Academic literature on the topic 'Cysteine proteinases – Inhibitors – Synthesis'

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Journal articles on the topic "Cysteine proteinases – Inhibitors – Synthesis"

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Rauber, P., B. Walker, S. Stone, and E. Shaw. "Synthesis of lysine-containing sulphonium salts and their properties as proteinase inhibitors." Biochemical Journal 250, no. 3 (1988): 871–76. http://dx.doi.org/10.1042/bj2500871.

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Some sulphonium salts derived from lysine were synthesized with the general structure R-Lys-CH2S+-(alkyl)2. They were examined as inhibitors of the cysteine proteinase clostripain, which has a preference for cleaving peptide bonds at the carboxy group of basic amino acids, and of a number of trypsin-related serine proteinases. Clostripain was irreversibly inactivated by all reagents examined, but in the case of the serine proteinases, depending on the reagent structure, irreversible and reversible inhibitions were observed. These were kinetically characterized.
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Zumbrunn, A., S. Stone, and E. Shaw. "The synthesis and properties of peptidylmethylsulphonium salts with two cationic residues as potential inhibitors of prohormone processing." Biochemical Journal 256, no. 3 (1988): 989–94. http://dx.doi.org/10.1042/bj2560989.

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Peptidylmethylsulphonium salts incorporating consecutive basic residues at the C-terminus of the peptidyl portion such as -Arg-Arg-, -Arg-Lys-, -Lys-Lys- and -Lys-Arg- were synthesized and examined as proteinase inhibitors. Serine proteinases with a specificity directed towards hydrolysis at cationic residues were found to be unaffected by these derivatives. On the other hand, cysteine proteinases, cathepsin B and, in particular, clostripain were readily inactivated by affinity labelling. The reagents thus are of promise for the study of prohormone processing promoted by cysteine proteinases.
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Gamboa de Dominguez, ND, and PJ Rosenthal. "Cysteine proteinase inhibitors block early steps in hemoglobin degradation by cultured malaria parasites." Blood 87, no. 10 (1996): 4448–54. http://dx.doi.org/10.1182/blood.v87.10.4448.bloodjournal87104448.

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Erythrocytic malaria parasites degrade hemoglobin as a source of amino acids for parasite protein synthesis. Cysteine proteinase inhibitors have been shown to block the hydrolysis of globin by cultured parasites, indicating that a malarial cysteine proteinase is required for this process. In the present study, we have evaluated the role of parasite proteinases in earlier steps of hemoglobin degradation, namely the disassociation of the hemoglobin tetramer and the separation of heme from globin. Hemoglobin did not spontaneously denature or release heme under the pH and reducing conditions of th
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Rauber, P., H. Angliker, B. Walker, and E. Shaw. "The synthesis of peptidylfluoromethanes and their properties as inhibitors of serine proteinases and cysteine proteinases." Biochemical Journal 239, no. 3 (1986): 633–40. http://dx.doi.org/10.1042/bj2390633.

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A synthesis of peptidylfluoromethanes is described that utilizes the conversion of phthaloyl amino acids into their fluoromethane derivatives. These can be deblocked and elongated. The inactivation of chymotrypsin by Cbz-Phe-CH2F (benzyloxycarbonylphenylalanylfluoromethane) was found to be considerably slower than that of the analogous chloromethane. The fluoromethane analogue inactivates chymotrypsin with an overall rate constant that is 2% of that observed for the inactivation of the enzyme with the chloromethane. However, the result is the same. The reagent complexes in a substrate-like man
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Angliker, H., P. Wikström, P. Rauber, S. Stone, and E. Shaw. "Synthesis and properties of peptidyl derivatives of arginylfluoromethanes." Biochemical Journal 256, no. 2 (1988): 481–86. http://dx.doi.org/10.1042/bj2560481.

