(Q34429365)

2 August 2017

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title

Exploring the catalytic core of complex I by Yarrowia lipolytica yeast genetics (English)

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2 August 2017

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Kerscher S

1

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2 August 2017

Kashani-Poor N

2

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2 August 2017

Zwicker K

3

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2 August 2017

Zickermann V

4

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2 August 2017

Brandt U

5

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2 August 2017

1 June 2001

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Journal of Bioenergetics and Biomembranes

2 August 2017

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2 August 2017

33

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2 August 2017

3

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2 August 2017

187-196

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https://scigraph.springernature.com/pub.10.1023/a:1010726818165

2 August 2017

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Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica

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The NuoI subunit of the Rhodobacter capsulatus respiratory Complex I (equivalent to the bovine TYKY subunit) is required for proper assembly of the membraneous and peripheral domains of the enzyme

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12 December 2020

Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase).

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12 December 2020

Functional analysis of upstream regulating regions from the Yarrowia lipolytica XPR2 promoter

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12 December 2020

The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH.

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Characterization of the putative 2x[4Fe-4S]-binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Expression, reconstitution, and EPR characterization

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Efficient large scale purification of his-tagged proton translocating NADH:ubiquinone oxidoreductase (complex I) from the strictly aerobic yeast Yarrowia lipolytica

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The first nuclear-encoded complex I mutation in a patient with Leigh syndrome

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The iron-sulfur clusters in the two related forms of mitochondrial NADH: ubiquinone oxidoreductase made by Neurospora crassa

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Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems

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Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy

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12 December 2020

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12 December 2020

The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors.

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12 December 2020

Analysis of the pathogenic human mitochondrial mutation ND1/3460, and mutations of strictly conserved residues in its vicinity, using the bacterium Paracoccus denitrificans

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12 December 2020

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12 December 2020

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12 December 2020

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12 December 2020

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12 December 2020

Iron-sulfur N-1 clusters studied in NADH-ubiquinone oxidoreductase and in soluble NADH dehydrogenase

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12 December 2020

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12 December 2020

An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria

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12 December 2020

Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction

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12 December 2020

Function of Conserved Acidic Residues in the PSST Homologue of Complex I (NADH:Ubiquinone Oxidoreductase) fromYarrowia lipolytica

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12 December 2020

Photolabelling of a mitochondrially encoded subunit of NADH dehydrogenase with [3H]dihydrorotenone.

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12 December 2020

A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex.

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12 December 2020

Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice.

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12 December 2020

Identifiers

DOI

10.1023/A:1010726818165

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Dimensions Publication ID

2 August 2017

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