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Electron Transport Complex III
Known as:
Dihydroubiquinone-Cytochrome-c Reductase
, Dihydroubiquinone Cytochrome c Reductase
, Ubihydroquinone-Cytochrome-c Reductase
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A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to…
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National Institutes of Health
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Related topics
Related topics
16 relations
Coenzyme Q cytochrome C reductase/Citrate synthase:CRto:Pt:Tiss:Qn
Coenzyme Q cytochrome C reductase:CCnt:Pt:Tiss:Qn
In Blood
Laccase
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Narrower (4)
Cytochrome bc1 Complex
Histiocytoid Cardiomyopathy
Rieske iron-sulfur protein
UQCRH protein, human
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2008
Highly Cited
2008
Mitochondrial complex III deficiency associated with a homozygous mutation in UQCRQ.
O. Barel
,
Z. Shorer
,
+7 authors
O. Birk
American Journal of Human Genetics
2008
Corpus ID: 7999680
Highly Cited
2003
Highly Cited
2003
Identification of Novel Mitochondrial Protein Components ofChlamydomonas reinhardtii. A Proteomic Approach1
R. van Lis
,
A. Atteia
,
G. Mendoza-Hernández
,
D. González-Halphen
Plant Physiology
2003
Corpus ID: 7148378
Pure mitochondria of the photosynthetic algaChlamydomonas reinhardtii were analyzed using blue native-polyacrylamide gel…
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Highly Cited
2003
Highly Cited
2003
A deletion in the human QP-C gene causes a complex III deficiency resulting in hypoglycaemia and lactic acidosis
S. Haut
,
M. Brivet
,
+7 authors
A. Slama
Human Genetics
2003
Corpus ID: 24273072
Mitochondrial respiratory chain complex III (ubiquinol-cytochrome c reductase) consists of 11 subunits, only one (cytochrome b…
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Highly Cited
2001
Highly Cited
2001
A mutant mitochondrial respiratory chain assembly protein causes complex III deficiency in patients with tubulopathy, encephalopathy and liver failure
P. Lonlay
,
I. Valnot
,
+12 authors
A. Rötig
Nature Genetics
2001
Corpus ID: 10132444
Complex III (CIII; ubiquinol cytochrome c reductase of the mitochondrial respiratory chain) catalyzes electron transfer from…
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Highly Cited
1999
Highly Cited
1999
Effects of resveratrol on the rat brain respiratory chain.
R. Zini
,
C. Morin
,
A. Bertelli
,
A. Bertelli
,
J. Tillement
Drugs under experimental and clinical research
1999
Corpus ID: 42050998
The aim of this work was to investigate the possible effects of resveratrol on the mitochondrial respiratory chain in rat brains…
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Highly Cited
1999
Highly Cited
1999
A mitochondrial cytochrome b mutation but no mutations of nuclearly encoded subunits in ubiquinol cytochrome c reductase (complex III) deficiency
I. Valnot
,
J. Kassis
,
+6 authors
A. Rötig
Human Genetics
1999
Corpus ID: 30584267
Abstract Ubiquinol cytochrome c reductase (complex III) deficiency represents a clinically heterogeneous group of mitochondrial…
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Highly Cited
1992
Highly Cited
1992
BCS1, a novel gene required for the expression of functional Rieske iron‐sulfur protein in Saccharomyces cerevisiae.
F. Nóbrega
,
M. Nóbrega
,
'. AlexanderTzagoloff
EMBO Journal
1992
Corpus ID: 9119030
Respiratory deficient pet mutants of Saccharomyces cerevisiae assigned to complementation group G2 define a new gene, named BCS1…
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Highly Cited
1991
Highly Cited
1991
Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide
G. Isaya
,
F. Kalousek
,
Wayne A. Fenton
,
L. E. Rosenberg
Journal of Cell Biology
1991
Corpus ID: 11493029
Many precursors of mitochondrial proteins are processed in two successive steps by independent matrix peptidases (MPP and MIP…
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Highly Cited
1988
Highly Cited
1988
Molecular basis for resistance to antimycin and diuron, Q-cycle inhibitors acting at the Qi site in the mitochondrial ubiquinol-cytochrome c reductase in Saccharomyces cerevisiae.
J. di Rago
,
A. Colson
Journal of Biological Chemistry
1988
Corpus ID: 40118636
Highly Cited
1975
Highly Cited
1975
Cytochrome c2 and reaction center of Rhodospeudomonas spheroides Ga. membranes. Extinction coefficients, content, half-reduction potentials, kinetics and electric field alterations.
P. Dutton
,
K. Petty
,
H. Bonner
,
Steven D. Morse
Biochimica et Biophysica Acta
1975
Corpus ID: 6102762
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