Relevant bibliographies by topics / Cysteine protease

Academic literature on the topic 'Cysteine protease'

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Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "Cysteine protease"

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Mitchell, Angela M., and R. Jude Samulski. "Mechanistic Insights into the Enhancement of Adeno-Associated Virus Transduction by Proteasome Inhibitors." Journal of Virology 87, no. 23 (September 11, 2013): 13035–41. http://dx.doi.org/10.1128/jvi.01826-13.

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Proteasome inhibitors (e.g., bortezomib, MG132) are known to enhance adeno-associated virus (AAV) transduction; however, whether this results from pleotropic proteasome inhibition or off-target serine and/or cysteine protease inhibition remains unresolved. Here, we examined recombinant AAV (rAAV) effects of a new proteasome inhibitor, carfilzomib, which specifically inhibits chymotrypsin-like proteasome activity and no other proteases. We determined that proteasome inhibitors act on rAAV through proteasome inhibition and not serine or cysteine protease inhibition, likely through positive changes late in transduction.
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FAMPA, P., C. V. LISBOA, A. M. JANSEN, A. L. S. SANTOS, and M. I. RAMIREZ. "Protease expression analysis in recently field-isolated strains of Trypanosoma cruzi: a heterogeneous profile of cysteine protease activities between TC I and TC II major phylogenetic groups." Parasitology 135, no. 9 (July 14, 2008): 1093–100. http://dx.doi.org/10.1017/s0031182008004587.

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SUMMARYProtease expression among TCI and TCII field isolates was analysed. Gelatin-containing gels revealed hydrolysis bands with molecular masses ranging from 45 to 66 kDa. The general protease expression profile showed that TCII isolates presented higher heterogeneity compared to TCI. By utilizing protease inhibitors, we showed that all active proteases at acid pH are cysteine-proteases and all proteases active at alkaline pH are metalloproteases. However, the expression of cruzipain, the T. cruzi major cysteine-protease, did not reproduce a heterogeneous TCII cysteine zymogram profile. Dendogram analyses based on presence/absence matrices of proteases and cruzipain bands showed a TCI separation from the TCII group with 50–60% similarity. We suggest that the observed cysteine protease diversification contributes to differential host infection between TCI and II genotypes.
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Jairajpuri, Mohamad Aman, and Shoyab Ansari. "Using serpins cysteine protease cross-specificity to possibly trap SARS-CoV-2 Mpro with reactive center loop chimera." Clinical Science 134, no. 17 (September 1, 2020): 2235–41. http://dx.doi.org/10.1042/cs20200767.

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Abstract Human serine protease inhibitors (serpins) are the main inhibitors of serine proteases, but some of them also have the capability to effectively inhibit cysteine proteases. Severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) main protease (Mpro) is a chymotrypsin-type cysteine protease that is needed to produce functional proteins essential for virus replication and transcription. Serpin traps its target proteases by presenting a reactive center loop (RCL) as protease-specific cleavage site, resulting in protease inactivation. Mpro target sites with its active site serine and other flanking residues can possibly interact with serpins. Alternatively, RCL cleavage site of serpins with known evidence of inhibition of cysteine proteases can be replaced by Mpro target site to make chimeric proteins. Purified chimeric serpin can possibly inhibit Mpro that can be assessed indirectly by observing the decrease in ability of Mpro to cleave its chromogenic substrate. Chimeric serpins with best interaction and active site binding and with ability to form 1:1 serpin–Mpro complex in human plasma can be assessed by using SDS/PAGE and Western blot analysis with serpin antibody. Trapping SARS-CoV-2 Mpro cysteine protease using cross-class serpin cysteine protease inhibition activity is a novel idea with significant therapeutic potential.
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SIJWALI, Puran S., Bhaskar R. SHENAI, Jiri GUT, Ajay SINGH, and Philip J. ROSENTHAL. "Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3." Biochemical Journal 360, no. 2 (November 26, 2001): 481–89. http://dx.doi.org/10.1042/bj3600481.

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In the malaria parasite Plasmodium falciparum, erythrocytic trophozoites hydrolyse haemoglobin to provide amino acids for parasite protein synthesis. Cysteine protease inhibitors block parasite haemoglobin hydrolysis and development, indicating that cysteine proteases are required for these processes. Three papain-family cysteine protease sequences have been identified in the P. falciparum genome, but the specific roles of their gene products and other plasmodial proteases in haemoglobin hydrolysis are uncertain. Falcipain-2 was recently identified as a principal trophozoite cysteine protease and potential drug target. The present study characterizes the related P. falciparum cysteine protease falcipain-3. As is the case with falcipain-2, falcipain-3 is expressed by trophozoites and appears to be located within the food vacuole, the site of haemoglobin hydrolysis. Both proteases require a reducing environment and acidic pH for optimal activity, and both prefer peptide substrates with leucine at the P2 position. The proteases differ, however, in that falcipain-3 undergoes efficient processing to an active form only at acidic pH, is more active and stable at acidic pH, and has much lower specific activity against typical papain-family peptide substrates, but has greater activity against native haemoglobin. Thus falcipain-3 is a second P. falciparum haemoglobinase that is particularly suited for the hydrolysis of native haemoglobin in the acidic food vacuole. The redundancy of cysteine proteases may offer optimized hydrolysis of both native haemoglobin and globin peptides. Consideration of both proteases will be necessary to evaluate cysteine protease inhibitors as antimalarial drugs.
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Van Wyk, S. G., K. J. Kunert, B. J. Vorster, and U. Schluter. "Interaction of cysteine protease inhibitor mutants with cysteine proteases." South African Journal of Botany 76, no. 2 (April 2010): 406. http://dx.doi.org/10.1016/j.sajb.2010.02.053.

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Semenov, Andrey, Jed E. Olson, and Philip J. Rosenthal. "Antimalarial Synergy of Cysteine and Aspartic Protease Inhibitors." Antimicrobial Agents and Chemotherapy 42, no. 9 (September 1, 1998): 2254–58. http://dx.doi.org/10.1128/aac.42.9.2254.