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Two peptide derivatives of arginylfluoromethane (Arg-CH2F), namely Bz(benzoyl)-Phe-ArgCH2F and D-Phe-Pro-Arg-CH2F, have been synthesized by extension of available methods, i.e. the Dakin-West reaction [Rasnick (1985) Anal. Biochem. 149, 461-465] or synthesis of a phthaloyl-blocked C-terminal fluoromethane [Rauber, Angliker, Walker & Shaw (1986) Biochem. J. 239, 633-640; Angliker, Wikström, Rauber & Shaw (1987) Biochem. J. 241, 871-875] with subsequent elongation. The guanidino group of arginine was protected as the bis-Cbz (benzyloxycarbonyl) derivative. The products were examined as a
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Ando, R. "Cyclopropenone-containing cysteine proteinase inhibitors. Synthesis and enzyme inhibitory activities." Bioorganic & Medicinal Chemistry 7, no. 4 (1999): 571–79. http://dx.doi.org/10.1016/s0968-0896(99)00007-3.

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Saitoh, Eiichi, and Satoko Isemura. "Molecular Biology of Human Salivary Cysteine Proteinase Inhibitors." Critical Reviews in Oral Biology & Medicine 4, no. 3 (1993): 487–93. http://dx.doi.org/10.1177/10454411930040033301.

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The synthesis of human cystatins of family II is controlled by a multigene family having at least 7 members that are localized on chromosome 20, the cystatin gene family. Proteolytic degradation and phosphorylation of the gene products give rise to heterogeneity and multiplicity of cystatins in human saliva. These cysteine proteinase inhibitors, as well as other members of the cystatin superfamily, are evolutionally and functionally related to Bowman-Birk type serine proteinase inhibitors.
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Zumbrunn, A., S. Stone, and E. Shaw. "Synthesis and properties of Cbz-Phe-Arg-CHN2 (benzyloxycarbonylphenylalanylarginyldiazomethane) as a proteinase inhibitor." Biochemical Journal 250, no. 2 (1988): 621–23. http://dx.doi.org/10.1042/bj2500621.

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The preparation of peptides terminating in -Arg-CHN2 has been attempted because of their potential value as proteinase inactivators. We have succeeded in one case, converting Cbz-Phe-ArgOH to the diazomethane without blocking the guanidino group. As expected from previous results with such reagents, the new derivative was extremely effective in inactivating a cysteine proteinase specific for cleaving at arginyl bonds, that is, clostripain. However, in contrast with the inertness of serine proteinases to reagents of this type in the cases examined previously, plasma kallikrein was inactivated b
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Walker, B., B. M. Cullen, G. Kay, I. M. Halliday, A. McGinty, and J. Nelson. "The synthesis, kinetic characterization and application of a novel biotinylated affinity label for cathepsin B." Biochemical Journal 283, no. 2 (1992): 449–53. http://dx.doi.org/10.1042/bj2830449.

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In this study we report on the synthesis, kinetic characterization and application of a novel biotinylated and active-site-directed inactivator of cathepsin B. Thus the peptidyldiazomethane biotinyl-Phe-Ala-diazomethane has been synthesized by a combination of solid-phase and solution methodologies and has been shown to be a very efficient inactivator of bovine and human cathepsin B. The respective apparent second-order rate constants (k0bs./[I]) for the inactivation of the human and bovine enzymes by this reagent, namely approximately 5.4 x 10(4) M-1.min-1 and approximately 7.8 x 10(4) M-1.mi
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Ling, H., S. Vamvakas, G. Busch, et al. "Suppressing role of transforming growth factor-beta 1 on cathepsin activity in cultured kidney tubule cells." American Journal of Physiology-Renal Physiology 269, no. 6 (1995): F911—F917. http://dx.doi.org/10.1152/ajprenal.1995.269.6.f911.

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Elevated expression and activity of transforming growth factor-beta 1 (TGF-beta 1) have been indicated in various renal diseases, implicating the potential involvement of this growth factor in the accumulation of extracellular matrix. To assess its potential role on protein turnover in tubule cells, we investigated in LLC-PK1 cells the effects of TGF-beta 1 on the activities of lysosomal cysteine proteinases cathepsins B, H, and L + B, which play a major role in the degradation of both cellular protein and extracellular matrix. The results show that 1-10 ng/ml TGF-beta 1 exerted inhibitory eff
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Dissertations / Theses on the topic "Cysteine proteinases – Inhibitors – Synthesis"

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Bridges, Sylvia Shadinger. "Design, synthesis, and evaluation of cysteine protease inhibitors." Diss., Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/29738.

