Relevant bibliographies by topics / Protease

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Protease'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 May 2024

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Journal articles on the topic "Protease"

1

Watanabe, Katsuji, and Koichi Hayano. "Source of soil protease in paddy fields." Canadian Journal of Microbiology 39, no. 11 (November 1, 1993): 1035–40. http://dx.doi.org/10.1139/m93-157.

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Properties of soil proteases and proteases from Bacillus spp. obtained from water-logged paddy fields treated with organic manure or chemical fertilizer or not treated with fertilizer were compared to elucidate the sources of soil proteases. The major extractable soil proteases were metal chelator sensitive neutral proteases that were active in hydrolyzing benzyloxycarbonyl-L-phenylalanyl-L-leucine and benzyloxycarbonyl-L-phenylalanyl-L-tyrosyl-L-leucine. In this respect they resembled extracellular proteases from Bacillus subtilis (six isolates), Bacillus cereus (four isolates), and Bacillus mycoides (three isolates) isolated from the same fields. The major extractable soil protease from the manured field was a serine neutral protease that was active in hydrolyzing casein. It resembled an extracellular protease from B. subtilis (eight isolates) isolated from the same field. Extractable soil proteases accounted for 18–96% of the total soil protease in the aforementioned soil. We concluded that a major source of soil protease in water-logged paddy fields is proteolytic Bacillus spp.Key words: soil protease, metal chelator sensitive neutral protease, serine neutral protease, proteolytic Bacillus spp.
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Mallia-Milanes, Brendan, Antoine Dufour, Christopher Philp, Nestor Solis, Theo Klein, Marlies Fischer, Charlotte E. Bolton, Steven Shapiro, Christopher M. Overall, and Simon R. Johnson. "TAILS proteomics reveals dynamic changes in airway proteolysis controlling protease activity and innate immunity during COPD exacerbations." American Journal of Physiology-Lung Cellular and Molecular Physiology 315, no. 6 (December 1, 2018): L1003—L1014. http://dx.doi.org/10.1152/ajplung.00175.2018.

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Dysregulated protease activity is thought to cause parenchymal and airway damage in chronic obstructive pulmonary disease (COPD). Multiple proteases have been implicated in COPD, and identifying their substrates may reveal new disease mechanisms and treatments. However, as proteases interact with many substrates that may be protease inhibitors or proteases themselves, these webs of protease interactions make the wider consequences of therapeutically targeting proteases difficult to predict. We therefore used a systems approach to determine protease substrates and protease activity in COPD airways. Protease substrates were determined by proteomics using the terminal amine isotopic labeling of substrates (TAILS) methodology in paired sputum samples during stable COPD and exacerbations. Protease activity and specific protein degradation in airway samples were assessed using Western blotting, substrate assays, and ex vivo cleavage assays. Two hundred ninety-nine proteins were identified in human COPD sputum, 125 of which were proteolytically processed, including proteases, protease inhibitors, mucins, defensins, and complement and other innate immune proteins. During exacerbations, airway neutrophils and neutrophil proteases increased and more proteins were cleaved, particularly at multiple sites, consistent with degradation and inactivation. During exacerbations, different substrates were processed, including protease inhibitors, mucins, and complement proteins. Exacerbations were associated with increasing airway elastase activity and increased processing of specific elastase substrates, including secretory leukocyte protease inhibitor. Proteolysis regulates multiple processes including elastase activity and innate immune proteins in COPD airways and differs during stable disease and exacerbations. The complexity of protease, inhibitor, and substrate networks makes the effect of protease inhibitors hard to predict which should be used cautiously.
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Kostallas, George, and Patrik Samuelson. "Novel Fluorescence-Assisted Whole-Cell Assay for Engineering and Characterization of Proteases and Their Substrates." Applied and Environmental Microbiology 76, no. 22 (September 17, 2010): 7500–7508. http://dx.doi.org/10.1128/aem.01558-10.

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ABSTRACT We have developed a sensitive and highly efficient whole-cell methodology for quantitative analysis and screening of protease activity in vivo. The method is based on the ability of a genetically encoded protease to rescue a coexpressed short-lived fluorescent substrate reporter from cytoplasmic degradation and thereby confer increased whole-cell fluorescence in proportion to the protease's apparent activity in the Escherichia coli cytoplasm. We demonstrated that this system can reveal differences in the efficiency with which tobacco etch virus (TEV) protease processes different substrate peptides. In addition, when analyzing E. coli cells expressing TEV protease variants that differed in terms of their in vivo solubility, cells containing the most-soluble protease variant exhibited the highest fluorescence intensity. Furthermore, flow cytometry screening allowed for enrichment and subsequent identification of an optimal substrate peptide and protease variant from a large excess of cells expressing suboptimal variants (1:100,000). Two rounds of cell sorting resulted in a 69,000-fold enrichment and a 22,000-fold enrichment of the superior substrate peptide and protease variant, respectively. Our approach presents a new promising path forward for high-throughput substrate profiling of proteases, engineering of novel protease variants with desired properties (e.g., altered substrate specificity and improved solubility and activity), and identification of protease inhibitors.
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Paulin, John P., and Francisco C. Franco. "Modified bis‐tetrahydrofuran inhibitors toward improved binding to HIV‐1 proteases." Vietnam Journal of Chemistry 59, no. 5 (October 2021): 563–79. http://dx.doi.org/10.1002/vjch.202000179.