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ABSTRACT It has been proposed that the Plasmodium falciparumcysteine protease falcipain and aspartic proteases plasmepsin I and plasmepsin II act cooperatively to hydrolyze hemoglobin as a source of amino acids for erythrocytic parasites. Inhibitors of each of these proteases have potent antimalarial effects. We have now evaluated the antimalarial effects of combinations of cysteine and aspartic protease inhibitors. When incubated with cultured P. falciparumparasites, cysteine and aspartic protease inhibitors exhibited synergistic effects in blocking parasite metabolism and development. The inhibitors also demonstrated apparent synergistic inhibition of plasmodial hemoglobin degradation both in culture and in a murine malaria model. When evaluated for the treatment of murine malaria, a combination of cysteine and aspartic protease inhibitors was much more effective than higher concentrations of either compound used alone. These results support a model whereby plasmodial cysteine and aspartic proteases participate in the degradation of hemoglobin, and they suggest that combination antimalarial therapy with inhibitors of the two classes of proteases is worthy of further study.
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Mann, Krin, and Hélène Sanfaçon. "Expanding Repertoire of Plant Positive-Strand RNA Virus Proteases." Viruses 11, no. 1 (January 15, 2019): 66. http://dx.doi.org/10.3390/v11010066.

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Many plant viruses express their proteins through a polyprotein strategy, requiring the acquisition of protease domains to regulate the release of functional mature proteins and/or intermediate polyproteins. Positive-strand RNA viruses constitute the vast majority of plant viruses and they are diverse in their genomic organization and protein expression strategies. Until recently, proteases encoded by positive-strand RNA viruses were described as belonging to two categories: (1) chymotrypsin-like cysteine and serine proteases and (2) papain-like cysteine protease. However, the functional characterization of plant virus cysteine and serine proteases has highlighted their diversity in terms of biological activities, cleavage site specificities, regulatory mechanisms, and three-dimensional structures. The recent discovery of a plant picorna-like virus glutamic protease with possible structural similarities with fungal and bacterial glutamic proteases also revealed new unexpected sources of protease domains. We discuss the variety of plant positive-strand RNA virus protease domains. We also highlight possible evolution scenarios of these viral proteases, including evidence for the exchange of protease domains amongst unrelated viruses.
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Shibao, Priscila Yumi Tanaka, Milene Ferro, Fernando Fonseca Pereira de Paula, Bruno Salata Lima, and Flávio Henrique-Silva. "Identification and Functional Analysis of a Pseudo-Cysteine Protease from the Midgut Transcriptome of Sphenophorus levis." International Journal of Molecular Sciences 22, no. 21 (October 25, 2021): 11476. http://dx.doi.org/10.3390/ijms222111476.

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The Sphenophorus levis (Coleoptera, Curculionidae) is one of the main pests of sugarcane in Brazil. Although its major digestive proteases are known, its complex digestive process still needs to be further understood. We constructed a transcriptome from the midgut of 30-day-old larvae and identified sequences similar to its major digestive protease (cysteine cathepsin Sl-CathL), however, they presented a different amino acid than cysteine in the active cleft. We identified, recombinantly produced, and characterized Sl-CathL-CS, a pseudo cysteine protease, and verified that higher gene expression levels of Sl-CathL-CS occur in the midgut of 30-day old larvae. We reverted the serine residue to cysteine and compared the activity of the mutant (Sl-CathL-mutSC) with Sl-CathL-CS. Sl-CathL-CS presented no protease activity, but Sl-CathL-mutSC hydrolyzed Z-Phe-Arg-AMC (Vmax = 1017.60 ± 135.55, Km = 10.77 mM) and was inhibited by a cysteine protease inhibitor E-64 (Ki = 38.52 ± 1.20 μM), but not by the serine protease inhibitor PMSF. Additionally, Sl-CathL-CS interacted with a sugarcane cystatin, while Sl-CathL-mutSC presented weaker interaction. Finally, protein ligand docking reinforced the differences in the catalytic sites of native and mutant proteins. These results indicate that Sl-CathL-CS is a pseudo-cysteine protease that assists protein digestion possibly by interacting with canecystatins, allowing the true proteases to work.
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Lee, Jung-Yub, Su-Min Song, Eun-Kyung Moon, Yu-Ran Lee, Bijay Kumar Jha, Dinzouna-Boutamba Sylvatrie Danne, Hee-Jae Cha, et al. "Cysteine Protease Inhibitor (AcStefin) Is Required for Complete Cyst Formation of Acanthamoeba." Eukaryotic Cell 12, no. 4 (February 8, 2013): 567–74. http://dx.doi.org/10.1128/ec.00308-12.

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ABSTRACTThe encystation ofAcanthamoebaleads to the formation of resilient cysts from vegetative trophozoites. This process is essential for parasite survival under unfavorable conditions, such as those associated with starvation, low temperatures, and biocides. Furthermore, cysteine proteases have been implicated in the massive turnover of intracellular components required for encystation. Thus, strict modulation of the activities of cysteine proteases is required to protectAcanthamoebafrom intracellular damage. However, mechanisms underlying the control of protease activity during encystation have not been established inAcanthamoeba. In the present study, we identified and characterizedAcanthamoebacysteine protease inhibitor (AcStefin), which was found to be highly expressed during encystation and to be associated with lysosomes by fluorescence microscopy. Recombinant AcStefin inhibited various cysteine proteases, including human cathepsin B, human cathepsin L, and papain. Transfection with small interfering RNA against AcStefin increased cysteine protease activity during encystation and resulted in incomplete cyst formation, reduced excystation efficiency, and a significant reduction in cytoplasmic area. Taken together, these results indicate that AcStefin is involved in the modulation of cysteine proteases and that it plays an essential role during the encystation ofAcanthamoeba.
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Davis, David A., Keisuke Yusa, Laura A. Gillim, Fonda M. Newcomb, Hiroaki Mitsuya, and Robert Yarchoan. "Conserved Cysteines of the Human Immunodeficiency Virus Type 1 Protease Are Involved in Regulation of Polyprotein Processing and Viral Maturation of Immature Virions." Journal of Virology 73, no. 2 (February 1, 1999): 1156–64. http://dx.doi.org/10.1128/jvi.73.2.1156-1164.1999.

