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Page 1
Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.
Cell. 2012 Jan 20;148(1-2):150-63. doi: 10.1016/j.cell.2011.11.024.
Cell. 2012.
PMID: 22265408
Free PMC article.
Characterization of the membrane domain Nqo11 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans.
Kao MC, Di Bernardo S, Matsuno-Yagi A, Yagi T.
Kao MC, et al. Among authors: di bernardo s.
Biochemistry. 2002 Apr 2;41(13):4377-84. doi: 10.1021/bi025525d.
Biochemistry. 2002.
PMID: 11914084
Item in Clipboard
Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH:ubiquinone oxidoreductase (complex I).
Zu Y, Di Bernardo S, Yagi T, Hirst J.
Zu Y, et al. Among authors: di bernardo s.
Biochemistry. 2002 Aug 6;41(31):10056-69. doi: 10.1021/bi026026f.
Biochemistry. 2002.
PMID: 12146970
Item in Clipboard
Characterization of the membrane domain subunit NuoJ (ND6) of the NADH-quinone oxidoreductase from Escherichia coli by chromosomal DNA manipulation.
Kao MC, Di Bernardo S, Nakamaru-Ogiso E, Miyoshi H, Matsuno-Yagi A, Yagi T.
Kao MC, et al. Among authors: di bernardo s.
Biochemistry. 2005 Mar 8;44(9):3562-71. doi: 10.1021/bi0476477.
Biochemistry. 2005.
PMID: 15736965
Item in Clipboard
Characterization and topology of the membrane domain Nqo10 subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans.
Kao MC, Di Bernardo S, Matsuno-Yagi A, Yagi T.
Kao MC, et al. Among authors: di bernardo s.
Biochemistry. 2003 Apr 22;42(15):4534-43. doi: 10.1021/bi034166z.
Biochemistry. 2003.
PMID: 12693950
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Functional roles of four conserved charged residues in the membrane domain subunit NuoA of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli.
Kao MC, Di Bernardo S, Perego M, Nakamaru-Ogiso E, Matsuno-Yagi A, Yagi T.
Kao MC, et al. Among authors: di bernardo s.
J Biol Chem. 2004 Jul 30;279(31):32360-6. doi: 10.1074/jbc.M403885200. Epub 2004 Jun 2.
J Biol Chem. 2004.
PMID: 15175326
Free article.
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