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AbstractHIV treatment includes inhibiting HIV‐1 protease which is responsible for viral maturation. However, HIV‐1 protease responds to drug treatment by mutation making the protease‐resistant to inhibitors. In this study, binding interactions between bis‐tetrahydrofuran‐derived (bis‐THF) inhibitors and HIV‐1 protease were described by molecular docking. We characterized the binding energies and all the amino acids present during the binding of the bis‐THF derivatives to the wild type HIV‐1 protease and several mutant HIV‐1 proteases. We found that the modifications to the structure of darunavir helped improve its binding to the wild‐type protease. Also, these structures were found to interact with the mutant HIV‐1 proteases better than darunavir. Results showed that compound 4 had the highest binding energy to the wild‐type HIV‐1 protease and the V654/84 mutant, while compound 5 was found to interact greatly with cyclic urea‐based inhibitor‐resistant proteases and the multi‐protease inhibitor‐resistant HIV‐1 protease. The results may help explain how structural modifications to bis‐tetrahydrofuran inhibitors affect their response to wild‐type and resistant HIV‐1 proteases. Furthermore, this study is the first demonstration of the differences in the amino acids interacting with protease inhibitors for wild‐type and mutated HIV‐1 proteases and may help in the design of bis‐THF derivatives as HIV‐1 protease inhibitors.
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Hudig, D., N. J. Allison, T. M. Pickett, U. Winkler, C. M. Kam, and J. C. Powers. "The function of lymphocyte proteases. Inhibition and restoration of granule-mediated lysis with isocoumarin serine protease inhibitors." Journal of Immunology 147, no. 4 (August 15, 1991): 1360–68. http://dx.doi.org/10.4049/jimmunol.147.4.1360.

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Abstract To kill other cells, lymphocytes can exocytose granules that contain serine proteases and pore-forming proteins (perforins). We report that mechanism-based isocoumarin inhibitors inhibited the proteases and inactivated lysis. When inhibited proteases were restored, lysis was also restored, indicating that the proteases were essential for lysis. We found three new lymphocyte protease activities, "Asp-ase,"Met-ase," and "Ser-ase," which in addition to ly-tryptase and ly-chymase, comprise five different protease activities in rat RNK-16 granules. The general serine protease inhibitor 3,4-dichloroisocoumarin (DCI) inhibited all five protease activities. Essentially all protease molecules were inactivated by DCI before lysis was reduced, as determined from DCI's second order inhibition rate constants for the proteases, the DCI concentrations, and the times of pretreatment needed to block lysis. The pH favoring DCI inhibition of lysis was the pH optimum for protease activity. Isocoumarin reagents acylate, and may sometimes secondarily alkylate, serine protease active sites. Granule proteases, inhibited by DCI acylation, were deacylated with hydroxylamine, restoring both the protease and lytic activities. Hydroxylamine does not restore alkylated proteases and did not restore the lytic activities after inhibition with 4-chloro-7-guanidino-3-(2-phenylethoxy)-isocoumarin, a more alkylating mechanism-based inhibitor designed to react with tryptases. It is improbable that isocoumarin reagents directly inactivated pore-forming proteins because 1) these reagents require protease activation, 2) their nonspecific effects are alkylating, and 3) alkylated proteins are not restored by hydroxylamine. We conclude that serine proteases participate in lysis when lysis is mediated by the complete assembly of granule proteins.
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Taggart, Clifford, Marcus A. Mall, Gilles Lalmanach, Didier Cataldo, Andreas Ludwig, Sabina Janciauskiene, Nicole Heath, et al. "Protean proteases: at the cutting edge of lung diseases." European Respiratory Journal 49, no. 2 (February 2017): 1501200. http://dx.doi.org/10.1183/13993003.01200-2015.

