| Name | glyceraldehyde 3 phosphate dehydrogenase |
|---|---|
| Synonyms | CDABP0047; G3PD; GAPD; GAPD protein; GAPDH; Glyceraldehyde 3 phosphate dehydrogenase; GAPD proteins; Glyceraldehyde 3 phosphate dehydrogenases |
| Name | paraquat |
|---|---|
| CAS | 1,1′-dimethyl-4,4′-bipyridinium |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 10585871 | Mitsumoto A, Kim KR, Oshima G, Kunimoto M, Okawa K, Iwamatsu A, Nakagawa Y: Glyoxalase I is a novel -responsive protein. Biochem J. 1999 Dec 15;344 Pt 3:837-44. Glox I was selectively inactivated by NO; compounds that induce oxidative stress (H (2) O (2), paraquat and arsenite) failed to inhibit this enzyme. |
0(0,0,0,0) | Details |
| 17913294 | Bustos DM, Bustamante CA, Iglesias AA: Involvement of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in response to oxidative stress. J Plant Physiol. 2008 Mar 13;165(4):456-61. Epub 2007 Oct 25. |
3(0,0,0,3) | Details |
| 10366417 | Ejima K, Nanri H, Araki M, Uchida K, Kashimura M, Ikeda M: 17beta- induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress. Eur J Endocrinol. 1999 Jun;140(6):608-13. METHODS: The regenerative effects of the protein thiol/disulfide oxidoreductases, PDI, Trx and Grx, on oxidatively damaged proteins were assayed using H2O2-inactivated glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a reporter enzyme. Other sex hormones such as and did not affect the contents of these oxidoreductases in BAECs. (HNE)-protein adducts, which are generated by lipid peroxidation, were accumulated in BAECs exposed to paraquat, whereas the pretreatment of BAECs with 17beta- suppressed their accumulation. |
2(0,0,0,2) | Details |
| 17055214 | Takizawa M, Komori K, Tampo Y, Yonaha M: Paraquat-induced oxidative stress and dysfunction of cellular redox systems including antioxidative defense enzymes peroxidase and thioredoxin reductase. Toxicol In Vitro. 2007 Apr;21(3):355-63. Epub 2006 Sep 14. Taken together, the results suggest that the reduced regenerative ability of oxidatively damaged proteins including GAPDH due to the inactivation of thioredoxin reductase and peroxidase by paraquat may contribute to increasing oxidative stress, leading to cell death. |
89(1,1,2,4) | Details |
| 11814328 | Tsukamoto M, Tampo Y, Sawada M, Yonaha M: Paraquat-induced oxidative stress and dysfunction of the redox cycle in pulmonary microvascular endothelial cells. Toxicol Appl Pharmacol. 2002 Jan 15;178(2):82-92. Viability loss was accompanied by increased -protein mixed disulfide formation, as well as a loss in glyceraldehyde-3-phosphate dehydrogenase activity, indicating a low defense potential. |
1(0,0,0,1) | Details |
| 11245791 | Mano J, Ohno C, Domae Y, Asada K: Chloroplastic peroxidase is the primary target of methylviologen-induced photooxidative stress in spinach leaves: its relevance to monodehydroascorbate radical detected with in vivo ESR. Biochim Biophys Acta. 2001 Apr 2;1504(2-3):275-87. Following APX, superoxide dismutase and (+)-glyceraldehyde 3-phosphate dehydrogenase, both of which are vulnerable to H2O2, were inactivated by MV plus light. |
1(0,0,0,1) | Details |
| 12691523 | Prieto-Alamo MJ, Cabrera-Luque JM, Pueyo C: Absolute quantitation of normal and ROS-induced patterns of gene expression: an in vivo real-time PCR study in mice. Gene Expr. 2003;11(1):23-34. By absolute real-time PCR we demonstrate that the transcript amounts of two of the most popular internall controls (coding GAPDH and beta-actin) fluctuate dramatically across diverse mouse or human tissues. Quantitations reported: i) determine mouse-to-mouse variability in basal gene expression, ii) establish organ- and embryo-associated differences in mouse, iii) compare mouse and human tissue-specific profiles, iv) examine the time course (30-240 min) expression in liver and lung of mice treated with paraquat generator) at 30 mg kg (-1) (one half LD50 value), and v) explore the utility of absolute real-time PCR in field studies with genetically diverse mice. |
1(0,0,0,1) | Details |
| 10036768 | Yoo HY, Kim SS, Rho HM: Overexpression and simple purification of human superoxide dismutase (SOD1) in yeast and its resistance to oxidative stress. J Biotechnol. 1999 Feb 5;68(1):29-35. The structural gene of human Cu/Zn superoxide dismutase (hSOD1) was cloned into a yeast expression vector containing the promoter of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gene. The yeast overexpressing hSOD1 appeared to be more resistant to oxidative stresses such as paraquat, and heat shock. |
1(0,0,0,1) | Details |