| Name | protein is |
|---|---|
| Synonyms | ANX 2; p36; LIP 2; LIP2; ANX2; ANX2L4; ANX2P1; ANX2P2… |
| Name | paraquat |
|---|---|
| CAS | 1,1′-dimethyl-4,4′-bipyridinium |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 18773310 | Chinta SJ, Rane A, Poksay KS, Bredesen DE, Andersen JK, Rao RV: Coupling endoplasmic reticulum stress to the cell death program in dopaminergic cells: effect of paraquat. Neuromolecular Med. 2008;10(4):333-42. Epub 2008 Sep 5. We demonstrate that paraquat triggers ER stress, cell dysfunction, and dopaminergic cell death. p23, a small co-chaperone protein, is cleaved during ER stress-induced cell death triggered by paraquat and blockage of the caspase cleavage site of p23 was associated with decreased cell death. |
81(1,1,1,1) | Details |
| 11421444 | Szigeti Z, Racz I, Lasztity D: Paraquat resistance of weeds--the case of Conyza canadensis (L.) Cronq. Z Naturforsch C. 2001 May-Jun;56(5-6):319-28. A paraquat-inducible protein is supposed to play a role in the resistance, which presumably functions by binding paraquat to an inactivating site and/or by carrying paraquat to metabolically inactive cell compartment (vacuole, cell wall). |
31(0,1,1,1) | Details |
| 15888317 | Kondo M, Yanase S, Ishii T, Hartman PS, Matsumoto K, Ishii N: The p38 signal transduction pathway participates in the oxidative stress-mediated translocation of DAF-16 to Caenorhabditis elegans nuclei. Mech Ageing Dev. 2005 Jun-Jul;126(6-7):642-7. Epub 2005 Jan 11. The DAF-16 protein is translocated to the nucleus when animals were subjected to oxidative stress in the form of paraquat. |
6(0,0,1,1) | Details |
| 11467833 | Won SH, Lee BH, Lee HS, Jo J: An Ochrobactrum anthropi gene conferring paraquat resistance to the heterologous host Escherichia coli. Biochem Biophys Res Commun. 2001 Jul 27;285(4):885-90. These results suggest that the PqrA protein is a membrane protein that plays an important role in protecting cells against paraquat toxicity. |
6(0,0,1,1) | Details |
| 18208471 | Li WY, Shao G, Lam HM: Ectopic expression of GmPAP3 alleviates oxidative damage caused by salinity and osmotic stresses. New Phytol. 2008;178(1):80-91. Epub 2008 Jan 16. Confocal and electron microscopic studies demonstrated that GmPAP3 protein is mainly localized in mitochondria, a primary site for reactive species (ROS) production. In addition, when GmPAP3 transgenic Arabidopsis thaliana seedlings were subjected to NaCl, PEG, and paraquat (PQ) treatments, the percentage of root elongation was significantly higher than the wild type. |
1(0,0,0,1) | Details |
| 15750345 | Kim DW, Eum WS, Jang SH, Kim SY, Choi HS, Choi SH, An JJ, Lee SH, Lee KS, Han K, Kang TC, Won MH, Kang JH, Kwon OS, Cho SW, Kim TY, Park J, Choi SY: Transduced Tat-SOD fusion protein protects against ischemic brain injury. . Mol Cells. 2005 Feb 28;19(1):88-96. Recently, we reported that when Tat-SOD fusion protein is transduced into pancreatic beta cells it protects the beta cells from destruction by relieving oxidative stress in ROS-implicated diabetes (Eum et al., 2004). When Tat-SOD was added to the culture medium of neuronal cells, it rapidly entered the cells and protected them against paraquat-induced cell death. |
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 |
| 17071759 | Duque E, Rodriguez-Herva JJ, de la Torre J, Dominguez-Cuevas P, Munoz-Rojas J, Ramos JL: The RpoT regulon of Pseudomonas putida DOT-T1E and its role in stress endurance against solvents. J Bacteriol. 2007 Jan;189(1):207-19. Epub 2006 Oct 27. The translated gene product of the open reading frame PP3005 is an inner membrane protein, whereas the PP3007 protein is periplasmic. The mutant strain was hypersensitive to toluene and other solvents but just as tolerant as the wild type of stress imposed by heat, antibiotics, NaCl, paraquat, H (2) O (2), and |
1(0,0,0,1) | Details |
| 12028379 | Horsburgh MJ, Wharton SJ, Cox AG, Ingham E, Peacock S, Foster SJ: MntR modulates expression of the PerR regulon and resistance in Staphylococcus aureus through control of uptake. Mol Microbiol. 2002 Jun;44(5):1269-86. Therefore, the control of Mn (II)-regulated members of the PerR regulon and the Fur protein is modulated by MntR through its control of Mn (II) uptake. |