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Proteases were traditionally viewed as mere protein-degrading enzymes with a very restricted spectrum of substrates. A major expansion in protease research has uncovered a variety of novel substrates, and it is now evident that proteases are critical pleiotropic actors orchestrating pathophysiological processes. Recent findings evidenced that the net proteolytic activity also relies upon interconnections between different protease and protease inhibitor families in the protease web.In this review, we provide an overview of these novel concepts with a particular focus on pulmonary pathophysiology. We describe the emerging roles of several protease families including cysteine and serine proteases.The complexity of the protease web is exemplified in the light of multidimensional regulation of serine protease activity by matrix metalloproteases through cognate serine protease inhibitor processing. Finally, we will highlight how deregulated protease activity during pulmonary pathogenesis may be exploited for diagnosis/prognosis purposes, and utilised as a therapeutic tool using nanotechnologies.Considering proteases as part of an integrative biology perspective may pave the way for the development of new therapeutic targets to treat pulmonary diseases related to intrinsic protease deregulation.
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Schuhmann, Holger, Ulrike Mogg, and Iwona Adamska. "A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains." Biochemical Journal 435, no. 1 (March 15, 2011): 167–74. http://dx.doi.org/10.1042/bj20101613.

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Deg/HtrA proteases are a large group of ATP-independent serine endoproteases found in almost every organism. Their usual domain arrangement comprises a trypsin-type protease domain and one or more PDZ domains. All Deg/HtrA proteases form homo-oligomers with trimers as the basic unit, where the active protease domain mediates the interaction between individual monomers. Among the members of the Deg/HtrA protease family, the plant protease DEG7 is unique since it contains two protease domains (one active and one degenerated) and four PDZ domains. In the present study, we investigated the oligomerization behaviour of this unusual protease using yeast two-hybrid analysis in vivo and with recombinant protein in vitro. We show that DEG7 forms trimeric complexes, but in contrast with other known Deg/HtrA proteases, it shows a new principle of oligomerization, where trimerization is based on the interactions between degenerated protease domains. We propose that, during evolution, a duplicated active protease domain degenerated and specialized in protein–protein interaction and complex formation.
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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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Karlsson, Anna, Patricia Saravia-Otten, Karin Tegmark, Eva Morfeldt, and Staffan Arvidson. "Decreased Amounts of Cell Wall-Associated Protein A and Fibronectin-Binding Proteins in Staphylococcus aureus sarA Mutants due to Up-Regulation of Extracellular Proteases." Infection and Immunity 69, no. 8 (August 1, 2001): 4742–48. http://dx.doi.org/10.1128/iai.69.8.4742-4748.2001.

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ABSTRACT Data have been presented indicating that Staphylococcus aureus cell surface protein can be degraded by extracellular proteases produced by the same bacterium. We have found that insarA mutant cells, which produce high amounts of four major extracellular proteases (staphylococcal serine protease [V8 protease] [SspA], cysteine protease [SspB], aureolysin [metalloprotease] [Aur], and staphopain [Scp]), the levels of cell-bound fibronectin-binding proteins (FnBPs) and protein A were very low compared to those of wild-type cells, in spite of unaltered or increased transcription of the corresponding genes. Cultivation ofsarA mutant cells in the presence of the global protease inhibitor α2-macroglobulin resulted in a 16-fold increase in cell-bound FnBPs, indicating that extracellular proteases were responsible for the decreased amounts of FnBPs in sarAmutant cells. The protease inhibitor E64 had no effect on the level of FnBPs, indicating that cysteine proteases were not involved. Inactivation of either ssp or aur in the prototype S. aureus strain 8325-4 resulted in a threefold increase in the amount of cell-bound FnBPs. Inactivation of the same protease genes in a sarA mutant of 8325-4 resulted in a 10- to 20-fold increase in cell-bound protein A. As the serine protease requires aureolysin to be activated, it can thus be concluded that the serine protease is the most important protease in the release of cell-bound FnBPs and protein A.
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Greenfield, Lucy M., Paul W. Hill, Eric Paterson, Elizabeth M. Baggs, and Davey L. Jones. "Do plants use root-derived proteases to promote the uptake of soil organic nitrogen?" Plant and Soil 456, no. 1-2 (September 23, 2020): 355–67. http://dx.doi.org/10.1007/s11104-020-04719-6.

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Abstract Aims The capacity of plant roots to directly acquire organic nitrogen (N) in the form of oligopeptides and amino acids from soil is well established. However, plants have poor access to protein, the central reservoir of soil organic N. Our question is: do plants actively secrete proteases to enhance the breakdown of soil protein or are they functionally reliant on soil microorganisms to undertake this role? Methods Growing maize and wheat under sterile hydroponic conditions with and without inorganic N, we measured protease activity on the root surface (root-bound proteases) or exogenously in the solution (free proteases). We compared root protease activities to the rhizosphere microbial community to estimate the ecological significance of root-derived proteases. Results We found little evidence for the secretion of free proteases, with almost all protease activity associated with the root surface. Root protease activity was not stimulated under N deficiency. Our findings suggest that cereal roots contribute one-fifth of rhizosphere protease activity. Conclusions Our results indicate that plant N uptake is only functionally significant when soil protein is in direct contact with root surfaces. The lack of protease upregulation under N deficiency suggests that root protease activity is unrelated to enhanced soil N capture.
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Dissertations / Theses on the topic "Protease"

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Wartchow, Charles Aaron. "Carbohydrate protease conjugates (CPC) : stabilized proteases for peptide synthesis /." The Ohio State University, 1993. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487847309050511.