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ABSTRACT We investigated the role of the two highly conserved cysteine residues, cysteines 67 and 95, of the human immunodeficiency virus type 1 (HIV-1) protease in regulating the activity of that protease during viral maturation. To this end, we generated four HIV-1 molecular clones: the wild type, containing both cysteine residues; a protease mutant in which the cysteine at position 67 was replaced by an alanine (C67A); a C95A protease mutant; and a double mutant (C67A C95A). When immature virions were produced in the presence of an HIV-1 protease inhibitor, KNI-272, and the inhibitor was later removed, limited polyprotein processing was observed for wild-type virion preparations over a 20-h period. Treatment of immature wild-type virions with the reducing agent dithiothreitol considerably improved the rate and extent of Gag processing, suggesting that the protease is, in part, reversibly inactivated by oxidation of the cysteine residues. In support of this, C67A C95A virions processed Gag up to fivefold faster than wild-type virions in the absence of a reducing agent. Furthermore, oxidizing agents, such as H2O2 and diamide, inhibited Gag processing of wild-type virions, and this effect was dependent on the presence of cysteine 95. Electron microscopy revealed that a greater percentage of double-mutant virions than wild-type virions developed a mature-like morphology on removal of the inhibitor. These studies provide evidence that under normal culture conditions the cysteines of the HIV-1 protease are susceptible to oxidation during viral maturation, thus preventing immature virions from undergoing complete processing following their release. This is consistent with the cysteines being involved in the regulation of viral maturation in cells under oxidative stress.
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Dissertations / Theses on the topic "Cysteine protease"

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James, Karen Amanda Ellis. "Design, synthesis, and evaluation of novel cysteine protease inhibitors." Diss., Georgia Institute of Technology, 2002. http://hdl.handle.net/1853/30283.

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Ismail, Ihab. "Function and Regulation of Xylem Cysteine Protease 1 and Xylem Cysteine Protease 2 in Arabidopsis." Diss., Virginia Tech, 2003. http://hdl.handle.net/10919/11243.

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A functional water-conducting system, the tracheary elements of the xylem, is required to sustain plant growth and development. Tracheary element formation is dependent on many biological processes terminated by programmed cell death and cellular autolysis. The final two processes are probably dependent on the activity of hydrolytic enzymes such as XCP1 and XCP2 known to be expressed in tracheary elements during these final two processes. Thus, the transcriptional regulation of XCP1 and the function of XCP2 were investigated. Qualitative and quantitative assessments of GUS activity as directed by various fragments of the XCP1 promoter showed that a 237-bp internal region was able to drive GUS expression in a tracheary element-specific manner in Arabidopsis. A 25-bp deletion at the 3' end of this region abolished GUS expression. The 237-bp region served as bait in a yeast one-hybrid analysis. Screening of yeast colonies retrieved 109 putative positive interactions, which included a potential transcriptional regulator, indole acetic acid-induced protein 8 (IAA8). An auxin responsive element that potentially binds auxin responsive transcription factors was found within the 25-bp deletion. Cis-elements were predicted by Genomatix and Athamap computer programs. The cis-elements form pyrimidine and gibberellic acid responsive elements that can potentially bind Dof and Myb transcription factors, respectively. In an independent effort, attempts to develop a mapping population to isolate upstream regulators of XCP1 expression did not succeed. Functionally, tracheary element-specific expression of XCP2 in Arabidopsis suggested a specialized role for XCP2 in final phases of tracheary element differentiation. The function of XCP2 was assessed using T-DNA insertional mutants, post-transcriptional gene silencing, and through tracheary element-specific expression of the cysteine protease inhibitor, soyacystatin N in Arabidopsis. Our findings revealed that the absence of XCP2 expression due to T-DNA insertional mutagenesis did not affect plant growth and development in the laboratory. Soyacystatin N was an effective in vitro inhibitor of cysteine proteases. Plants expressing 35S-driven cytosolic form of soyacystatin exhibited stunting and reduced apical dominance. Plants expressing pXCP1-driven cytosolic soyacystatin did not differ from wild type plants. Additionally, transgenic plants expressing pXCP1- and 35S-directed XCP2-double-stranded RNA for the silencing of XCP2 showed no unusual phenotypes compared to their wild type counterparts
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Pol, Ewa. "Mechanism of interaction of the mammalian cysteine protease inhibitors, cystatin A and B, with target proteases /." Uppsala : Swedish Univ. of Agricultural Sciences (Sveriges lantbruksuniv.), 2001. http://epsilon.slu.se/avh/2001/91-576-5927-3.pdf.

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Leung, Donmienne Doen Mun. "Studies of serine and cysteine protease inhibitors /." St. Lucia, Qld, 2001. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe16491.pdf.

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Acquistapace, Bethany R. "Analysis of a trichomonas vaginalis cysteine protease." Scholarly Commons, 2007. https://scholarlycommons.pacific.edu/uop_etds/669.

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Trichomoniasis affects 170 million people worldwide, and 7.4 million in the USA. There is increasing focus on the role of cysteine proteases in Trichomonas vaginalis because of their role in virulence of other parasitic protozoa. Determining their location and function will provide insight about their role in the pathogenicity of T. vaginalis and their feasibility as a drug target. This study begins to characterize the first sequenced cysteine protease (CP1). E. coli and P. pastoris expression systems were developed to produce CP1 to generate antiserum, and to have enough active protein for biochemical characterization. Secondly, endogenous and epitope tagged CP1 were localized in T. vaginalis vesicles. These vesicles were confirmed to have alkaline phosphatase activity which is a characteristic of lysosomes. Lastly, deletion mutants of CP1 were created to determine the role of the prodomain in targeting CP1 to vesicles.
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Shabab, M. "Study on cysteine protease and their inhibitors." Thesis(Ph.D.), CSIR-National Chemical Laboratory, Pune, 2009. http://dspace.ncl.res.in:8080/xmlui/handle/20.500.12252/2736.

