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Chemical Compound Review

CHEMBL120178     5-[5-[[(2S)-1-carboxy-3-oxo- propan-2...

Synonyms: AC1NS24U, sulfonamide analog 1
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Disease relevance of Inhibitor 2


High impact information on Inhibitor 2


Chemical compound and disease context of Inhibitor 2


Biological context of Inhibitor 2

  • In particular, we were looking for (1) altered gene expression in the transformed cells that reverts to normal following exposure to a selective cyclooxygenase-2 inhibitor, (2) novel genes, and (3) genes encoding membrane receptors or ligands [15].
  • In 'prophase extracts', spontaneous activation of the cdc2 kinase is inhibited by beta-glycerophosphate and NaF, but not by okadaic acid, inhibitor 1 and inhibitor 2 or divalent cation chelation [16].
  • Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding [17].
  • We also calculated the effect of mutations on the folding kinetics of chymotrypsin inhibitor 2, the most intensively studied two-state protein, with some success [18].
  • The major S6 phosphatase in cell extracts was identified as a type 1 enzyme by its chromatographic properties, its sensitivity to inhibitor 2, and its substrate specificity [19].

Anatomical context of Inhibitor 2


Associations of Inhibitor 2 with other chemical compounds


Gene context of Inhibitor 2


Analytical, diagnostic and therapeutic context of Inhibitor 2


  1. Phorbol ester induces the biosynthesis of glycosylated and nonglycosylated plasminogen activator inhibitor 2 in high excess over urokinase-type plasminogen activator in human U-937 lymphoma cells. Genton, C., Kruithof, E.K., Schleuning, W.D. J. Cell Biol. (1987) [Pubmed]
  2. Primary myxedema with thyrotrophin-binding inhibitor immunoglobulins. Clinical and laboratory findings in 15 patients. Konishi, J., Iida, Y., Kasagi, K., Misaki, T., Nakashima, T., Endo, K., Mori, T., Shinpo, S., Nohara, Y., Matsuura, N. Ann. Intern. Med. (1985) [Pubmed]
  3. Overexpression of plasminogen activator inhibitor 2 in human melanoma cells inhibits spontaneous metastasis in scid/scid mice. Mueller, B.M., Yu, Y.B., Laug, W.E. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  4. Inhibition of retinoblastoma protein degradation by interaction with the serpin plasminogen activator inhibitor 2 via a novel consensus motif. Darnell, G.A., Antalis, T.M., Johnstone, R.W., Stringer, B.W., Ogbourne, S.M., Harrich, D., Suhrbier, A. Mol. Cell. Biol. (2003) [Pubmed]
  5. Mutations of the CDKN2/p16INK4 gene in Australian melanoma kindreds. Walker, G.J., Hussussian, C.J., Flores, J.F., Glendening, J.M., Haluska, F.G., Dracopoli, N.C., Hayward, N.K., Fountain, J.W. Hum. Mol. Genet. (1995) [Pubmed]
  6. The structure and regulation of protein phosphatases. Cohen, P. Annu. Rev. Biochem. (1989) [Pubmed]
  7. Cell cycle oscillation of phosphatase inhibitor-2 in rat fibroblasts coincident with p34cdc2 restriction. Brautigan, D.L., Sunwoo, J., Labbé, J.C., Fernandez, A., Lamb, N.J. Nature (1990) [Pubmed]
  8. Targets for dioxin: genes for plasminogen activator inhibitor-2 and interleukin-1 beta. Sutter, T.R., Guzman, K., Dold, K.M., Greenlee, W.F. Science (1991) [Pubmed]
  9. NF-kappaB translocation prevents host cell death after low-dose challenge by Legionella pneumophila. Losick, V.P., Isberg, R.R. J. Exp. Med. (2006) [Pubmed]
