| Name | ND5 |
|---|---|
| Synonyms | MT ND5; MTND 5; MTND5; NADH dehydrogenase 5; NADH dehydrogenase subunit 5; ND5; mitochondrially encoded NADH dehydrogenase 5; NADH dehydrogenase 5s… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 18291703 | Dlaskova A, Hlavata L, Jezek P: Oxidative stress caused by blocking of mitochondrial complex I H (+) pumping as a link in aging/disease vicious cycle. Int J Biochem Cell Biol. 2008;40(9):1792-805. Epub 2008 Jan 19. Rotenone caused a 5-fold J (m) increase (AC (50) 2 microM), which was attenuated by uncoupling, membrane potential (DeltaPsi (m)), and DeltapH-collapse, since addition of FCCP (IC (50) 55 nM), valinomycin, and nigericin prevented this increase. A hydrophobic amiloride that acts on the ND5 subunit and inhibits Complex I H (+) pumping enhanced J (m) and even countered the FCCP effect (AC (50) 0.3 microM). |
3(0,0,0,3) | Details |
| 12079358 | Cardol P, Matagne RF, Remacle C: Impact of mutations affecting ND mitochondria-encoded subunits on the activity and assembly of complex I in Chlamydomonas. J Mol Biol. 2002 Jun 21;319(5):1211-21. The mitochondrial rotenone-sensitive NADH:ubiquinone oxidoreductase (complex I) comprises more than 35 subunits, the majority of which are encoded by the nucleus. In Chlamydomonas reinhardtii, only five components (ND1, ND2, ND4, ND5 and ND6) are coded for by the mitochondrial genome. |
2(0,0,0,2) | Details |
| 20074573 | Nakamaru-Ogiso E, Han H, Matsuno-Yagi A, Keinan E, Sinha SC, Yagi T, Ohnishi T: The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor. FEBS Lett. 2010 Mar 5;584(5):883-8. Epub 2010 Jan 13. We found that [3H] BPA was photo-crosslinked to ND2, ND1 and ND5 subunits, by the three dimensional separation (blue-native/doubled SDS-PAGE) of [3H] BPA-treated bovine heart submitochondrial particles. The cross-linking was blocked by rotenone. |
1(0,0,0,1) | Details |
| 1332758 | Finel M, Skehel JM, Albracht SP, Fearnley IM, Walker JE: Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme. Biochemistry. 1992 Nov 24;31(46):11425-34. The line shapes of the EPR spectra of the Fe-S clusters are slightly broadened relative to spectra measured on complex I purified by conventional means, and the quinone reductase activity is insensitive to rotenone. The sequences of many of them contain hydrophobic segments that could be membrane spanning, including at least two mitochondrial gene products, ND4 and ND5. |
1(0,0,0,1) | Details |
| 11695835 | Chomyn A: Mitochondrial genetic control of assembly and function of complex I in mammalian cells. J Bioenerg Biomembr. 2001 Jun;33(3):251-7. Subsequently, we isolated several mutants affected in one or another of the mtDNA-encoded subunits of complex I by exposing established cell lines to high concentrations of rotenone. In fact, the synthesis of the ND5 polypeptide is rate limiting for the activity of the enzyme. |
1(0,0,0,1) | Details |
| 7823960 | Hofhaus G, Attardi G: Efficient selection and characterization of mutants of a human cell line which are defective in mitochondrial DNA-encoded subunits of respiratory NADH dehydrogenase. Mol Cell Biol. 1995 Feb;15(2):964-74. In the course of analysis of eight mutants of the human cell line VA2B selected for their resistance to high concentrations of the complex I inhibitor rotenone, seven were found to be respiration deficient, and among these, six exhibited a specific defect of complex I. A detailed molecular analysis of the six complex I-deficient mutants revealed that two of them exhibited a frameshift mutation in the ND4 gene, in homoplasmic or in heteroplasmic form, resulting in the complete or partial loss, respectively, of the ND4 subunit; two other mutants exhibited a frameshift mutation in the ND5 gene, in near-homoplasmic or heteroplasmic form, resulting in the ND5 subunit being undetectable or strongly decreased, respectively. |
1(0,0,0,1) | Details |