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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 some notable exceptions. Both enzymes prefer disubstituted amides to monosubstituted amides in the P1' position and potency increased as we increased the hydrophobicity of the inhibitor in this position. Extending the inhibitor to P5 resulted in increased inhibitory potency, especially against IrAE, and both enzymes prefer small over large hydrophobic residues in the P2 position. Aza-peptide Michael acceptor inhibitors are more potent than aza-peptide epoxide inhibitors and, for some of these compounds, second order inhibition rate constants are the fastest yet discovered. We have also synthesized aza-peptidyl Michael acceptor and epoxide inhibitors for the parasitic cysteine proteases; cruzain, rhodesain. We have found that monosubstituted amides were favored over disubstituted amides indicating the involvement of the amide hydrogen in a H-bond network. We have shown that aza-peptide epoxides were as potent as Michael acceptors and we have obtained compounds with IC50 values as low as 20 nM. We have worked on the synthesis of heterocyclic peptidyl α-ketoamides, peptidyl ketones and aza-peptidyl ketones as calpain inhibitors. We have synthesized peptidyl α-ketoamides with nucleotide bases in the primed region to create compounds that can cross the blood-brain barrier. We have improved the potency by introducing a hydrophobic group on the adenine ring. We have obtained compounds with Ki values in the nanomolar range. We have designed peptidyl aminoketones as a new class of inhibitors for calpain. Peptidyl aminoketones were less potent than peptidyl α-ketoamides but still reasonable inhibitors of calpain that have the potential to cross the BBB.
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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.
Murthy, Niren, Committee Member ; Doyle, Donald, Committee Member ; Fahrni, Christoph, Committee Member ; May, Sheldon, Committee Member ; Powers, James, Committee Chair.
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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-activated human enzyme involved in neurodegeneration. These inhibitors proved to be poor inactivators of calpain, demonstrating that the aza-peptide epoxide is a warhead specific to clan CD cysteine proteases (caspases, gingipains). Subsequently, a known epoxide inhibitor of calpain was optimized to create a more potent inhibitor. Several of these inhibitors were more potent than the parent, and all were demonstrated to inhibit calpain in a breast cancer cell line which was treated with paclitaxel to spike calpain activity. The second project involved the design and solid phase synthesis of aza-peptide Michael acceptor caspases inhibitors. The two goals of this project were to develop a solid phase method for synthesis of inhibitors that are tedious to synthesize in solution phase, and to use a variety of amino acid residues to determine the optimal interactions in the P3? position for various caspases. The synthesis was successful, and the optimal P3? residues were determined. The third project involved the kinetic evaluation of aza-peptide epoxide and Michael acceptor inhibitor designed for the gingipains. Gingipains K and R are virulence factors in the pathology of Porphyromonas gingivalis involved in gingivitis and periodontal disease. These inhibitors proved to be extremely potent inactivators of gingipains, with some of the highest rates of inhibition measured in the Powers laboratory. Gingipain K preferred larger, aromatic moieties in the P1? position, while gingipain R preferred the Michael acceptor inhibitors, with the P1? substituent having less of an impact on potency.
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Håkansson, Katarina. "Cystatin C functions in vitro and in vivo studies on target enzyme inhibition by cystatin C variants and cystatin C deficient mice /." Lund : Dept. of Clinical Chemistry, University of Lund, University Hospital, 1998. http://catalog.hathitrust.org/api/volumes/oclc/40343026.html.

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Books on the topic "Cysteine protease"

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

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Massimi, Isabella. SspB cysteine protease of Staphylococcus aureus promotes detachment of human keratinocytes and degrades fibronectin and vitronectin. Ottawa: National Library of Canada, 2001.

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Kirschke, Heidrun. Lysosomal cysteine proteases. 2nd ed. Oxford: Oxford University Press, 1997.

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Quigley, Kim. The use of deuterium kinetic solvent isotope effects and the proton inventory method in the elucidation of the catalyticmechanism of the cysteine protease papain. Birmingham: University of Birmingham, 1987.

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Robinson, Mark W., and John P. Dalton, eds. Cysteine Proteases of Pathogenic Organisms. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-8414-2.

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Cysteine proteases of pathogenic organisms. New York: Springer Science+Business Media, 2011.

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

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

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Cam, Patterson, and Cyr Douglas M, eds. Ubiquitin-proteasome protocols. Totowa, N.J: Humana Press, 2005.

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Estrada, Sergio. Cystatin A, a mammalian cysteine proteinase inhibitor: Mechanism of inhibition of target proteinases by recombinant cystatin A variants. Uppsala: Sveriges Lantbruksuniversitet, 1998.

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Book chapters on the topic "Cysteine protease"

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Horstkorte, Rüdiger, Bettina Büttner, Kaya Bork, Navdeep Sahota, Sarah Sabir, Laura O’Regan, Joelle Blot, et al. "Non-Lysosomal Cysteine Protease." In Encyclopedia of Signaling Molecules, 1254. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100933.

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Ghosh, Arun K., and Sandra Gemma. "Design of Cysteine Protease Inhibitors." In Structure-Based Design of Drugs and Other Bioactive Molecules, 131–42. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527665211.ch5.

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Wilkesman, Jeff. "Cysteine Protease Zymography: Brief Review." In Zymography, 25–31. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7111-4_3.

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Nishida, Y., H. Tsushima, N. Toki, H. Sumi, and H. Mihara. "Thiol protease inhibitor released from human malignant melanoma." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk, 751–60. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-069.

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Kawashima, G., M. Inomata, and K. Imahori. "Control mechanism of calcium-activated neutral protease (CANP) activity." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk, 359–68. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-036.

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Vincent, J. L., and N. J. Brewin. "Cysteine Protease Localisation in Pea Root Nodules." In Nitrogen Fixation: From Molecules to Crop Productivity, 260. Dordrecht: Springer Netherlands, 2002. http://dx.doi.org/10.1007/0-306-47615-0_138.

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Colella, Rita, Ann F. Chambers, and David T. Denhardt. "Anticarcinogenic Activities of Naturally Occurring Cysteine Proteinase Inhibitors." In Protease Inhibitors as Cancer Chemopreventive Agents, 199–216. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2882-1_12.

