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Journal Abstract Search

211 related items for PubMed ID: 18312271

  • 1.
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  • 2. TusA (YhhP) and IscS are required for molybdenum cofactor-dependent base-analog detoxification.
    Kozmin SG, Stepchenkova EI, Schaaper RM.
    Microbiologyopen; 2013 Oct; 2(5):743-55. PubMed ID: 23894086
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  • 4. Molybdenum cofactor-dependent resistance to N-hydroxylated base analogs in Escherichia coli is independent of MobA function.
    Kozmin SG, Schaaper RM.
    Mutat Res; 2007 Jun 01; 619(1-2):9-15. PubMed ID: 17349664
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  • 6. Crystal structure of the hydroxylaminopurine resistance protein, YiiM, and its putative molybdenum cofactor-binding catalytic site.
    Namgung B, Kim JH, Song WS, Yoon SI.
    Sci Rep; 2018 Feb 19; 8(1):3304. PubMed ID: 29459651
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  • 7. The Chlamydomonas reinhardtii molybdenum cofactor enzyme crARC has a Zn-dependent activity and protein partners similar to those of its human homologue.
    Chamizo-Ampudia A, Galvan A, Fernandez E, Llamas A.
    Eukaryot Cell; 2011 Oct 19; 10(10):1270-82. PubMed ID: 21803866
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  • 8. Hypersensitivity of Escherichia coli Delta(uvrB-bio) mutants to 6-hydroxylaminopurine and other base analogs is due to a defect in molybdenum cofactor biosynthesis.
    Kozmin SG, Pavlov YI, Dunn RL, Schaaper RM.
    J Bacteriol; 2000 Jun 19; 182(12):3361-7. PubMed ID: 10852865
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  • 9. Catalytic electrochemistry of the bacterial Molybdoenzyme YcbX.
    Kalimuthu P, Harmer JR, Baldauf M, Hassan AH, Kruse T, Bernhardt PV.
    Biochim Biophys Acta Bioenerg; 2022 Oct 01; 1863(7):148579. PubMed ID: 35640667
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  • 10. A critical role for the putative NCS2 nucleobase permease YjcD in the sensitivity of Escherichia coli to cytotoxic and mutagenic purine analogs.
    Kozmin SG, Stepchenkova EI, Chow SC, Schaaper RM.
    mBio; 2013 Oct 29; 4(6):e00661-13. PubMed ID: 24169576
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  • 12. The twists and turns of enzyme function.
    White RH.
    J Bacteriol; 2010 Apr 29; 192(8):2023-5. PubMed ID: 20154124
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  • 13. Base analog N6-hydroxylaminopurine mutagenesis in Escherichia coli: genetic control and molecular specificity.
    Pavlov YI, Suslov VV, Shcherbakova PV, Kunkel TA, Ono A, Matsuda A, Schaaper RM.
    Mutat Res; 1996 Oct 25; 357(1-2):1-15. PubMed ID: 8876675
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  • 14. Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three Escherichia coli proteins.
    Stallmeyer B, Nerlich A, Schiemann J, Brinkmann H, Mendel RR.
    Plant J; 1995 Nov 25; 8(5):751-62. PubMed ID: 8528286
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  • 15. Rhodobacter capsulatus XdhC is involved in molybdenum cofactor binding and insertion into xanthine dehydrogenase.
    Neumann M, Schulte M, Jünemann N, Stöcklein W, Leimkühler S.
    J Biol Chem; 2006 Jun 09; 281(23):15701-8. PubMed ID: 16597619
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  • 16. Iron-Dependent Regulation of Molybdenum Cofactor Biosynthesis Genes in Escherichia coli.
    Zupok A, Gorka M, Siemiatkowska B, Skirycz A, Leimkühler S.
    J Bacteriol; 2019 Sep 01; 201(17):. PubMed ID: 31235512
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  • 17. Identification of YdhV as the First Molybdoenzyme Binding a Bis-Mo-MPT Cofactor in Escherichia coli.
    Reschke S, Duffus BR, Schrapers P, Mebs S, Teutloff C, Dau H, Haumann M, Leimkühler S.
    Biochemistry; 2019 Apr 30; 58(17):2228-2242. PubMed ID: 30945846
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  • 18. Electrochemically driven catalysis of the bacterial molybdenum enzyme YiiM.
    Kalimuthu P, Harmer JR, Baldauf M, Hassan AH, Kruse T, Bernhardt PV.
    Biochim Biophys Acta Bioenerg; 2022 Mar 01; 1863(3):148523. PubMed ID: 34921810
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  • 19. Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft.
    Nichols JD, Xiang S, Schindelin H, Rajagopalan KV.
    Biochemistry; 2007 Jan 09; 46(1):78-86. PubMed ID: 17198377
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  • 20. Genetic analysis of tellurate reduction reveals the selenate/tellurate reductase genes ynfEF and the transcriptional regulation of moeA by NsrR in Escherichia coli.
    Fujita D, Tobe R, Tajima H, Anma Y, Nishida R, Mihara H.
    J Biochem; 2021 Apr 29; 169(4):477-484. PubMed ID: 33136147
    [Abstract] [Full Text] [Related]

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