Biochemical and Biophysical Research Communications
Cloning and sequencing of a cDNA for human mitochondrial ubiquinone-binding protein of complex III
References (31)
- et al.
J. Biol. Chem.
(1975) - et al.
J. Biol. Chem.
(1983) - et al.
Arch. Biochem. Biophys.
(1980) - et al.
Biochem. Biophys. Res. Commun.
(1984) - et al.
Biochem. Biophys. Res. Commun.
(1986) - et al.
Biochem. Biophys. Res. Commun.
(1982) J. Theor. Biol.
(1976)- et al.
Biochem. Biophys. Res. Commun.
(1986) - et al.
Anal. Biochem.
(1986) - et al.
Biochem. Biophys. Res. Commun.
(1987)
Anal. Biochem.
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
Biochim. Biophys. Acta
Cited by (25)
Cell-permeable mitochondrial ubiquinol-cytochrome c reductase binding protein induces angiogenesis in vitro and in vivo
2015, Cancer LettersCitation Excerpt :As shown in Fig. 2D, western blot analysis of mitochondrial fractions confirmed that PTD-UQCRB localized to the mitochondrial inner-membrane, where endogenous UQCRB protein exists. The mitochondrial targeting signal of UQCRB (amino acids 1–35) could be responsible for delivery and functional localization of PTD-UQCRB to mitochondria [11]. Since UQCRB is a complex III subunit of the mitochondrial respiratory chain, PTD-UQCRB transduction may affect mROS production.
A mutation in the mitochondrial protein UQCRB promotes angiogenesis through the generation of mitochondrial reactive oxygen species
2014, Biochemical and Biophysical Research CommunicationsCitation Excerpt :However, information on the relationship between complex III and angiogenesis is limited. Ubiquinol-cytochrome c reductase binding protein (UQCRB), a nuclear-encoded 13.4-kDa subunit of complex III, has been shown to play a role in the electron transport and maintenance of complex III [5]. Recently, a potential role of UQCRB in angiogenesis has been demonstrated by identifying it as a target of the natural anti-angiogenesis inhibitor terpestacin [6].
Target identification of bioactive compounds
2012, Bioorganic and Medicinal ChemistryCitation Excerpt :They first synthesized biotinylated-terpestacin, which was then immobilized on a streptavidin-coated well plate, and four rounds of phage biopanning were conducted using T7 phages expressing functional human cDNA libraries. As a result, UQCRB, a 13.4 kDa subunit of complex III in the mitochondrial respiratory chain,32 was identified as a terpestacin-binding protein. Knockdown of UQCRB by siRNA resulted in inhibition of hypoxia-induced HIF-1α accumulation and VEGF expression in HT1080 cells.
Terpestacin inhibits tumor angiogenesis by targeting UQCRB of mitochondrial complex III and suppressing hypoxia-induced reactive oxygen species production and cellular oxygen sensing
2010, Journal of Biological ChemistryCitation Excerpt :In the present study we identified the binding protein of terpestacin and clarified the cellular mechanism underlying its effects on angiogenesis. We find that terpestacin specifically binds to the 13.4-kDa subunit (UQCRB in human; accession number NM_006294; QCR7 in yeast; Sub 6 in bovine or chicken) of Complex III in the mitochondrial respiratory chain (14). The biological activity of terpestacin correlates significantly with the response to UQCRB knockdown in mammalian cells.
Ubiquinol-Cytochrome-c Reductase from Human and Bovine Mitochondria
1995, Methods in Enzymology