1(0,0,0,1) | Details |
| 14977943 | Wang G, Maier RJ: An quinone reductase of Helicobacter pylori plays an important role in oxidative stress resistance and host colonization. Infect Immun. 2004 Mar;72(3):1391-6. We propose that the physiological function of the H. pylori MdaB protein is that of an quinone reductase that plays an important role in managing oxidative stress and contributes to successful colonization of the host. The mdaB mutant is also more sensitive to H (2) O (2), organic hydroperoxides, and the -generating agent paraquat. |
1(0,0,0,1) | Details |
| 19270741 | Gegg ME, Cooper JM, Schapira AH, Taanman JW: Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells. PLoS One. 2009;4(3):e4756. Epub 2009 Mar 9. This mitochondrial dysfunction resulted in increased markers of oxidative stress under basal conditions and increased cell death following treatment with the free radical generator paraquat. The PINK1 protein is a serine/threonine kinase localized in mitochondria and the cytosol. |
1(0,0,0,1) | Details |
| 15933023 | Brondsted L, Andersen MT, Parker M, Jorgensen K, Ingmer H: The HtrA protease of Campylobacter jejuni is required for heat and tolerance and for optimal interaction with human epithelial cells. Appl Environ Microbiol. 2005 Jun;71(6):3205-12. Under both conditions, the level of misfolded protein is known to increase, and we propose that the heat-sensitive phenotype of the htrA mutant is caused by an accumulation of misfolded protein in the periplasm. While lack of HtrA reduces the tolerance of C. jejuni, the htrA mutant was not sensitive to compounds that increase the formation of radicals, such as paraquat, cumene hydroperoxide, and H2O2. |
1(0,0,0,1) | Details |
| 16718483 | Lee SC, Choi HW, Hwang IS, Choi du S, Hwang BK: Functional roles of the pepper pathogen-induced bZIP transcription factor, CAbZIP1, in enhanced resistance to pathogen infection and environmental stresses. Planta. 2006 Oct;224(5):1209-25. Epub 2006 May 23. Transient expression analysis of the CAbZIP1-GFP fusion protein in Arabidopsis protoplasts revealed that the CAbZIP1 protein is localized in the nucleus. |
1(0,0,0,1) | Details |
| 15575693 | Lu C, Bentley WE, Rao G: A high-throughput approach to promoter study using green fluorescent protein. Biotechnol Prog. 2004 Nov-Dec;20(6):1634-40. Green fluorescent protein (GFP) is a reporter that has had a significant impact due to its many advantages over other reporter genes: it is autofluorescent, it enables in situ detection, it is relatively small, and it is also nontoxic. They both displayed dose-dependent induction to paraquat-generated with sodA leading acnA in strength and time. |
1(0,0,0,1) | Details |
| 12722632 | Nefedova LN, Fantin IuS, Zinchenko VV, Babykin MM: [The prqA and mvrA genes encoding carrier proteins control resistance to methyl viologen in the cyanobacterium Synechocystis sp. Genetika. 2003 Mar;39(3):336-40. It is assumed that the MvrA protein is required for efficient elimination from cells of toxic substances formed upon oxidative stress or participates in the repair of membranes destroyed by oxidants. |
1(0,0,0,1) | Details |
| 10207625 | Demple B, Hidalgo E, Ding H: Transcriptional regulation via redox-sensitive iron- centres in an oxidative stress response. Biochem Soc Symp. 1999;64:119-28. In the absence of oxidative stress, the [2Fe-2S] centres are in the reduced form and the protein is inactive, although it still binds the soxS promoter. Agents that generate in the cell (e.g. paraquat) cause rapid oxidation of the metal centres, which triggers the transcriptional activity of SoxR; removal of the oxidative stress is followed by rapid re-reduction of the [2Fe-2S] centres. |
1(0,0,0,1) | Details |
| 15946826 | Borsetti F, Tremaroli V, Michelacci F, Borghese R, Winterstein C, Daldal F, Zannoni D: Tellurite effects on Rhodobacter capsulatus cell viability and superoxide dismutase activity under oxidative stress conditions. Res Microbiol. 2005 Aug;156(7):807-13. The latter effect was also seen upon incubation with sublethal amounts of paraquat, a cytosolic generator of anions (O2-), in parallel with a strong increase in tellurite resistance (TeR). |
0(0,0,0,0) | Details |