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Journal Abstract Search

98 related items for PubMed ID: 21224018

  • 1. Role of the C-terminal domain of the regulatory subunit of AHAS isozyme III: use of random mutagenesis with in vivo reconstitution (REM-ivrs).
    Slutzker A, Vyazmensky M, Chipman DM, Barak Z.
    Biochim Biophys Acta; 2011 Mar; 1814(3):449-55. PubMed ID: 21224018
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  • 3. Interactions between large and small subunits of different acetohydroxyacid synthase isozymes of Escherichia coli.
    Vyazmensky M, Zherdev Y, Slutzker A, Belenky I, Kryukov O, Barak Z, Chipman DM.
    Biochemistry; 2009 Sep 15; 48(36):8731-7. PubMed ID: 19653643
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  • 9. Acetohydroxyacid synthase isozyme I from Escherichia coli has unique catalytic and regulatory properties.
    Vinogradov V, Vyazmensky M, Engel S, Belenky I, Kaplun A, Kryukov O, Barak Z, Chipman DM.
    Biochim Biophys Acta; 2006 Mar 15; 1760(3):356-63. PubMed ID: 16326011
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  • 13. Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I.
    Belenky I, Steinmetz A, Vyazmensky M, Barak Z, Tittmann K, Chipman DM.
    FEBS J; 2012 Jun 15; 279(11):1967-79. PubMed ID: 22443469
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  • 14. High-level production of valine by expression of the feedback inhibition-insensitive acetohydroxyacid synthase in Saccharomyces cerevisiae.
    Takpho N, Watanabe D, Takagi H.
    Metab Eng; 2018 Mar 15; 46():60-67. PubMed ID: 29477860
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  • 20. Subunit-subunit interactions are weakened in mutant forms of acetohydroxy acid synthase insensitive to valine inhibition.
    Kyselková M, Janata J, Ságová-Marecková M, Kopecký J.
    Arch Microbiol; 2010 Mar 15; 192(3):195-200. PubMed ID: 20107768
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