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Imahori, K., S. Kawashima, and M. Nakamura. "Characterization of low molecular weight and high molecular weight endogenous inhibitors of calcium activated neutral protease." In Cysteine Proteinases and their Inhibitors, edited by Vito Turk, 617–30. Berlin, Boston: De Gruyter, 1986. http://dx.doi.org/10.1515/9783110846836-059.

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Matsueda, Rei, Hideaki Umeyama, Eiki Kominami, and Nobuhiko Katunuma. "Cysteine Protease Inhibitors with S-(3-Nitro-2-Pyridinesulfenyl)-Cysteine Residue in Affinity Analogs of Peptide Substrates." In Advances in Experimental Medicine and Biology, 265–70. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4615-9546-5_44.

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Arthur, Gavin D., and Angelo N. Belcastro. "A calcium stimulated cysteine protease involved in isoproterenol induced cardiac hypertrophy." In The Cellular Basis of Cardiovascular Function in Health and Disease, 241–48. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5765-4_31.

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Conference papers on the topic "Cysteine protease"

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Hassan, H. J., L. Cianetti, P. M. Mannucci, V. Vicente, R. Cortese, and C. Peschle. "HEREDITARY THROMBOPHILIA CAUSED BY MISSENSE MUTATION IN PROTEIN C GENE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642944.

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The structure of the gene for protein C was analyzed in 13 protein C deficient unrelated patients (11 heterozygous, 2 homozygous), who showed an equivalent reduction of this serine protease at both enzymatic and antigen level. No deletion(s) or rearrangement(s) was demonstrated by Southern blot after hybridization to a cDNA probe. One patient showed a variant restriction pattern after Bam HI digestion, characterized by an abnormal 9.6 kb band in addition to the 8.3 and 1.3 normal ones. Extensive family studies, including 7 heterozygotes with the same clinical phenotype, showed the same abnormal pattern in all and only these heterozygotes. Protein C gene from the propositus was cloned in EMBL3 lambda vector. A 411 bp PstI - SacI fragment from exon 9 encompassing the mutation in the Bam HI site was subcloned in M13mpl8. Its sequence showed a single transversion in the Bam HI palyndrome (GGATCC -> GCATCC) : this causes a substitution of the 402 thryptophan residue with a cystein. The 402 thryptophan residue is constantly conserved in a biochemical domain present in all eukaryotic serine proteases: substitution of the large thryptophan aromatic ring with the small cysteine hydrophilic side-chain conceivably leads to destabilization of the tertiary structure of protein C in these heterozygotes. Thus, the point mutation reported here is sufficient to explain the protein C deficiency in these subjects, and is apparently responsible for their clinical phenotype.
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Santi, Claudio, Luca Sancineto, Francesca Mangiavacchi, Cecilia Scimmi, and Sougat Misra. "ELECTROPHILIC ORGANOSELENIUM COMPOUNDS AND SARS-COV-2: PRO-OXIDANT ACTIVITY AS A MORE PROMISING WAY TOWARDS THE DRUGGABILITY." In 1st INTERNATIONAL Conference on Chemo and BioInformatics. Institute for Information Technologies, University of Kragujevac,, 2021. http://dx.doi.org/10.46793/iccbi21.020s.

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Ebselent has been recently reported as the most efficient hinibitors of Sars-Cov-2 main protease (Mpro) thought the electrophilic covalent pro-oxidation of the reactive Cysteine 145. According to similar evidences in literature we can propose a general mechanism to explore a novel and promising application of mild organoselenium centered electrophiles in medicinal chemistry. New insights in the field of covalent and non-covalent inhibition of Mpro as well as the antiviral SARS-Cov2 activity of novel organoselenium compounds will be here discussed
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Kossack, R., S. Breinlinger, T. Nguyen, T. Schirmeister, H. Enke, and T. Niedermeyer. "The putative PAINs nostotrebin 6 and derivatives from Nostoc sp. inhibit the trypanosomal cysteine protease rhodesain." In GA 2017 – Book of Abstracts. Georg Thieme Verlag KG, 2017. http://dx.doi.org/10.1055/s-0037-1608156.

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Suzuki, Koji, Yoshihiro Deyashiki, Junji Nishioka, Kazunori Toma, and Shuji Yamamoto. "THE INHIBITOR OF ACTIVATED PROTEIN C: STRUCTURE AND FUNCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642963.

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In the final step of protein C pathway, activated protein C (APC) is neutralized with a plasma inhibitor, termed protein C inhibitor (PCI). PCI was first described by Marlar and Griffin (1980) and then isolated from human plasma as a homogeneous form and characterized by the authors (1983). PCI is a single chain glycoprotein with M 57,000 and a plasma concentration of 5 ug/ml. Analysis of a cDNA nucleotide sequence has clarified that a precursor of human PCI consists of a mature protein of 387 amino acid residues (M 43,759) and a signal peptide of 19 amino acid residues. Only one cysteine residue is present in the entire protein as in α1antitrypsin (α1AT) and α1antichymotrypsin (α1ACT). Three Asn-X-Ser/Thr sequences and two Ser/Thr-X-X-Pro sequences are present as potential attachment sites of carbohydrate chains. Based on the amino acid sequence of the carboxyl-terminal peptide released from the inhibitor by APC digestion, the reactive site peptide bond of PCI was found to be Arg(354)-Ser(355). It is similar to the reactive sites of the other serine protease inhibitors which are located to their carboxyl-terminal Arg(393)-Ser (394), Met(358)-Ser(359) and Leu(358)-Ser(359) in antithrombin III, α1AT and α1ACT, respectively. The alignment of the amino acid sequence of PCI with heparin cofactor II, α1plasmin inhibitor, ovalbumin, angiotensinogen and the above noted plasma inhibitors showed that PCI is a member of serine protease inhibitor superfamily. PCI inhibits APC noncompetitively in a 1:1 stoichiometry and forms a covalent acyl-bond with a Ser residue in the active center of APC. The half life of APC in plasma approximately 30 min, which is rather slow compared with the other protease inhibitors. However, optimal concentrations of heparin, dextran sulfate and its derivatives potentiate the rate of inhibition 30-60 fold. PCI has Ki of 10-8m for APC, and can inhibit thrombin, Factor Xa, urokinase and tissue plasminogen activator as well in the presence of heparin or dextran sulfate, though the Ki for these enzymes is slightly higher. During the complex formation with APC, PCI is cleaved by the complexed APC to form a modified form with M 54,000. PCI is synthesized in several hepatoma cell lines and decreased in plasma of patients with liver cirrhosis. It is also decreased in patients with DIC or those during cardiopulmonary bypass in parallel with the decrease in protein C, suggesting that PCI participates in regulation of the protein C pathway in intravascular coagulation. Recently, we have obtained the recombinant PCI from COS-1 cells which were transfected with expression vector pSV2 containing the cDNA of PCI. The recombinant PCI had the same Mr and specific activity as the protein purified from plasma. It also had an affinity for heparin and dextran sulfate. Moreover, we have predicted a three dimentional structure of the proteolytically modified PCI with computer graphics based on its amino acid sequence homology with the modified α1AT whose structure had been elucidated with X-ray crystallography. All potential carbohydrate attachment sites were estimated to exist on the surface of the protein. Succesively we have constructed the interaction model between the intact PCI predicted from the modified form and the active center of APC which was simulated from that of trypsin. From the model, it was observed that the amino-group of Arg (354, PI site) of PCI could strongly interact with the carboxy1-group of Asp (88, SI site) of the heavy chain of APC at the base of the active center pocket of the enzyme.
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"Functional characterization of papain-like cysteine proteases genes in rice." In Plant Genetics, Genomics, Bioinformatics, and Biotechnology. Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, 2019. http://dx.doi.org/10.18699/plantgen2019-124.