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Proteases are enzymes that cleave protein amide bonds. Proteases are involved in a myriad of biological processes and are considered good targets for drug design. The proteases described herein are cysteine proteases, which utilize a cysteine residue thiol to attack the amide carbonyl, leading to amide bond cleavage. Irreversible inhibitors of cysteine proteases react with the active site cysteine, forming a covalent bond and rendering the enzyme inactive. The first project involved the design and synthesis of aza-peptide epoxide inhibitors for calpain, a clan CA, ubiquitous, calcium-activa
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Tehrani, Kamin A. "Synthesis and kinetics of cysteine proteinase inhibitors." Thesis, Georgia Institute of Technology, 1991. http://hdl.handle.net/1853/26967.

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Rukamp, Karrie Eileen Adlington. "Design and synthesis of inhibitors for serine and cysteine proteases." Diss., Available online, Georgia Institute of Technology, 2004:, 2003. http://etd.gatech.edu/theses/available/etd-04082004-180343/unrestricted/rukamp%5Fkarrie%5Fe%5Fa%5F200312%5Fphd.pdf.

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Rukamp, Brian John. "Design, synthesis, and evaluation of novel thiobenzyl ester substrates and aza-peptide inhibitors for serine and cysteine proteases." Diss., Available online, Georgia Institute of Technology, 2004:, 2003. http://etd.gatech.edu/theses/available/etd-04072004-180202/unrestricted/rukamp%5Fbrian%5Fj%5F200312%5Fphd.pdf.

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Millar, Tarek Lawson. "Synthesis and evaluation of CA clan cysteine inhibitors." Thesis, University of Canterbury. Chemistry, 2008. http://hdl.handle.net/10092/1911.

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This investigation involved the synthesis of potential CA clan cysteine inhibitors of m-calpain and cathepsin B. Inhibitors 2.1.3a-j were based on the SJA-6017 construct containing the N-(4-fluorobenzenesulfonyl) moiety at the P₃ address region. The inhibitor 2.1.3k was based on CAT-0059 a novel dipeptide dialdehyde inhibitor containing the 5-formyl pyrrole moiety at the P₃ address region. Chapter 1 introduces proteases in particular m-calpain and cathepsin B implicated in human pathologies cataract and tumour metastasis respectably. Structure, disease processes and known inhibitors for m-calp
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Ovat, Asli. "Design, synthesis and evaluation of cysteine protease inhibitors." Diss., Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/33822.

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Cysteine proteases are important drug targets due to their involvement in many biological processes such as protein turnover, digestion, blood coagulation, apoptosis, cell differentiation, cell signaling, and the immune response. In this thesis, we have reported the design, synthesis and evaluation of clan CA and clan CD cysteine protease inhibitors. Aza-peptidyl Michael acceptor and epoxide inhibitors for asparaginyl endopeptidases (legumains) from the bloodfluke, Schistosoma mansoni (SmAE) and the hard tick, Ixodes ricinus (IrAE) were designed and synthesized. SARs were similar, but with s
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McGinty, Ann Marie. "The design, synthesis and application of novel inhibitors of cysteine proteinases." Thesis, Queen's University Belfast, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.482053.

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Krauser, Joel Anderson. "Design, synthesis and evaluation of novel inhibitors and fluorogenic substrates for cysteine proteases and metallo proteases." Diss., Georgia Institute of Technology, 2001. http://hdl.handle.net/1853/30003.

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Campbell, Amy. "Design, synthesis, and evaluation of cysteine protease inhibitors." Diss., Available online, Georgia Institute of Technology, 2005, 2005. http://etd.gatech.edu/theses/available/etd-11222005-132114/.