  10. Calcineurin does not mediate exercise-induced increase in muscle GLUT4. Garcia-Roves, P.M., Jones, T.E., Otani, K., Han, D.H., Holloszy, J.O. Diabetes (2005) [Pubmed]
  11. Normal cholesterol absorption in rats deficient in intestinal acyl coenzyme A:cholesterol acyltransferase activity. Gallo, L.L., Wadsworth, J.A., Vahouny, G.V. J. Lipid Res. (1987) [Pubmed]
  12. The protein phosphatases involved in cellular regulation. Primary structure of inhibitor-2 from rabbit skeletal muscle. Holmes, C.F., Campbell, D.G., Caudwell, F.B., Aitken, A., Cohen, P. Eur. J. Biochem. (1986) [Pubmed]
  13. Nucleotide variations in genes encoding plasminogen activator inhibitor-2 and serine proteinase inhibitor B10 associated with prostate cancer. Shioji, G., Ezura, Y., Nakajima, T., Ohgaki, K., Fujiwara, H., Kubota, Y., Ichikawa, T., Inoue, K., Shuin, T., Habuchi, T., Ogawa, O., Nishimura, T., Emi, M. J. Hum. Genet. (2005) [Pubmed]
  14. Design and synthesis of novel HIV-1 protease inhibitors incorporating oxyindoles as the P2'-ligands. Ghosh, A.K., Schiltz, G., Perali, R.S., Leshchenko, S., Kay, S., Walters, D.E., Koh, Y., Maeda, K., Mitsuya, H. Bioorg. Med. Chem. Lett. (2006) [Pubmed]
  15. CD24 is a new oncogene, early at the multistep process of colorectal cancer carcinogenesis. Sagiv, E., Memeo, L., Karin, A., Kazanov, D., Jacob-Hirsch, J., Mansukhani, M., Rechavi, G., Hibshoosh, H., Arber, N. Gastroenterology (2006) [Pubmed]
  16. Cdc2 H1 kinase is negatively regulated by a type 2A phosphatase in the Xenopus early embryonic cell cycle: evidence from the effects of okadaic acid. Félix, M.A., Cohen, P., Karsenti, E. EMBO J. (1990) [Pubmed]
  17. Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Otzen, D.E., Itzhaki, L.S., elMasry, N.F., Jackson, S.E., Fersht, A.R. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  18. A simple model for calculating the kinetics of protein folding from three-dimensional structures. Muñoz, V., Eaton, W.A. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  19. Differential regulation of S6 phosphorylation by insulin and epidermal growth factor in Swiss mouse 3T3 cells: insulin activation of type 1 phosphatase. Olivier, A.R., Ballou, L.M., Thomas, G. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  20. Effects of skeletal muscle protein phosphatase inhibitor-2 on protein synthesis and protein phosphorylation in rabbit reticulocyte lysates. Ernst, V., Levin, D.H., Foulkes, J.G., London, I.M. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  21. Sequence and molecular characterization of human monocyte/neutrophil elastase inhibitor. Remold-O'Donnell, E., Chin, J., Alberts, M. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  22. FDP D-dimer induces the secretion of interleukin-1, urokinase-type plasminogen activator, and plasminogen activator inhibitor-2 in a human promonocytic leukemia cell line. Hamaguchi, M., Morishita, Y., Takahashi, I., Ogura, M., Takamatsu, J., Saito, H. Blood (1991) [Pubmed]
  23. Dioxin-responsive genes: examination of dose-response relationships using quantitative reverse transcriptase-polymerase chain reaction. Vanden Heuvel, J.P., Clark, G.C., Kohn, M.C., Tritscher, A.M., Greenlee, W.F., Lucier, G.W., Bell, D.A. Cancer Res. (1994) [Pubmed]
  24. Helicobacter pylori induces plasminogen activator inhibitor 2 in gastric epithelial cells through nuclear factor-kappaB and RhoA: implications for invasion and apoptosis. Varro, A., Noble, P.J., Pritchard, D.M., Kennedy, S., Hart, C.A., Dimaline, R., Dockray, G.J. Cancer Res. (2004) [Pubmed]