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Petushkova, Anastasiia, Arthur Zalevsky, Neonila Gorokhovets, Vladimir Makarov, Lyudmila Savvateeva, Marina Serebryakova, Andrey Golovin, Evgeni Zernii, and Andrey Zamyatnin. "pH-Dependent Specificity of Papain-Like Cysteine Proteases Is Determined by S1 Binding Pocket." In IECBM 2022. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/iecbm2022-13385.

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7

Rabbani, Naila, Paul John Thornalley, Maryam Al-Motawa, and Mingzhan Xue. "Vulnerabilities of the SARS-Cov-2 Virus to Proteotoxicity – Opportunity for Repurposed Chemotherapy of COVID-19 Infection." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2020. http://dx.doi.org/10.29117/quarfe.2020.0291.

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The global pandemic of COVID-19 disease caused by infection with the SARS-CoV-2 Coronavirus, has produced an urgent requirement and search for improved treatments whilst effective vaccines are developed. A strategy for improved drug therapy is to increase levels of endogenous reactive metabolites for selective toxicity to SARS-CoV-2 by preferential damage to the viral proteome. Key reactive metabolites producing major quantitative damage to the proteome in physiological systems are: Reactive oxygen species (ROS) and the reactive glycating agent methylglyoxal (MG); cysteine residues and arginine residues are their most susceptible targets, respectively. From sequenced-based prediction of the SARS-CoV-2 proteome, we found 0.8-fold enrichment or depletion of cysteine residues in functional domains of the viral proteome; whereas there was a 4.6-fold enrichment of arginine residues, suggesting SARS-CoV-2 is resistant to oxidative agents and sensitive to MG. We examined activated arginine residues in functional domain with predicted low pKa by neighboring group interaction in the SARS-CoV-2. We found 25 such arginine residues, including 2 in the spike protein and 10 in the nucleoprotein. These sites were partially conserved in related coronaviridae: SARS-COV and MERS. We also screened and identified drugs, which increase cellular MG concentration to virucidal levels and found two antitumor drugs with historical antiviral activity, doxorubicin and paclitaxel were the best candidate for repurposing. Our findings provide evidence of potential vulnerability of SARS-CoV2 to inactivation by MG and a scientific rationale for repurposing of doxorubicin and paclitaxel for treatment of COVID-19 disease, providing efficacy and adequate therapeutic index may be established.
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Roncaglioni, M. C., A. Falanga, A. P. Bolognese Dalessandro, B. Casali, and M. B. Donti. "ENZYMATIC AND IMMUNOLOGIC CHARACTERIZATION OF A CYSTEINE PROTEINASE PROCOAGULANT IN SEVERAL MURINE METASTASIZING TUMO." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643663.

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Involvement of the hemostatic systemin tumor metastasis growth has been repeatedly suggested and several tumor-associated procoagulants have been described. We have studied here the procoagulant activity (PCA) of tissue extracts from 4 murine metastasizing tumors: Lewis Lung Carcinoma (3LL), B16 melanoma (B16), JW sarcoma (JWS) and the M4 variant of the mFS6 fibrosarcoma (M4). The experiments were designed to identify cancer procoagulant (CP) a FVII independent FX activating cysteine proteinase or tissue factor (TF) in these tumors. Tissue extracts from 3LL, B16 and JWS initiated coagulation both in the presence and absence of FVII (FVII independent activity ranging from 70% to 86% of the total activity). The PCA of the same tumors was significantly decreased (p < 0.01) by cysteine proteinase inhibitors (1 mM iodoacetamide (IA) and 0.1 mM HgCl2 ) and the inhibitionby HgCl2 was reversed by -SH group activators (di-thiatreital, KCN, IiDTA). In addition these samples were able of directly activating pure bovineFX in a two stage clotting assay. The PCA of M4 extract was dependent on FVII,was not significantly affected by IA and HgCl2 and was inhibited by concanavalin A, a known TF inhibitor. An Ouchterlony double immunodiffusion study showed immunological cross-reactivity of 3LL, B16 and JWS to a polyclonal antibody to purified CP (from rabbit V2 carcinoma; obtained from S.G. Gordon, Denver, USA). No cross-reactivity was present between this antibody and M4. This study shows that the PCA of M4 is TF, whereas the procoagulant(s) of 3LL, B16 and JWS are enzymatically and immunologically indistinguishable from CP.
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Falang, A., G. M. Alessio, M. Donati, and T. A. Barbui. "DISSEMINATED INTRAVASCULAR COAGULATION (DIC) AND ACUTE LEUKEMIA:IDENTIFICATION OF A NEW CELLULAR PROCOAGULANT." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643661.