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De, Veer Simon J. "Development of novel protease inhibitors for epidermal kallikrein proteases." Thesis, Queensland University of Technology, 2014. https://eprints.qut.edu.au/114508/1/Simon_de%20Veer_Thesis.pdf.

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Preserving the integrity of the skin's outermost layer (the epidermis) is vital for humans to thrive in hostile surroundings. Covering the entire body, the epidermis forms a thin but impenetrable cellular cordon that repels external assaults and blocks the escape of water and electrolytes from within. This structure exists in a perpetual state of repair and regeneration where the production of new cellular subunits (keratinocytes) at the base of the epidermis is offset by the gradual release of terminally differentiated corneocytes from the surface. It is increasingly clear that proteinases (hereafter termed proteases) are essential for assembling and maintaining the epidermal barrier. More than thirty proteases are expressed by keratinocytes or immune cells that infiltrate the skin, and the activity of each must be maintained within narrow limits and confined to the correct time and place. Accordingly, dysregulated proteolytic activity is a common factor in a multitude of skin disorders that range in severity from relatively mild to life-threatening. Serine proteases from the kallikrein-related peptidase (KLK) family are widely recognised as key modulators of epidermal barrier function. For several decades, KLK proteases have been regarded as major contributors to the natural shedding of corneocytes from the skin's surface by degrading (corneo)desmosomes in the stratum corneum. Additionally, controlled KLK proteolytic activity influences the step-wise processing of key molecules involved in hydration and acidification (pro-filaggrin), and anti-microbial defence (cathelicidins). Further, KLK proteases have prominent roles in the response to barrier disruption that involve stimulating inflammation and alerting the immune system. Thus, failure to properly control KLK proteolytic activity represents a significant threat to epidermal barrier function, as seen in a spectrum of skin disorders, including Netherton syndrome and atopic dermatitis. The focus of this study was to develop novel inhibitors for three KLK proteases with the strongest links to epidermal (patho)physiology (KLK5, KLK7 and KLK14) by engineering the naturally occurring cyclic peptide, sunflower trypsin inhibitor-1 (SFTI-1). Initially, each target protease was screened against a dedicated library of individually synthesised peptide substrates (sparse matrix library) to identify sequence combinations that bound to the active site with high affinity. This approach yielded a series of efficient tetrapeptide substrates for each protease that outperformed existing substrates from conventional screening methods, such as positional scanning and phage display. Strikingly, the optimal substrates for KLK5, KLK7 and KLK14 each displayed a unique physicochemical signature, indicating that the active site of each protease was configured to recognise distinct cleavage motifs. This phenomenon was explored in more detail by analysing structures of diverse serine proteases from the S1A (chymo)trypsin fold, which identified several points of high sequence variation in the active site cleft that likely contribute to divergent cleavage site specificities. Subsequently, favoured cleavage sequences for KLK5, KLK7 and KLK14 were substituted into the contact β-strand of SFTI-1 to generate inhibitor variants with improved affinity and selectivity. Whereas most inhibitor design strategies based on Laskowski inhibitors (including SFTI-1) focus mainly on optimising the interaction between protease and inhibitor, this study paired binding loop modifications with a second step that aimed to refine the intramolecular hydrogen bond network, as shown recently for engineered SFTI variants targeting KLK4. Like the previous study, improving the tendency for an inhibitor to form intramolecular hydrogen bonds generally led to improvements in inhibitory activity. However, it was also evident that certain hydrogen bonds were detrimental, revealing that the quantity of hydrogen bonds should not be the only criteria during this screening process. Additionally, the iterative optimisation of inhibitors for KLK5 highlighted the need to consider both sides of the reactive site when engineering Laskowski inhibitors as generating a selective KLK5 variant was dependent on substituting the P2′ residue. Using this design process, it was possible to successfully re-direct the inhibitory activity of SFTI-1 to three separate protease targets that showed varying affinity for the wild-type inhibitor. To delve further into the Laskowski mechanism, SFTI-1 was used as a model system to explore the molecular basis for Laskowski inhibitor potency and specificity. Here, inhibitor association and dissociation kinetics were characterised for a series of variants with different binding sequences and hydrogen bond tendencies. These analyses revealed that the primary determinant for rapid association was the pre-organised conformation of the inhibitor binding loop rather than its sequence, whereas coordinated inter- and intramolecular interactions promoted efficient religation and slow dissociation. As the conformation of the binding loop is conserved, inhibitor selectivity dictated by the binding sequence was found to arise from modulating the off-rate. Performing additional analyses on eight fold-divergent inhibitor families revealed that these concepts were generally applicable to Laskowski inhibitors, providing broad new insights on protease inhibitor function and design. These findings were subsequently applied to engineer an additional series of potent inhibitors with broad-range activity. Finally, the substrates and inhibitors developed for KLK5, KLK7 and KLK14 were used in biological assays to investigate the activity and significance of each target protease in healthy and diseased skin. KLK peptide substrates were applied to profile KLK hyperactivity in skin extracts from transgenic KLK5 mice and Spink5-/- mice. Additionally, KLK inhibitors were used to sequentially block different KLKs in gel-based and in situ zymography experiments. Selective and broad-range inhibitors were also evaluated in ex vivo desquamation assays to examine the relative importance of KLK5, KLK7 and KLK14 during corneocyte shedding, which revealed a major role for KLK7. Collectively, these findings shed light on the individual contributions of KLK proteases to maintaining the epidermal barrier and identify a series of therapeutic leads for further development as novel treatments for skin disorders associated with dysregulated KLK proteolytic activity.
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Josh, R. S. "Tailoring potent plant protease inhibitor against helicoverpa armigera proteases." Thesis(Ph.D.), CSIR-National Chemical Laboratory, Pune, 2014. http://dspace.ncl.res.in:8080/xmlui/handle/20.500.12252/1969.

