| Name | protein is |
|---|---|
| Synonyms | ANX 2; p36; LIP 2; LIP2; ANX2; ANX2L4; ANX2P1; ANX2P2… |
| Name | rotenone |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 11696188 | Svensson AS, Rasmusson AG: Light-dependent gene expression for proteins in the respiratory chain of potato leaves. Plant J. 2001 Oct;28(1):73-82. Corresponding immunodetected NDA protein is specifically decreased in mitochondria isolated from dark-treated plants, accompanied by a lower capacity for internal rotenone-insensitive oxidation. |
31(0,1,1,1) | Details |
| 11479321 | Bai Y, Hajek P, Chomyn A, Chan E, Seo BB, Matsuno-Yagi A, Yagi T, Attardi G: Lack of complex I activity in human cells carrying a mutation in MtDNA-encoded ND4 subunit is corrected by the Saccharomyces cerevisiae -quinone oxidoreductase (NDI1) gene. J Biol Chem. 2001 Oct 19;276(42):38808-13. Epub 2001 Jul 30. In these cells the corresponding protein is localized in mitochondria, its -binding site faces the matrix compartment as in yeast mitochondria, and in perfect correlation with its abundance restores partially or fully -dependent respiration that is rotenone-insensitive, -sensitive, and antimycin A-sensitive. |
31(0,1,1,1) | Details |
| 12758076 | Marques I, Duarte M, Videira A: The 9.8 kDa subunit of complex I, related to bacterial Na (+)-translocating NADH dehydrogenases, is required for enzyme assembly and function in Neurospora crassa. J Mol Biol. 2003 May 30;329(2):283-90. Respiration of mutant mitochondria on matrix is rotenone-insensitive, confirming that the 9.8 kDa protein is required for the assembly and activity of complex I. |
6(0,0,1,1) | Details |
| 12615344 | Bandeiras TM, Salgueiro CA, Huber H, Gomes CM, Teixeira M: The respiratory chain of the thermophilic archaeon Sulfolobus metallicus: studies on the type-II NADH dehydrogenase. Biochim Biophys Acta. 2003 Mar 6;1557(1-3):13-9. The membranes of the thermoacidophilic archaeon Sulfolobus metallicus exhibit an consumption activity of 0.5 nmol O (2) min (-1) mg (-1), which is insensitive to rotenone, suggesting the presence of a type-II NADH dehydrogenase. The pure protein is a monomer with an apparent molecular mass of 49 kDa, having a high N-terminal amino acid sequence similarity towards other prokaryotic enzymes of the same type. |
1(0,0,0,1) | Details |
| 17101781 | Pan Y, Mansfield KD, Bertozzi CC, Rudenko V, Chan DA, Giaccia AJ, Simon MC: Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro. Mol Cell Biol. 2007 Feb;27(3):912-25. Epub 2006 Nov 13. Importantly, the ODD fusion protein is regulated with kinetics identical to endogenous HIF-1alpha during cellular hypoxia and reoxygenation. Furthermore, cells treated with mitochondrial inhibitors, such as rotenone and myxothiazol, provided direct evidence that PHDs remain active in hypoxic cells lacking functional mitochondria. |
1(0,0,0,1) | Details |
| 10526093 | Rutledge EM, Mongin AA, Kimelberg HK: Intracellular ATP depletion inhibits swelling-induced D-[3H] release from primary astrocyte cultures. Brain Res. 1999 Sep 18;842(1):39-45. One prominent feature of the VSOR/VSOAC is that non-hydrolyzed intracellular ATP binding to the channel or an accessory protein is required for its activation. When the cells were pretreated for 10 min with a combination of the metabolic inhibitors 2-deoxyglucose and rotenone, 100 mM K (+) media- or hypotonic media-induced D-[3H] release was completely suppressed. |
1(0,0,0,1) | Details |
| 10200266 | Au HC, Seo BB, Matsuno-Yagi A, Yagi T, Scheffler IE: The NDUFA1 gene product (MWFE protein) is essential for activity of complex I in mammalian mitochondria. Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4354-9. Complementation with hamster NDUFA1 cDNA restored the rotenone-sensitive complex I activity of these mutant cells to approximately 100% of the parent cell activity. |
