(Q56531442)

https://api.crossref.org/works/10.1074%2FJBC.M002074200

NADH:ubiquinone oxidoreductase from bovine heart mitochondria: sequence of a novel 17.2-kDa subunit.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

The bacterial energy-transducing NADH-quinone oxidoreductases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

In vivo dissection of the mitochondrial respiratory NADH: ubiquinone oxidoreductase (complex I).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Iron-sulfur clusters/semiquinones in complex I.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Properties of the common inhibitor-binding domain in mitochondrial NADH-dehydrogenase (complex I).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Redox components and structure of the respiratory NADH:ubiquinone oxidoreductase (complex I).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

The complex I from Rhodobacter capsulatus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Low molecular weight analogs of coenzyme Q as hydrogen acceptors and donors in systems of the respiratory chain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Kinetics of the mitochondrial NADH-ubiquinone oxidoreductase interaction with hexammineruthenium(III).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

An Algorithm for Least-Squares Estimation of Nonlinear Parameters

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

NADH-quinone oxidoreductase, the most complex complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Kinetics of the mitochondrial three-subunit NADH dehydrogenase interaction with hexammineruthenium(III).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Disruption of the gene encoding the NADH-binding subunit of NADH: ubiquinone oxidoreductase in Neurospora crassa. Formation of a partially assembled enzyme without FMN and the iron-sulphur cluster N-3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Structural organization of complex I from bovine mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Natural variation in the potency and binding sites of mitochondrial quinone-like inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

NADH-quinone oxidoreductase: PSST subunit couples electron transfer from iron-sulfur cluster N2 to quinone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200

Role of Deprotonation Events in Ubihydroquinone:CytochromecOxidoreductase from Bovine Heart and Yeast Mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002074200