes with daily changes in environmental conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez, Sabrina E -- Petrillo, Ezequiel -- Beckwith, Esteban J -- Zhang, Xu -- Rugnone, Matias L -- Hernando, C Esteban -- Cuevas, Juan C -- Godoy Herz, Micaela A -- Depetris-Chauvin, Ana -- Simpson, Craig G -- Brown, John W S -- Cerdan, Pablo D -- Borevitz, Justin O -- Mas, Paloma -- Ceriani, M Fernanda -- Kornblihtt, Alberto R -- Yanovsky, Marcelo J -- Howard Hughes Medical Institute/ -- England -- Nature. 2010 Nov 4;468(7320):112-6. doi: 10.1038/nature09470. Epub 2010 Oct 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉IFEVA, Facultad de Agronomia, UBA-CONICET, C1417DSE Buenos Aires, Argentina.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20962777" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing/*genetics ; Animals ; Arabidopsis/enzymology/genetics/*physiology/radiation effects ; Arabidopsis Proteins/genetics/*metabolism ; Base Sequence ; Circadian Clocks/genetics/*physiology ; Circadian Rhythm/genetics/*physiology ; Darkness ; Drosophila Proteins/genetics/*metabolism ; Drosophila melanogaster/enzymology/genetics/*physiology/radiation effects ; Gene Expression Profiling ; Gene Expression Regulation, Plant ; Light ; Methylation ; Mutation ; Period Circadian Proteins/genetics ; Phenotype ; Protein Methyltransferases/genetics/*metabolism ; Protein-Arginine N-Methyltransferases/genetics/*metabolism ; RNA Precursors/genetics/metabolism ; RNA Splice Sites/genetics ; RNA, Messenger/genetics/metabolism ; Spliceosomes/metabolism ; Transcription Factors/genetics
    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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  • 6
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    "Sequence-gazing?" (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beckwith, J -- New York, N.Y. -- Science. 1991 Mar 8;251(4998):1161-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006404" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics ; Base Sequence ; Escherichia coli/*genetics ; *Genes, Bacterial ; *Open Reading Frames
    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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  • 7
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    Misreading Dr. Venter's genome (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-12-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beckwith, Jon -- Morris, Corey -- New York, N.Y. -- Science. 2007 Dec 7;318(5856):1550.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18063771" target="_blank"〉PubMed〈/a〉
    Keywords: Antisocial Personality Disorder/*genetics ; Genetic Predisposition to Disease ; *Genome, Human ; Humans ; Male ; *Minisatellite Repeats ; Monoamine Oxidase/*genetics
    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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  • 8
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    Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-09-01
    Description: The presence of lipopolysaccharide (LPS) on the cell surface of Gram-negative bacteria is critical for viability. A conserved beta-barrel membrane protein LptD (lipopolysaccharide transport protein D) translocates LPS from the periplasm across the outer membrane (OM). In Escherichia coli, this protein contains two disulfide bonds and forms the OM LPS translocon with the lipoprotein LptE. Here, we identified seven in vivo states on the oxidative-folding pathway of LptD. Proper assembly involved a nonfunctional intermediate containing non-native disulfides. Intermediate formation required the oxidase DsbA, and subsequent maturation to the active form with native disulfides was triggered by LptE. Thus, disulfide bond-dependent protein folding of LptD requires the proper assembly of a two-protein complex to promote disulfide bond rearrangement.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3489181/" 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/PMC3489181/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chng, Shu-Sin -- Xue, Mingyu -- Garner, Ronald A -- Kadokura, Hiroshi -- Boyd, Dana -- Beckwith, Jonathan -- Kahne, Daniel -- 41883/PHS HHS/ -- AI081059/AI/NIAID NIH HHS/ -- R01 AI081059/AI/NIAID NIH HHS/ -- R01 GM041883/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Sep 28;337(6102):1665-8. Epub 2012 Aug 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22936569" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/chemistry/genetics/*metabolism ; Biological Transport ; Cystine/genetics/*metabolism ; Escherichia coli/genetics/*metabolism ; Escherichia coli Proteins/chemistry/genetics/*metabolism ; Lipopolysaccharides/*metabolism ; Protein Disulfide-Isomerases/metabolism ; Protein Folding ; Protein Structure, Secondary
    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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  • 9
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    Turkey must end violent response to protests (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-07-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altindis, Emrah -- Alpar, M Ali -- Aksay, Emre -- Beckwith, Jonathan -- Bokel, Christian -- Curl, Robert F -- Darnell, Robert B -- Elledge, Stephen J -- Erman, Burak -- Frahm, Jens -- Goff, Stephen P -- Greengard, Paul -- Hoffmann, Roald -- Ilhan, Bayazit -- Kaslin, Jan -- Lipkin, Steven M -- Poulopoulou, Cornelia -- Raz, Erez -- Rubin, Mark A -- Salturk, Mehmet -- Schrock, Richard R -- Trautmann, Alain -- Unutmaz, Derya -- Weinstein, Harel -- Kizil, Caghan -- New York, N.Y. -- Science. 2013 Jul 19;341(6143):236. doi: 10.1126/science.341.6143.236-a.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23869001" target="_blank"〉PubMed〈/a〉
    Keywords: Asphyxia/*chemically induced/mortality ; Hospitalization/statistics & numerical data ; *Human Rights ; Humans ; Tear Gases/*toxicity ; Turkey ; Violence/*prevention & control ; Wounds and Injuries/etiology/mortality
    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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  • 10
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    An open letter to Elias Zerhouni (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altman, Sidney -- Bassler, Bonnie L -- Beckwith, Jon -- Belfort, Marlene -- Berg, Howard C -- Bloom, Barry -- Brenchley, Jean E -- Campbell, Allan -- Collier, R John -- Connell, Nancy -- Cozzarelli, Nicholas R -- Craig, Nancy L -- Darst, Seth -- Ebright, Richard H -- Elledge, Stephen J -- Falkow, Stanley -- Galan, Jorge E -- Gottesman, Max -- Gourse, Richard -- Grindley, Nigel D F -- Gross, Carol A -- Grossman, Alan -- Hochschild, Ann -- Howe, Martha -- Hurwitz, Jerard -- Isberg, Ralph R -- Kaplan, Samuel -- Kornberg, Arthur -- Kustu, Sydney G -- Landick, Robert C -- Landy, Arthur -- Levy, Stuart B -- Losick, Richard -- Long, Sharon R -- Maloy, Stanley R -- Mekalanos, John J -- Neidhardt, Frederick C -- Pace, Norman R -- Ptashne, Mark -- Roberts, Jeffrey W -- Roth, John R -- Rothman-Denes, Lucia B -- Salyers, Abigail -- Schaechter, Moselio -- Shapiro, Lucy -- Silhavy, Thomas J -- Simon, Melvin I -- Walker, Graham -- Yanofsky, Charles -- Zinder, Norton -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1409-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746409" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Warfare ; *Biomedical Research/economics ; *Bioterrorism ; Financing, Government ; *Microbiology ; *National Institutes of Health (U.S.) ; Peer Review, Research ; Public Health ; *Research Support as Topic ; United States
    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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