1(0,0,0,1) | Details |
| 17474759 | Murai M, Ishihara A, Nishioka T, Yagi T, Miyoshi H: The ND1 subunit constructs the inhibitor binding domain in bovine heart mitochondrial complex I. Biochemistry. 2007 May 29;46(21):6409-16. Epub 2007 May 3. Immnoprecipitation of the [125I] TDA-labeled complex I with anti-bovine ND1 antibody indicated that the labeled protein is the ND1 subunit. A variety of complex I inhibitors such as piericidin A and rotenone efficiently suppressed the specific binding of [125I] TDA to ND1, indicating that they share a common binding domain. |
1(0,0,0,1) | Details |
| 10982813 | Seo BB, Wang J, Flotte TR, Yagi T, Matsuno-Yagi A: Use of the -quinone oxidoreductase (NDI1) gene of Saccharomyces cerevisiae as a possible cure for complex I defects in human cells. J Biol Chem. 2000 Dec 1;275(48):37774-8. Acta 1412, 56-65) and that the Ndi1 protein is capable of compensating respiratory deficiencies caused by defects in the host -quinone oxidoreductase (complex I). The Ndi1 enzyme of Saccharomyces cerevisiae is a single subunit rotenone-insensitive -quinone oxidoreductase that is located on the matrix side of the inner mitochondrial membrane. |
1(0,0,0,1) | Details |
| 12646413 | Xia R, Webb JA, Gnall LL, Cutler K, Abramson JJ: Skeletal muscle sarcoplasmic reticulum contains a -dependent oxidase that generates Am J Physiol Cell Physiol. 2003 Jul;285(1):C215-21. Epub 2003 Mar 19. Its activity is inhibited by diphenylene iodonium (10 microM), antimycin A (200 nM), and rotenone (40 nM) but is not coupled to the generation of or the stimulation of the ryanodine receptor. The rate of production per milligram of protein is larger in SR than in mitochondria. |
1(0,0,0,1) | Details |
| 17005863 | Malagelada C, Ryu EJ, Biswas SC, Jackson-Lewis V, Greene LA: RTP801 is elevated in Parkinson brain substantia nigral neurons and mediates death in cellular models of Parkinson's disease by a mechanism involving mammalian target of rapamycin inactivation. J Neurosci. 2006 Sep 27;26(39):9996-10005. Here, we find that RTP801 protein is also induced in this and additional cellular and animal PD models. |
1(0,0,0,1) | Details |
| 4172100 | Hoppel C, Cooper C: The action of digitonin on rat liver mitochondria. Biochem J. 1968 Apr;107(3):367-75. When it is suspended in water little protein is lost but there is a marked loss of phosphorylation. Almost all the -cytochrome c reductase (rotenone-insensitive) is lost whereas the major portions of the soluble and bound enzymes are retained. |
1(0,0,0,1) | Details |
| 16139213 | Meulener M, Whitworth AJ, Armstrong-Gold CE, Rizzu P, Heutink P, Wes PD, Pallanck LJ, Bonini NM: Drosophila DJ-1 mutants are selectively sensitive to environmental toxins associated with Parkinson's disease. Curr Biol. 2005 Sep 6;15(17):1572-7. DJ-1alpha and DJ-1beta double knockout flies are viable, fertile, and have a normal lifespan; however, they display a striking selective sensitivity to those environmental agents, including paraquat and rotenone, linked to PD in humans. These studies demonstrate that fly DJ-1 activity is selectively involved in protection from environmental oxidative insult in vivo and that the DJ-1beta protein is biochemically responsive to oxidative stress. |
1(0,0,0,1) | Details |