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Hamill, J. A. "Involvement of proteases and protease inhibitors in potato late blight." Thesis, Queen's University Belfast, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.426731.

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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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Lourbakos, Afrodite 1972. "Activation of human protease-activated receptors by proteases from a periodontal pathogen." Monash University, Dept. of Biochemistry and Molecular Biology, 2001. http://arrow.monash.edu.au/hdl/1959.1/8876.

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Deo, Shivdeep. "DETECTION OF SECRETED PROTEASES AND A MEMBRANE PROTEASE IN PATHOGENIC ACANTHAMOEBA CULBERTSONI." VCU Scholars Compass, 2011. http://scholarscompass.vcu.edu/etd/256.

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Acanthamoeba culbertsoni (A. culbertsoni) is an amphizoic amoeba that is the causative agent of Granulomatous Amoebic Encephalitis (GAE), an often fatal central nervous system infection that is seen most frequently in severely immunocompromised patients and is characterized by hemorrhagic and necrotic lesions of the brain as well as varying degrees of granuloma formation. A.culbertsoni isolates have also been identified in a few cases of Amoebic Keratitis, a painful, sight-threatening corneal infection that disproportionately affects contact lens users irrespective of immune status. Common features of both infections include amoebic interaction with host extracellular matrix (ECM) components as requisites for both attachment to, and subsequent invasion of, host tissues to facilitate disease establishment. Previous studies have demonstrated that pathogenic species of Acanthamoeba , such as A.culbertsoni, bind to the ECM proteins Laminin-1 and Collagen I to a greater extent than non-pathogenic species. It has also been documented in the literature that secreted Acanthamoeba proteases have the ability to degrade components of the extracellular matrix. The role of amoebic proteases in mediating the attachment and invasion processes is not entirely understood. Initial experiments conducted in the present study revealed secretion of approximately 150 and 55-kDa serine proteases during attachment as well as invasion of the ECM by A. culbertsoni. However, inhibition of these serine proteases using phenylmethylsulfonyl fluoride (PMSF) did not diminish the ability of amoebae to attach or invade. It was demonstrated that secretion of the observed proteases occurred in a constitutive rather than substrate-induced manner and that amoebae secrete these proteases under a number of different conditions. Additionally, a 140-kDa membrane-associated serine protease was identified which may prove to play a role in focal proteolytic degradation. Collectively, our results suggest that attachment to extracellular matrix components is mediated through non-protease-dependent mechanisms. We also suggest that ECM invasion by A.culbertsoni is predominately a mechanical process that may be supplemented or enhanced by focal proteolytic degradation of extracellular matrix components by membrane-associated proteases.
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Groll, Michael. "Strukturelle und funktionelle Zusammenhänge und Unterschiede archaebakterieller und eukaryontischer 20S-Proteasome." Doctoral thesis, Humboldt-Universität zu Berlin, Medizinische Fakultät - Universitätsklinikum Charité, 2005. http://dx.doi.org/10.18452/13957.