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There is an enhanced incidence (>50%) of severe coagulopathy in association with several types of acute leukemias. Cell associated procoagulants are considered important in this context. So far only a Tissue Factor (TF)-type procoagulant has been described in leukemic cells. We have set up here the experimentalconditions to identify other possible cellular procoagulants in leukemia. We have tested blast cell extracts from 21 patients with 5 different cytological subtypes (from Ml to M5 of acute non lymphoid leukemia (ANLL), according to theFAB classification, in order to assay whether they express "cancer procoagulant" (CP), a F VH-independent FX activating cysteine proteinase (Falanga … Gordon, 1985; Donati, et al. 1986). All the samples shortened the recalcification time of normal human plasma, the effect being significantly greater (p<0.001) in the M3 group. The activity was 20% to 100% independent from the presence of FVII and was susceptible to 2 cysteine proteinase inhibitors (Iodoacetamide, 2 mM, and HgCl2 ,0.1 mM) in all of the extracts but the M5 type. In addition, M2 and M3 samples directly activated pure FX in a two stage clotting assay. Control cell extracts from 10 healthy donors did not show any procoagulant activity, under the same conditions. This study provides evidence for a new procoagulant expressed by cells of ANLL; the peculiar characteristics of this procoagulant (i.e. its confinement to the malignant phenotype, its shedding into the plasma, its possible modulation by vitamin K antagonists) make this observation of potential interest in the development of new diagnostic and therapeutic tools in ANLL.
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Carey, P. C. "Studies of enzymes by resonance Raman spectroscopy." In International Laser Science Conference. Washington, D.C.: Optica Publishing Group, 1986. http://dx.doi.org/10.1364/ils.1986.thg3.

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By creating a resonance Raman probe in the active site of an enzyme, it is possible to obtain the vibrational spectrum associated with those bonds undergoing catalytic transformation. The approach involves reacting thionoesters RC(= S)OCH3 with a class of enzymes known as cysteine proteases which have an essential SH group in their active sights HS-enzyme. The reaction produces an intermediate RC(= S) S-enzyme which is a dithioester with a λmax near 315 nm. The 324-nm excited RR spectra of the dithioester provide a wealth of detail on the substrate during catalysis; the confirmation of the substrate in the active sight can be monitored and characterized, structure rate constant relationships developed, reaction pathways mapped, and evidence sought for geometric distortion. The novel findings stemming from the RR data are difficult to reconcile with the conventional view of enzyme mechanism.
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Reports on the topic "Cysteine protease"

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Sanders, Tanya C. A New Class of Serine and Cysteine Protease Inhibitor with Chemotherapeutic Potential. Fort Belvoir, VA: Defense Technical Information Center, June 1999. http://dx.doi.org/10.21236/ada370850.

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Sanders, Tanya C. A New Class of Serine and Cysteine Protease Inhibitor with Chemotherapeutic Potential. Fort Belvoir, VA: Defense Technical Information Center, July 1998. http://dx.doi.org/10.21236/ada353868.

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Gafni, Yedidya, Moshe Lapidot, and Vitaly Citovsky. Dual role of the TYLCV protein V2 in suppressing the host plant defense. United States Department of Agriculture, January 2013. http://dx.doi.org/10.32747/2013.7597935.bard.

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TYLCV-Is is a major tomato pathogen, causing extensive crop losses in Israel and the U.S. We have identified a TYLCV-Is protein, V2, which acts as a suppressor of RNA silencing. Intriguingly, the counter-defense function of V2 may not be limited to silencing suppression. Our recent data suggest that V2 interacts with the tomato CYP1 protease. CYP1 belongs to the family of papain-like cysteine proteases which participate in programmed cell death (PCD) involved in plant defense against pathogens. Based on these data we proposed a model for dual action of V2 in suppressing the host antiviral defense: V2 targets SGS3 for degradation and V2 inhibits CYP1 activity. To study this we proposed to tackle three specific objectives. I. Characterize the role of V2 in SGS3 proteasomal degradation ubiquitination, II. Study the effects of V2 on CYP1 maturation, enzymatic activity, and accumulation and, III. Analyze the effects of the CYP1-V2 interaction on TYLCV-Is infection. Here we describe results from our study that support our hypothesis: the involvement of the host's innate immune system—in this case, PCD—in plant defense against TYLCV-Is. Also, we use TYLCV-Is to discover the molecular pathway(s) by which this plant virus counters this defense. Towards the end of our study we discovered an interesting involvement of the C2 protein encoded by TYLCV-Is in inducing Hypersensitive Response in N. benthamianaplants which is not the case when the whole viral genome is introduced. This might lead to a better understanding of the multiple processes involved in the way TYLCV is overcoming the defense mechanisms of the host plant cell. In a parallel research supporting the main goal described, we also investigated Agrobacteriumtumefaciens-encoded F-box protein VirF. It has been proposed that VirF targets a host protein for the UPS-mediated degradation, very much the way TYLCV V2 does. In our study, we identified one such interactor, an Arabidopsistrihelix-domain transcription factor VFP3, and further show that its very close homolog VFP5 also interacted with VirF. Interestingly, interactions of VirF with either VFP3 or VFP5 did not activate the host UPS, suggesting that VirF might play other UPS-independent roles in bacterial infection. Another target for VirF is VFP4, a transcription factor that both VirF and its plant functional homolog VBF target to degradation by UPS. Using RNA-seqtranscriptome analysis we showed that VFP4 regulates numerous plant genes involved in disease response, including responses to viral and bacterial infections. Detailed analyses of some of these genes indicated their involvement in plant protection against Agrobacterium infection. Thus, Agrobacterium may facilitate its infection by utilizing the host cell UPS to destabilize transcriptional regulators of the host disease response machinery that limits the infection.
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Fluhr, Robert, and Andreas Fischer. Functional analysis of barley cysteine proteases and their role in nitrogen remobilization from senescing leaves. United States Department of Agriculture, January 2016. http://dx.doi.org/10.32747/2016.7600048.bard.

