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Chemical Compound Review

AC1NRATW     3-[[(2S)-2-[[(1R)-1- [[(1R,2R)-1-carboxy-4...

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High impact information on PEPTIDOMIMETIC INHIBITOR


Chemical compound and disease context of PEPTIDOMIMETIC INHIBITOR






Associations of PEPTIDOMIMETIC INHIBITOR with other chemical compounds



  • Instead, PS1 had a direct effect on the inhibition of Ass production by a designed peptidomimetic inhibitor: the inhibition was significantly less effective in cells expressing FAD-causing mutations in either APP or PS1 than in cells expressing the wild-type proteins [26].
  • To determine whether one enzyme plays a predominant role in Rab8 prenylation in vivo, the incorporation of [3H]mevalonate into Rab8 was measured in human embryonal kidney 293 cells under conditions where the activity of GGTaseI, but not GGTaseII, was blocked by the peptidomimetic inhibitor GGTI-298 [27].
  • CPD and CPD-N are inhibited non-competitively by zinc chelator 1,10-phenanthroline and competitively by peptidomimetic inhibitor DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid [28].
  • A macrocyclic, peptidomimetic inhibitor of peptide deformylase was designed by covalently cross-linking the P1' and P3' side chains [29].
  • A peptidomimetic inhibitor of ras functionality markedly suppresses growth of human prostate tumor xenografts in mice. Prospects for long-term clinical utility [30].

Analytical, diagnostic and therapeutic context of PEPTIDOMIMETIC INHIBITOR

  • The sequence alignment of Sap2p, Sapt1p, and Sapp1p, and homology modeling of Sapp1p with the crystal structure of Sapt1p and the complex of Sap2p with a peptidomimetic inhibitor showed that the overall folds of Sap2p, Sapt1p, and Sapp1p are similar [31].