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In eukaryotes protein degradation is performed by the ubiquitin-proteasome system. The 26S proteasome, a 2.5MDa large multimeric molecular machine, consists of more than 30 subunits and represents the core component of this proteolytic pathway. The complex is assembled from a proteolytically active 20S proteasome and two 19S regulator cap complexes. So far crystal structure, topology and enzymatic mechanism have only been elucidated for the 20S proteasome core particle (CP). CPs are assembled from four stacked rings of seven subunits each, following an alpha7beta7beta7alpha7-stochiometry. The strict established order of the proteasomal assembly and maturation is essential to prevent uncontrolled and premature protein degradation in the cell. CPs belong to the class of Ntn-hydrolases. Peptide hydrolysis is performed inside a central cavity at the active sites of the beta-type subunits, with Ogam of the hydroxyl group of the N-terminal threonine acting as the nucleophile. Release of the proteolytically active threonine through N-O-Acetyl rearrangement is the last step of the proteasomal assembly. Compartmentalisation of CPs is an important way to regulate substrate access to the central cavity as well as release of the generated oligopeptides. The activity of eukaryotic CPs are controlled by an unique mechanism: docking of regulatory complexes, like Blm3, PA28 or 19S, causes a conformational change of the N-terminal residues of the latent alpha-subunits, resulting in an activation of the proteolytically active sites. Archaebacterial CPs lack such regulatory gating mechanism. The controlled degradation of proteins by the proteasome dominates a variety of biological essential processes, like metabolic adaptation, apoptosis, inflammation, immune and stress response, as well as cell proliferation and cell differentiation. Selective and specific natural and synthetic inhibitors of CPs might find their practical application in treatment of cancer or inflammatory diseases.
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Fishovitz, Jennifer. "A Chemical Approach to Distinguish ATP-dependent Proteases." Case Western Reserve University School of Graduate Studies / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=case1291142553.

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Tiew, Kok-Chuan. "Dengue virus protease inhibitors." Thesis, Wichita State University, 2011. http://hdl.handle.net/10057/6117.

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Dengue virus (DENV) is a major health threat that affects 2.5 billion people, or 40% of the world’s population. However, there are no approved antiviral drugs or vaccines to treat Dengue infection. This thesis describes the design, synthesis and discovery of a new class of inhibitors of DENV NS3 protease. Structure-activity relationship studies have been carried out in order to delineate the structural elements responsible for the activity of this series of compounds. A lead compound suitable for further development has been identified.
Thesis (M.S.)--Wichita State University, College of Liberal Arts and Sciences, Dept. of Chemistry.
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Books on the topic "Protease"

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Cheronis, J. C., and J. E. Repine, eds. Proteases, Protease Inhibitors and Protease-Derived Peptides. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0.

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Cheronis, John Chris Dion, 1951- and Repine John E, eds. Proteases, protease inhibitors, and protease-derived peptides: Importance in human pathophysiology and therapeutics. Basel: Birkhäuser Verlag, 1993.

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Lendeckel, Uwe, and Nigel M. Hooper, eds. Viral Proteases and Antiviral Protease Inhibitor Therapy. Dordrecht: Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-2348-3.

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1926-, Katunuma Nobuhiko, ed. Medical aspects of proteases and protease inhibitors. Amsterdam: IOS Press, 1997.

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B, Banner Carl D., and Nixon Ralph A, eds. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York, N.Y: New York Academy of Sciences, 1992.

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A, Nixon Ralph, Banner Carl D. B, and New York Academy of Sciences., eds. Proteases and protease inhibitors in Alzheimer's disease pathogenesis. New York: NewYork Academy of Sciences, 1992.

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Polgár, László. Mechanisms of protease action. Boca Raton, Fla: CRC Press, 1989.

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Chang, Henry E. HIV protease inhibitor report. 2nd ed. Brooklyn, NY (72 Orange St., #3C, Brooklyn 11201): National AIDS Treatment Advocacy Project, 1996.

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Franke, Lars. Von der Protease zur Peptidsynthase. Wiesbaden: Springer Fachmedien Wiesbaden, 2020. http://dx.doi.org/10.1007/978-3-658-30437-9.

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1953-, Ogden Richard C., and Flexner Charles W. 1956-, eds. Protease inhibitors in AIDS therapy. New York: Marcel Dekker, 2001.

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Book chapters on the topic "Protease"

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Powers, James C., Shinjiro Odake, Jozef Oleksyszyn, Hitoshi Hori, Toshihisa Ueda, Bogdan Boduszek, and Chih-Min Kam. "Proteases—Structures, Mechanism and Inhibitors." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 3–18. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_1.

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Steffens, Gerd J., Regina Heinzel-Wieland, Derek Saunders, Bernd Wolf, Arjan Rudolphus, Jan Stolk, Johannes A. Krarnps, and Joop A. Dijkman. "Oxidation Resistant Muteins of Antileukoproteinase as Potential Therapeutic Agents." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 111–21. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_10.

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Colman, Robert W. "Factor XII Activation and Inhibition in Inflammation." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 125–43. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_11.