  25. Gleevec inhibits beta-amyloid production but not Notch cleavage. Netzer, W.J., Dou, F., Cai, D., Veach, D., Jean, S., Li, Y., Bornmann, W.G., Clarkson, B., Xu, H., Greengard, P. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  26. The exon 3 encoded sequence of the intracellular serine proteinase inhibitor plasminogen activator inhibitor 2 is a protein binding domain. Jensen, P.H., Jensen, T.G., Laug, W.E., Hager, H., Gliemann, J., Pepinsky, B. J. Biol. Chem. (1996) [Pubmed]
  27. Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in vivo. Tan, Y.S., Morcos, P.A., Cannon, J.F. J. Biol. Chem. (2003) [Pubmed]
  28. Interaction of the 56,000-dalton phosphoprotein phosphatase from reticulocytes with regulin and inhibitor 2. Tipper, J., Wollny, E., Fullilove, S., Kramer, G., Hardesty, B. J. Biol. Chem. (1986) [Pubmed]
  29. S100A11, S100A10, annexin I, desmosomal proteins, small proline-rich proteins, plasminogen activator inhibitor-2, and involucrin are components of the cornified envelope of cultured human epidermal keratinocytes. Robinson, N.A., Lapic, S., Welter, J.F., Eckert, R.L. J. Biol. Chem. (1997) [Pubmed]
  30. Regulation of chromosome segregation by Glc8p, a structural homolog of mammalian inhibitor 2 that functions as both an activator and an inhibitor of yeast protein phosphatase 1. Tung, H.Y., Wang, W., Chan, C.S. Mol. Cell. Biol. (1995) [Pubmed]
  31. Interleukin-4 suppresses plasminogen activator inhibitor-2 formation in stimulated human monocytes. Hamilton, J.A., Whitty, G.A., Last, K., Royston, A.K., Hart, P.H., Burgess, D.R. Blood (1992) [Pubmed]
  32. Loss of expression of the p16/cyclin-dependent kinase inhibitor 2 tumor suppressor gene in melanocytic lesions correlates with invasive stage of tumor progression. Reed, J.A., Loganzo, F., Shea, C.R., Walker, G.J., Flores, J.F., Glendening, J.M., Bogdany, J.K., Shiel, M.J., Haluska, F.G., Fountain, J.W. Cancer Res. (1995) [Pubmed]
  33. Structural basis for potent slow binding inhibition of human matrix metalloproteinase-2 (MMP-2). Rosenblum, G., Meroueh, S.O., Kleifeld, O., Brown, S., Singson, S.P., Fridman, R., Mobashery, S., Sagi, I. J. Biol. Chem. (2003) [Pubmed]
  34. Saccharomyces cerevisiae homologs of mammalian B and B' subunits of protein phosphatase 2A direct the enzyme to distinct cellular functions. Zhao, Y., Boguslawski, G., Zitomer, R.S., DePaoli-Roach, A.A. J. Biol. Chem. (1997) [Pubmed]
  35. Phosphoprotein inhibitor CPI-17 specificity depends on allosteric regulation of protein phosphatase-1 by regulatory subunits. Eto, M., Kitazawa, T., Brautigan, D.L. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  36. Characterization of deletion mutants of the catalytic subunit of protein phosphatase-1. Zhang, Z., Zhao, S., Bai, G., Lee, E.Y. J. Biol. Chem. (1994) [Pubmed]
  37. Phosphorylase phosphatase regulatory subunit. "Western" blotting with immunoglobulins against inhibitor-2 reveals a protein of Mr = 60,000. Gruppuso, P.A., Johnson, G.L., Constantinides, M., Brautigan, D.L. J. Biol. Chem. (1985) [Pubmed]
  38. Phosphorylase phosphatase catalytic subunit. Evidence that the Mr = 33,000 enzyme fragment is derived from a native protein of Mr = 70,000. Brautigan, D.L., Shriner, C.L., Gruppuso, P.A. J. Biol. Chem. (1985) [Pubmed]
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