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  2. An alpha-helical peptidomimetic inhibitor of the HIV-1 Rev-RRE interaction. Mills, N.L., Daugherty, M.D., Frankel, A.D., Guy, R.K. J. Am. Chem. Soc. (2006) [Pubmed]
  3. The crystal structure of the Epstein-Barr virus protease shows rearrangement of the processed C terminus. Buisson, M., Hernandez, J.F., Lascoux, D., Schoehn, G., Forest, E., Arlaud, G., Seigneurin, J.M., Ruigrok, R.W., Burmeister, W.P. J. Mol. Biol. (2002) [Pubmed]
  4. CGP 53437, an orally bioavailable inhibitor of human immunodeficiency virus type 1 protease with potent antiviral activity. Alteri, E., Bold, G., Cozens, R., Faessler, A., Klimkait, T., Lang, M., Lazdins, J., Poncioni, B., Roesel, J.L., Schneider, P. Antimicrob. Agents Chemother. (1993) [Pubmed]
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  6. Reversible conformational changes induced in glycoprotein IIb-IIIa by a potent and selective peptidomimetic inhibitor. Kouns, W.C., Kirchhofer, D., Hadváry, P., Edenhofer, A., Weller, T., Pfenninger, G., Baumgartner, H.R., Jennings, L.K., Steiner, B. Blood (1992) [Pubmed]
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  9. Increased myeloproliferation in glutathione S-transferase pi-deficient mice is associated with a deregulation of JNK and Janus kinase/STAT pathways. Gate, L., Majumdar, R.S., Lunk, A., Tew, K.D. J. Biol. Chem. (2004) [Pubmed]
  10. Comparison of potential markers of farnesyltransferase inhibition. Adjei, A.A., Davis, J.N., Erlichman, C., Svingen, P.A., Kaufmann, S.H. Clin. Cancer Res. (2000) [Pubmed]
  11. In vitro studies of cross-resistance mutations against two hepatitis C virus serine protease inhibitors, VX-950 and BILN 2061. Lin, C., Gates, C.A., Rao, B.G., Brennan, D.L., Fulghum, J.R., Luong, Y.P., Frantz, J.D., Lin, K., Ma, S., Wei, Y.Y., Perni, R.B., Kwong, A.D. J. Biol. Chem. (2005) [Pubmed]
  12. VX-950, a Novel Hepatitis C Virus (HCV) NS3-4A Protease Inhibitor, Exhibits Potent Antiviral Activities in HCV Replicon Cells. Lin, K., Perni, R.B., Kwong, A.D., Lin, C. Antimicrob. Agents Chemother. (2006) [Pubmed]
  13. Role of hydroxyl group and R/S configuration of isostere in binding properties of HIV-1 protease inhibitors. Petroková, H., Dusková, J., Dohnálek, J., Skálová, T., Vondrácková-Buchtelová, E., Soucek, M., Konvalinka, J., Brynda, J., Fábry, M., Sedlácek, J., Hasek, J. Eur. J. Biochem. (2004) [Pubmed]
  14. Design and synthesis of a novel peptidomimetic inhibitor of HIV-1 Tat-TAR interactions: squaryldiamide as a new potential bioisostere of unsubstituted guanidine. Lee, C.W., Cao, H., Ichiyama, K., Rana, T.M. Bioorg. Med. Chem. Lett. (2005) [Pubmed]
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  16. Design and synthesis of novel imidazole-substituted dipeptide amides as potent and selective inhibitors of Candida albicans myristoylCoA:protein N-myristoyltransferase and identification of related tripeptide inhibitors with mechanism-based antifungal activity. Devadas, B., Freeman, S.K., Zupec, M.E., Lu, H.F., Nagarajan, S.R., Kishore, N.S., Lodge, J.K., Kuneman, D.W., McWherter, C.A., Vinjamoori, D.V., Getman, D.P., Gordon, J.I., Sikorski, J.A. J. Med. Chem. (1997) [Pubmed]
  17. Overexpression of the HIV-1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles. Karacostas, V., Wolffe, E.J., Nagashima, K., Gonda, M.A., Moss, B. Virology (1993) [Pubmed]
  18. Characterization of recombinant human renin: kinetics, pH-stability, and peptidomimetic inhibitor binding. Holzman, T.F., Chung, C.C., Edalji, R., Egan, D.A., Martin, M., Gubbins, E.J., Krafft, G.A., Wang, G.T., Thomas, A.M., Rosenberg, S.H. J. Protein Chem. (1991) [Pubmed]
  19. Regulation of interferon regulatory factor-3 by the hepatitis C virus serine protease. Foy, E., Li, K., Wang, C., Sumpter, R., Ikeda, M., Lemon, S.M., Gale, M. Science (2003) [Pubmed]
  20. Pharmacologic or genetic manipulation of glutathione S-transferase P1-1 (GSTpi) influences cell proliferation pathways. Ruscoe, J.E., Rosario, L.A., Wang, T., Gaté, L., Arifoglu, P., Wolf, C.R., Henderson, C.J., Ronai, Z., Tew, K.D. J. Pharmacol. Exp. Ther. (2001) [Pubmed]
  21. Targeting neutrophil collagenase/matrix metalloproteinase-8 and gelatinase B/matrix metalloproteinase-9 with a peptidomimetic inhibitor protects against endotoxin shock. Hu, J., Van den Steen, P.E., Dillen, C., Opdenakker, G. Biochem. Pharmacol. (2005) [Pubmed]
  22. Non-nucleoside inhibitors of the HCV polymerase. Sarisky, R.T. J. Antimicrob. Chemother. (2004) [Pubmed]
  23. Simultaneous monitoring of argatroban and its major metabolite using an HPLC method: potential clinical applications. Ahmad, S., Ahsan, A., George, M., Iqbal, O., Jeske, W.P., McKenna, R., Lewis, B.E., Walenga, J.M., Fareed, J. Clin. Appl. Thromb. Hemost. (1999) [Pubmed]
  24. Clinical laboratory monitoring of a synthetic antithrombin agent, argatroban, using high performance liquid chromatography and functional methods. Ahmad, S., Iqbal, O., Ahsan, A., Hoppensteadt, D.A., Lewis, B.E., Walenga, J.M., Fareed, J. International angiology : a journal of the International Union of Angiology. (1999) [Pubmed]
  25. Phosphoinositide, phosphopeptide and pyridone interactions of the Abl SH2 domain. Tokonzaba, E., Capelluto, D.G., Kutateladze, T.G., Overduin, M. Chemical biology & drug design. (2006) [Pubmed]
  26. FAD mutations in presenilin-1 or amyloid precursor protein decrease the efficacy of a gamma-secretase inhibitor: evidence for direct involvement of PS1 in the gamma-secretase cleavage complex. Xia, W., Ostaszewski, B.L., Kimberly, W.T., Rahmati, T., Moore, C.L., Wolfe, M.S., Selkoe, D.J. Neurobiol. Dis. (2000) [Pubmed]
  27. Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases. Wilson, A.L., Erdman, R.A., Castellano, F., Maltese, W.A. Biochem. J. (1998) [Pubmed]
  28. Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells. O'Malley, P.G., Sangster, S.M., Abdelmagid, S.A., Bearne, S.L., Too, C.K. Biochem. J. (2005) [Pubmed]
  29. Structure-based design of a macrocyclic inhibitor for peptide deformylase. Hu, X., Nguyen, K.T., Verlinde, C.L., Hol, W.G., Pei, D. J. Med. Chem. (2003) [Pubmed]
  30. A peptidomimetic inhibitor of ras functionality markedly suppresses growth of human prostate tumor xenografts in mice. Prospects for long-term clinical utility. Sirotnak, F.M., Sepp-Lorenzino, L., Kohl, N.E., Rosen, N., Scher, H.I. Cancer Chemother. Pharmacol. (2000) [Pubmed]
  31. Structure-based specificity mapping of secreted aspartic proteases of Candida parapsilosis, Candida albicans, and Candida tropicalis using peptidomimetic inhibitors and homology modeling. Majer, F., Pavlícková, L., Majer, P., Hradilek, M., Dolejsí, E., Hrusková-Heidingsfeldová, O., Pichová, I. Biol. Chem. (2006) [Pubmed]
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