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Stewart, John M. "The Kinin System in Inflammation." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 145–57. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_12.

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Maeda, Hiroshi, Takaaki Akaike, Yoshifumi Sakata, and Keishi Maruo. "Role of Bradykinin in Microbial Infection: Enhancement of Septicemia by Microbial Proteases and Kinin." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 159–65. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_13.

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Whalley, E. T., and J. C. Cheronis. "Kinin Antagonists as Human Therapeutics." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 167–76. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_14.

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Niedbala, Michael J. "Cytokine Regulation of Endothelial Cell Extracellular Proteolysis." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 179–93. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_15.

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Katunuma, Nobuhiko, Hisao Kakegawa, Yoichi Matsunaga, Takeshi Nikawa, and Eiki Korninami. "Different Functional Share of Individual Lysosomal Cathepsins in Normal and Pathological Conditions." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 195–210. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_16.

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Stewart, John M., and Michael E. Hall. "Neuropeptide Processing in Pathophysiology." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 211–26. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_17.

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Aimes, Ronald T., Sheila M. Nielsen-Preiss, and James P. Quigley. "Resolution of Timp-Free and Timp-Complexed 70kDa Progelatinase from Culture Medium of Rous Sarcoma Virus-Transformed Chicken Embryo Fibroblasts." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 227–43. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_18.

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Conference papers on the topic "Protease"

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David, Ioan, Ariana Velciov, and Gabriel Bujanca. "THE USE OF BIOENZYMATIC INDICATORS LIKE PROTEASE AND ASPARAGINASE ENZYMES ON BISCUIT PRODUCTS." In 23rd SGEM International Multidisciplinary Scientific GeoConference 2023. STEF92 Technology, 2023. http://dx.doi.org/10.5593/sgem2023v/6.2/s25.55.

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This article presents the rheological study of protease and asparaginase enzymes on dough obtained from white flour used for biscuits. Using alveographic method and falling number method we were able to determine the rheological characteristics of the dough used for biscuits and monitor the effects in the flour and finished products of protease and asparaginase enzymes taking into account different dosages. The technological process of preparing biscuits and crackers using protease and asparaginase becomes more healthy and efficient due to improvements in dough handling, volume and texture of the biscuits. Proteases catalyze the hydrolysis reaction of the peptide bond in the protein between the amino compound of one amino acid and the carboxyl compound of the next amino acid. This leads to the weakening of the gluten structure in the dough. Asparaginase catalyzes the conversion of asparagine and water to aspartic acid and ammonia. This conversion prevents the formation of acrylamide. The falling number and alveograph tests provide results which show that addition of protease and asparaginase to the dough improves the qualities of the finished product, the biscuits being crispier, more porous (they easily melt in the mouth) and more tender. Proteases increase the viscosity of the dough and decrease its stability and tolerance to kneading.
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Delucchi, DM, AS Benton, and RJ Freishtat. "Protease/Anti-Protease Functional Group Evaluation in Lung Disease." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5426.

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Tanabe, Naoya, Atsuyasu Sato, Tatsushi Mizutani, Yoko Hamakawa, Kiyoshi Uemasu, Susumu Sato, Shigeo Muro, and Toyohiro Hirai. "Protease anti-protease imbalance and small airways disease in COPD." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa4256.

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Tilman, Jessica, Amy Day, Natasha Madge, Peter Barnes, and Louise Donnelly. "Macrophage phenotype does not affect protease anti-protease imbalance in COPD." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa880.

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Mcelvaney, O. F., T. Asakura, S. Meinig, J. L. Torres-Castillo, R. S. Hagan, C. Gabillard, M. P. Murphy, et al. "Protease-Anti-Protease Compartmentalization in SARS-CoV-2 ARDS: Therapeutic Implications." In American Thoracic Society 2022 International Conference, May 13-18, 2022 - San Francisco, CA. American Thoracic Society, 2022. http://dx.doi.org/10.1164/ajrccm-conference.2022.205.1_meetingabstracts.a3629.

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Dickson, Eva F., Rebecca L. Goyan, James C. Kennedy, M. Mackay, M. A. K. Mendes, and Roy H. Pottier. "Protease-mediated drug delivery." In Applications of Photonic Technology, edited by Roger A. Lessard and George A. Lampropoulos. SPIE, 2003. http://dx.doi.org/10.1117/12.543446.

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Abdullah, Muhammad, Seher Ansar Khawaja, and Muhammad Farooq. "HIV-1 Protease Cleavages." In 2021 International Conference on Innovative Computing (ICIC). IEEE, 2021. http://dx.doi.org/10.1109/icic53490.2021.9692978.