| 6200477 | Handlogten ME, Kilberg MS: Induction and decay of amino acid transport in the liver. J Biol Chem. 1984 Mar 25;259(6):3519-25. The decay was blocked by either actinomycin or cycloheximide, but was unaffected by leupeptin, chloroquine, dinitrophenol, rotenone, or tunicamycin. Studies with cycloheximide and actinomycin suggest the following: 1) within 30 min after initiation of cell cultures, synthesis of the corresponding mRNA for the transport-inactivating protein has begun; 2) the mRNA for transport-inactivating protein is relatively long-lived, but the inactivating protein itself has a half-life of less than 1 h; and 3) actinomycin blocks the decay through inhibition of transport-inactivating protein biosynthesis rather than by protection of the mRNA for the protein responsible for System A activity. |
1(0,0,0,1) | Details |
| 19860724 | Agnati FL, Guidolin D, Baluska F, Leo G, Barlow PW, Carone C, Genedani S: A New Hypothesis of Pathogenesis Based on the Divorce between Mitochondria and their Host Cells: Possible Relevances for the Alzheimer's Disease. Curr Alzheimer Res. 2009 Sep 28. This proposal finds indirect support from observations on rotenone-poisoned glioblastoma cells which have been co-cultured with non-poisoned cells. It has also been demonstrated by means of immunocytochemistry that, in glioblastoma cell cultures, Amyloid Precursor Protein (APP) is present in TNTs, hence it may migrate from one cell to neighbouring cells. |
1(0,0,0,1) | Details |
| 17017540 | Hoglinger GU, Oertel WH, Hirsch EC: The rotenone model of parkinsonism--the five years inspection. J Neural Transm Suppl. 2006;(70):269-72. |
0(0,0,0,0) | Details |
| 11370674 | Velazquez I, Pardo JP: Kinetic characterization of the rotenone-insensitive internal oxidoreductase of mitochondria from Saccharomyces cerevisiae. Arch Biochem Biophys. 2001 May 1;389(1):7-14. Due to the fact that S. cerevisiae cells lack complex I, the expression of this protein is essential for cell growth under respiratory conditions. |
1(0,0,0,1) | Details |
| 16565515 | Jin J, Hulette C, Wang Y, Zhang T, Pan C, Wadhwa R, Zhang J: Proteomic identification of a stress protein, mortalin/mthsp70/GRP75: relevance to Parkinson disease. Mol Cell Proteomics. 2006 Jul;5(7):1193-204. Epub 2006 Mar 24. We confirmed that one of these, mortalin (mthsp70/GRP75, a mitochondrial stress protein), is substantially decreased in PD brains as well as in a cellular model of PD. |
1(0,0,0,1) | Details |
| 6626158 | Weisbecker U, Ibbotson GE, Livesey G, Williams KE: The fate of homologous 125I-labelled immunoglobulin G within rat visceral yolk sacs incubated in vitro. Biochem J. 1983 Sep 15;214(3):815-22. When 125I-labelled rat IgG (immunoglobulin G) is incubated in vitro with visceral yolk sacs from 17.5-day-pregnant rats, the protein is readily degraded. When rotenone (10 microM) is also present in the incubation medium, the rate of digestion of IgG is inhibited to the same extent as the rate of pinocytosis of 125I-labelled polyvinylpyrrolidone. |
1(0,0,0,1) | Details |
| 10491161 | Almeida T, Duarte M, Melo AM, Videira A: The 24-kDa iron- subunit of complex I is required for enzyme activity. Eur J Biochem. 1999 Oct 1;265(1):86-93. In agreement with this, the respiration of intact mitochondria or mitochondrial membranes from the mutant strain is insensitive to rotenone inhibition. This phenotype may explain the findings that the 24-kDa iron- protein is reduced or absent in human mitochondrial diseases. |
1(0,0,0,1) | Details |
| 12556227 | Duarte M, Peters M, Schulte U, Videira A: The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria. Biochem J. 2003 May 1;371(Pt 3):1005-11. Western blot analysis of fungal mitochondria fractionated with digitonin indicated that the protein is located at the inner face of the inner membrane of the organelle (internal enzyme). The respiratory activity of mitochondria from the resulting null-mutant ndi1 is almost fully inhibited by rotenone, an inhibitor of the -pumping complex I, when matrix-generated is used as substrate. |
1(0,0,0,1) | Details |