| Name | protein is |
|---|---|
| Synonyms | ANX 2; p36; LIP 2; LIP2; ANX2; ANX2L4; ANX2P1; ANX2P2… |
| Name | acrolein |
|---|---|
| CAS | 2-propenal |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 2118418 | LeBlanc GA, Waxman DJ: Mechanisms of cyclophosphamide action on hepatic P-450 expression. Cancer Res. 1990 Sep 15;50(18):5720-6. These observations suggest that P-450j protein is induced by cyclophosphamide treatment but that the protein is inactivated by the cyclophosphamide metabolite acrolein. |
81(1,1,1,1) | Details |
| 19490921 | Sarkar P, Hayes BE: Proteomic profiling of rat lung epithelial cells induced by acrolein. . Life Sci. 2009 Jul 31;85(5-6):188-95. Epub 2009 May 30. We have further validated two differentially expressed proteins namely annexin II (ANXII) and prohibitin (PHB) in lung epithelial cells treated with acrolein. |
6(0,0,1,1) | Details |
| 8441997 | Pearson PG, Omichinski JG, McClanahan RH, Soderlund EJ, Dybing E, Nelson SD: Metabolic activation of tris (2,3-dibromopropyl) to reactive intermediates. Toxicol Appl Pharmacol. 1993 Feb;118(2):186-95. Although this reactive metabolite also appears to bind to microsomal protein, the rate of binding of radiolabeled Tris-BP to protein is 15-20x greater than binding to DNA, and some metabolites that retain the are bound. |
1(0,0,0,1) | Details |
| 19080170 | Zhang W, Xu YC, Guo FJ, Meng Y, Li ML: Anti-diabetic effects of and and their impacts on retinol-binding protein 4 expression in rats with type 2 diabetes mellitus. Chin Med J. 2008 Nov 5;121(21):2124-8. Their mechanisms involve the RBP4-GLUT4 system, during which the serum RBP4 levels are lowered and the expression of tissue GLUT4 protein is up-regulated. |
1(0,0,0,1) | Details |
| 18793453 | Brackman G, Defoirdt T, Miyamoto C, Bossier P, Van Calenbergh S, Nelis H, Coenye T: and derivatives reduce virulence in Vibrio spp. by decreasing the DNA-binding activity of the quorum sensing response regulator LuxR. BMC Microbiol. 2008 Sep 16;8:149. Study of the effect in various mutants suggested that the target protein is LuxR. |
1(0,0,0,1) | Details |
| 10320559 | Butler JA, Sjoberg M, Coen CW: Evidence for oestrogen receptor alpha-immunoreactivity in gonadotrophin-releasing hormone-expressing neurones. J Neuroendocrinol. 1999 May;11(5):331-5. Having used the cingulate cortex to demonstrate the validity of our methods for detecting hitherto unrecognized oestrogen receptor alpha (ERalpha)-immunoreactive neurones, we have now employed immunoprecipitation and double-label immunohistochemistry to investigate whether the ERalpha protein is present in gonadotrophin-releasing hormone (GnRH)-containing cells. |
1(0,0,0,1) | Details |