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Items: 1 to 20 of 142

1.

Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).

Schneider D, Pohl T, Walter J, Dörner K, Kohlstädt M, Berger A, Spehr V, Friedrich T.

Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):735-9. doi: 10.1016/j.bbabio.2008.03.003. Epub 2008 Mar 15. Review.

2.

Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli.

Erhardt H, Steimle S, Muders V, Pohl T, Walter J, Friedrich T.

Biochim Biophys Acta. 2012 Jun;1817(6):863-71. doi: 10.1016/j.bbabio.2011.10.008. Epub 2011 Oct 28.

3.

Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (respiratory complex I).

Friedrich T, Dekovic DK, Burschel S.

Biochim Biophys Acta. 2016 Mar;1857(3):214-23. doi: 10.1016/j.bbabio.2015.12.004. Epub 2015 Dec 9. Review.

4.
5.

Iron-sulfur cluster N7 of the NADH:ubiquinone oxidoreductase (complex I) is essential for stability but not involved in electron transfer.

Pohl T, Bauer T, Dörner K, Stolpe S, Sell P, Zocher G, Friedrich T.

Biochemistry. 2007 Jun 5;46(22):6588-96. Epub 2007 May 10.

PMID:
17489563
6.

Semiquinone and cluster N6 signals in His-tagged proton-translocating NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.

Narayanan M, Gabrieli DJ, Leung SA, Elguindy MM, Glaser CA, Saju N, Sinha SC, Nakamaru-Ogiso E.

J Biol Chem. 2013 May 17;288(20):14310-9. doi: 10.1074/jbc.M113.467803. Epub 2013 Mar 29.

7.

Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I).

Pohl T, Spatzal T, Aksoyoglu M, Schleicher E, Rostas AM, Lay H, Glessner U, Boudon C, Hellwig P, Weber S, Friedrich T.

Biochim Biophys Acta. 2010 Dec;1797(12):1894-900. doi: 10.1016/j.bbabio.2010.10.013. Epub 2010 Oct 16.

8.

Lambda Red-mediated mutagenesis and efficient large scale affinity purification of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).

Pohl T, Uhlmann M, Kaufenstein M, Friedrich T.

Biochemistry. 2007 Sep 18;46(37):10694-702. Epub 2007 Aug 28.

PMID:
17722886
9.

Catalytic importance of acidic amino acids on subunit NuoB of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).

Flemming D, Hellwig P, Lepper S, Kloer DP, Friedrich T.

J Biol Chem. 2006 Aug 25;281(34):24781-9. Epub 2006 Jun 28.

10.

Iron-sulfur cluster N2 of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I) is located on subunit NuoB.

Flemming D, Schlitt A, Spehr V, Bischof T, Friedrich T.

J Biol Chem. 2003 Nov 28;278(48):47602-9. Epub 2003 Sep 15.

11.

Nucleotide-induced conformational changes in the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).

Pohl T, Schneider D, Hielscher R, Stolpe S, Dörner K, Kohlstädt M, Böttcher B, Hellwig P, Friedrich T.

Biochem Soc Trans. 2008 Oct;36(Pt 5):971-5. doi: 10.1042/BST0360971.

PMID:
18793172
12.

Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli.

Leif H, Sled VD, Ohnishi T, Weiss H, Friedrich T.

Eur J Biochem. 1995 Jun 1;230(2):538-48.

13.

Role of the conserved arginine 274 and histidine 224 and 228 residues in the NuoCD subunit of complex I from Escherichia coli.

Belevich G, Euro L, Wikström M, Verkhovskaya M.

Biochemistry. 2007 Jan 16;46(2):526-33.

PMID:
17209562
14.

Heterologous production, isolation, characterization and crystallization of a soluble fragment of the NADH:ubiquinone oxidoreductase (complex I) from Aquifex aeolicus.

Kohlstädt M, Dörner K, Labatzke R, Koç C, Heilscher R, Schiltz E, Einsle O, Hellwig P, Friedrich T.

Biochemistry. 2008 Dec 9;47(49):13036-45. doi: 10.1021/bi801307n.

PMID:
19006332
15.

Semiquinone intermediates are involved in the energy coupling mechanism of E. coli complex I.

Narayanan M, Leung SA, Inaba Y, Elguindy MM, Nakamaru-Ogiso E.

Biochim Biophys Acta. 2015 Aug;1847(8):681-9. doi: 10.1016/j.bbabio.2015.04.004. Epub 2015 Apr 11.

16.

Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.

Narayanan M, Sakyiama JA, Elguindy MM, Nakamaru-Ogiso E.

J Biochem. 2016 Oct;160(4):205-215. Epub 2016 Apr 26.

PMID:
27118783
17.

Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.

Zhu S, Vik SB.

J Biol Chem. 2015 Aug 21;290(34):20761-73. doi: 10.1074/jbc.M115.660381. Epub 2015 Jul 1.

18.

Roles of semiquinone species in proton pumping mechanism by complex I.

Nakamaru-Ogiso E, Narayanan M, Sakyiama JA.

J Bioenerg Biomembr. 2014 Aug;46(4):269-77. doi: 10.1007/s10863-014-9557-9. Epub 2014 Jul 31. Review.

19.

Characterization of two novel redox groups in the respiratory NADH:ubiquinone oxidoreductase (complex I).

Friedrich T, Brors B, Hellwig P, Kintscher L, Rasmussen T, Scheide D, Schulte U, Mäntele W, Weiss H.

Biochim Biophys Acta. 2000 Aug 15;1459(2-3):305-9. Review.

20.

Apoptosis-inducing Factor (AIF) and Its Family Member Protein, AMID, Are Rotenone-sensitive NADH:Ubiquinone Oxidoreductases (NDH-2).

Elguindy MM, Nakamaru-Ogiso E.

J Biol Chem. 2015 Aug 21;290(34):20815-26. doi: 10.1074/jbc.M115.641498. Epub 2015 Jun 10.

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