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Seto, Christopher T. Anticancer Agents Based on a New Class of Transition- State Analog Inhibitors for Serine and Cysteine Proteases. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada377205.

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Seto, Christopher. Anticancer Agents Based on a New Class of Transition-State Analog Inhibitors for Serine and Cysteine Proteases. Fort Belvoir, VA: Defense Technical Information Center, August 2000. http://dx.doi.org/10.21236/ada383963.

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Sessa, Guido, and Gregory Martin. A functional genomics approach to dissect resistance of tomato to bacterial spot disease. United States Department of Agriculture, January 2004. http://dx.doi.org/10.32747/2004.7695876.bard.

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The research problem. Bacterial spot disease in tomato is of great economic importance worldwide and it is particularly severe in warm and moist areas affecting yield and quality of tomato fruits. Causal agent of spot disease is the Gram-negative bacterium Xanthomonas campestris pv. vesicatoria (Xcv), which can be a contaminant on tomato seeds, or survive in plant debris and in association with certain weeds. Despite the economic significance of spot disease, plant protection against Xcvby cultural practices and chemical control have so far proven unsuccessful. In addition, breeding for resistance to bacterial spot in tomato has been undermined by the genetic complexity of the available sources of resistance and by the multiple races of the pathogen. Genetic resistance to specific Xcvraces have been identified in tomato lines that develop a hypersensitive response and additional defense responses upon bacterial challenge. Central goals of this research were: 1. To identify plant genes involved in signaling and defense responses that result in the onset of resistance. 2. To characterize molecular properties and mode of action of bacterial proteins, which function as avirulence or virulence factors during the interaction between Xcvand resistant or susceptible tomato plants, respectively. Our main achievements during this research program are in three major areas: 1. Identification of differentially expressed genes during the resistance response of tomato to Xcvrace T3. A combination of suppression subtractive hybridization and microarray analysis identified a large set of tomato genes that are induced or repressed during the response of resistant plants to avirulent XcvT3 bacteria. These genes were grouped in clusters based on coordinate expression kinetics, and classified into over 20 functional classes. Among them we identified genes that are directly modulated by expression of the type III effector protein AvrXv3 and genes that are induced also during the tomato resistance response to Pseudomonas syringae pv. tomato. 2. Characterization of molecular and biochemical properties of the tomato LeMPK3MAP kinase. A detailed molecular and biochemical analysis was performed for LeMPK3 MAP kinase, which was among the genes induced by XcvT3 in resistant tomato plants. LeMPK3 was induced at the mRNA level by different pathogens, elicitors, and wounding, but not by defense-related plant hormones. Moreover, an induction of LeMPK3 kinase activity was observed in resistant tomato plants upon Xcvinfection. LeMPK3 was biochemically defined as a dual-specificity MAP kinase, and extensively characterized in vitro in terms of kinase activity, sites and mechanism of autophosphorylation, divalent cation preference, Kₘand Vₘₐₓ values for ATP. 3. Characteriztion of molecular properties of the Xcveffector protein AvrRxv. The avirulence gene avrRxvis involved in the genetic interaction that determines tomato resistance to Xcvrace T1. We found that AvrRxv functions inside the plant cell, localizes to the cytoplasm, and is sufficient to confer avirulence to virulent Xcvstrains. In addition, we showed that the AvrRxv cysteine protease catalytic core is essential for host recognition. Finally, insights into cellular processes activated by AvrRxv expression in resistant plants were obtained by microarray analysis of 8,600 tomato genes. Scientific and agricultural significance: The findings of these activities depict a comprehensive and detailed picture of cellular processes taking place during the onset of tomato resistance to Xcv. In this research, a large pool of genes, which may be involved in the control and execution of plant defense responses, was identified and the stage is set for the dissection of signaling pathways specifically triggered by Xcv.
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Citovsky, Vitaly, and Yedidya Gafni. Suppression of RNA Silencing by TYLCV During Viral Infection. United States Department of Agriculture, December 2009. http://dx.doi.org/10.32747/2009.7592126.bard.

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The Israeli isolate of Tomato yellow leaf curl geminivirus (TYLCV-Is) is a major tomato pathogen, causing extensive (up to 100%) crop losses in Israel and in the south-eastern U.S. (e.g., Georgia, Florida). Surprisingly, however, little is known about the molecular mechanisms of TYLCV-Is interactions with tomato cells. In the current BARD project, we have identified a TYLCV-Is protein, V2, which acts as a suppressor of RNA silencing, and showed that V2 interacts with the tomato (L. esculentum) member of the SGS3 (LeSGS3) protein family known to be involved in RNA silencing. This proposal will use our data as a foundation to study one of the most intriguing, yet poorly understood, aspects of TYLCV-Is interactions with its host plants – possible involvement of the host innate immune system, i.e., RNA silencing, in plant defense against TYLCV-Is and the molecular pathway(s) by which TYLCV-Is may counter this defense. Our project sought two objectives: I. Study of the roles of RNA silencing and its suppression by V2 in TYLCV-Is infection of tomato plants. II. Study of the mechanism by which V2 suppresses RNA silencing. Our research towards these goals has produced the following main achievements: • Identification and characterization of TYLCV V2 protein as a suppressor of RNA silencing. (#1 in the list of publications). • Characterization of the V2 protein as a cytoplasmic protein interacting with the plant protein SlSGS3 and localized mainly in specific, not yet identified, bodies. (#2 in the list of publications). • Development of new tools to study subcellular localization of interacting proteins (#3 in the list of publications). • Characterization of TYLCV V2 as a F-BOX protein and its possible role in target protein(s) degradation. • Characterization of TYLCV V2 interaction with a tomato cystein protease that acts as an anti-viral agent. These research findings provided significant insights into (I) the suppression of RNA silencing executed by the TYLCV V2 protein and (II) characterization some parts of the mechanism(s) involved in this suppression. The obtained knowledge will help to develop specific strategies to attenuate TYLCV infection, for example, by blocking the activity of the viral suppressor of gene silencing thus enabling the host cell silencing machinery combat the virus.
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