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Thesis (Ph. D.)--Chemistry and Biochemistry, Georgia Institute of Technology, 2006.<br>Murthy, Niren, Committee Member ; Doyle, Donald, Committee Member ; Fahrni, Christoph, Committee Member ; May, Sheldon, Committee Member ; Powers, James, Committee Chair.
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Gheura, Iuliana L. "Design, synthesis and evaluation of AZA-peptide epoxides as inhibitors of cysteine proteases." Diss., Georgia Institute of Technology, 2002. http://hdl.handle.net/1853/30571.

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Books on the topic "Cysteine proteinases – Inhibitors – Synthesis"

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Turk, Vito, ed. Cysteine Proteinases and their Inhibitors. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836.

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Cystatins: Protease inhibitors, biomarkers, and immunomodulators. Nova Science, 2011.

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Turk, Boris. Papain-like cysteine proteinases: Regulation by proteinase inhibitors and pH. SverigesLantbruksuniversitet, 1996.

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Akpinar, Ozlem. Characterization of recombinant proteinase inhibitors in surimi application. 1998.

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Philippe, Taupin, ed. The cystatin superfamily of proteinase inhibitors. Nova Science Publishers, 2007.

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6

Turk, Vito. Cysteine Proteinases and their Inhibitors: Proceedings of the International Symposium Portoroz, Yugoslavia, September 15-18 1985. De Gruyter, Inc., 2019.

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Vito, Turk, and International Symposium on Cysteine Proteinases and Their Inhibitors (1st : 1985 : Portorož, Slovenia), eds. Cysteine proteinases and their inhibitors: Proceedings of the international symposium, Portorož, Yugoslavia, September 15-18, 1985. De Gruyter, 1986.

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(Editor), Michael F. Shaughnessy, Marcel V. e. Vennemann (Editor), and Cynthia Kleyn Kennedy (Editor), eds. Meta-Cognition: A Recent Review of Research, Theory, and Perspectives. Nova Science Publishers Inc, 2008.

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F, Shaughnessy Michael, Veenman Marcel, and Kennedy Cynthia Kleyn, eds. Meta-cognition: A recent review of research, theory, and perspectives. Nova Science Publishers, Inc., 2007.

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F, Shaughnessy Michael, Veenman Marcel, and Kennedy Cynthia Kleyn, eds. Meta-cognition: A recent review of research, theory, and perspectives. Nova Science Publishers, Inc., 2008.

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Book chapters on the topic "Cysteine proteinases – Inhibitors – Synthesis"

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Pohl, J., S. Davinič, I. Bláha, P. Štrop, and V. Kostka. "A study of the peptidyldipeptidase activity of bovine spleen cathepsin B using synthetic substrates." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-012.

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Délaissé, J. M., P. Ledent, Y. Eeckhout, and G. Vaes. "Cysteine proteinases and bone resorption." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-029.

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Sasaki, M., I. Ohkubo, C. Namikawa, et al. "Kininogens as thiol proteinase inhibitors." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-038.

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Sloane, B. F., T. T. Lah, N. A. Day, J. Rozhin, Y. Bando, and K. V. Honn. "Tumor cysteine proteinases and their inhibitors." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-068.

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Korant, B., T. Towatari, L. Ivanoff, C. Kettner, A. Cordova, and S. Petteway. "Viruses as vectors for cysteine proteases." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-032.

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Denteš, J., and Lj Vitale. "Cysteine proteinase inhibitors from fish liver." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-057.

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Lenarčič, B., M. Kokalj, and V. Turk. "Cysteine proteinase inhibitors from sea anemone." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-058.

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Barrett, A. J., H. Fritz, W. Müller-Esterl, et al. "NOMENCLATURE AND CLASSIFICATION OF THE PROTEINS HOMOLOGOUS WITH THE CYSTEINE PROTEINASE INHIBITOR CHICKEN CYSTATIN." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-004.

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Machleidt, W., A. Ritonja, T. Popovic, et al. "Human cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogens." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-005.

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Meloun, B., J. Pohl, and V. Kostka. "Tentative amino acid sequence of bovine spleen cathepsin B." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-006.

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