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Satog˘lu Dog˘an, M. Yu¨sra, Andrey Revyakin, Sang Park, Alexandros Pertsinidis, Christopher Brown, Steven Chu, Charles S. Craik, and Arun Majumdar. "A New Platform for Profiling Active Proteases With Single-Molecule Sensitivity." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13383.

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Proteases, such as urokinase plasminogen activator (uPA) and prostate specific antigen (PSA), have been used extensively as biomarkers for cancer. A necessary improvement in diagnostics with proteomics is to use the activity levels of proteases as a signal, as opposed to the total protease content. This will provide a better functional insight into the propagation of cancer, and ultimately could allow us to diagnose cancer at earlier stages. Here, we propose a new platform to capture and measure activity of specific proteases in patient samples, with single-molecule sensitivity.
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McCafferty, Darragh, Kelly Moffitt, and Timothy Ferguson. "Development of the first protease multiplex immunoassay for active neutrophilic serine protease biomarkers." In ERS International Congress 2021 abstracts. European Respiratory Society, 2021. http://dx.doi.org/10.1183/13993003.congress-2021.pa1143.

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Barbosa, Karen Eduarda, and Jorge Alexandre Nogueira Santos. "ANÁLISE DO PAPEL DA ENZIMA HIV- 1 PROTEASE NO CICLO REPLICATIVO DO HIV." In I Congresso Nacional de Microbiologia Clínica On-Line. Revista Multidisciplinar em Saúde, 2021. http://dx.doi.org/10.51161/rems/1197.

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Introdução: De acordo com os dados do boletim epidemiológico do Ministério da Saúde (2020), foram notificados 342.459 casos de infecção pelo vírus HIV no Brasil, entre os períodos de junho de 2007 a junho de 2020, demonstrando uma grande incidência da doença no país. Responsável pela depleção de linfócitos TDC4 +, o tratamento disponível consiste na terapia antirretroviral (HAART), baseada em inibidores de proteases entre os quais destaca-se a HIV-1 protease. Essa enzima é responsável pelo desenvolvimento do vírus, se constituindo num importante alvo farmacológico para o tratamento da AIDS. Objetivos: Nesse contexto, esse trabalho fará uma análise do papel da HIV-1 protease no ciclo de replicação do HIV. Materiais e Métodos: O presente trabalho tratou-se de um estudo descritivo que fez uso da base de dados do portal PUBMED, por meio da combinação das seguintes palavras chaves: HIV-1 protease, replication e AIDS. Filtrados os resultados de 2017 a 2021, obteve-se um total de 13 artigos para a recuperação dos dados. Resultados: O capsídeo viral possui as enzimas virais integrase, transcriptase reversa e proteases associadas ao genoma. A HIV-1 protease é um homodímero formado por 2 monômeros com 99 resíduos cada, e com o sítio formado pela tríade: Asp-25, Thr-26 e Gli-27. Localizada acima do sítio ativo da enzima, há a região flat que se abre para a entrada do substrato e também se fecha sobre ela quando complexada à substância. Ressalta-se que essa região também é importante para garantir a estabilidade da enzima. A clivagem das poliproteínas gag e pol, responsáveis pela formação das proteínas estruturais do vírus, ocorre quando dois resíduos de aspartato ligam-se a uma molécula de água e promovem a hidrólise do substrato. Tal clivagem permite um rearranjo das cadeias que agora se tornam funcionais e originam partículas infecciosas que poderão ser liberadas no citoplasma e progredir com a infecção. Conclusões: Essa enzima é relevante para o entendimento do ciclo replicativo do HIV, uma vez que se relaciona com a produção de proteínas virais funcionais. Sua inibição dá origem a partículas virais imaturas e por isso a enzima se constitui em um dos alvos para inibição.
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Reports on the topic "Protease"

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Smith, Jeffrey W. Protease Profiling in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada430267.

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Smith, Jeffrey W. Protease Profiling in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2003. http://dx.doi.org/10.21236/ada416743.

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Tung, Ching-Hsuan. Protease Mediated Anti-Cancer Therapy. Fort Belvoir, VA: Defense Technical Information Center, August 2006. http://dx.doi.org/10.21236/ada458446.

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Adam, Zach, and Eran Pichersky. Degradation of Abnormal Proteins in Chloroplasts of Higher Plants. United States Department of Agriculture, August 1994. http://dx.doi.org/10.32747/1994.7568768.bard.

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In this study we attempted to get a better understanding of processes involved in the degradation of abnormal proteins i chloroplasts. To achieve this goal, we used a number of complementary approaches. We first characterized the expression of the two subunits of Clp protease. We demonstrated that both of them were expressed in chloroplasts in a constitutive fashion, but the expression of the regulatory subunit ClpC was enhanced by light. We generated a mutant the lumenal protein OEE33 which was targeted to the stroma in in vitro experiments. In the wrong compartment it was found unstable, and characterization of its degradation revealed that it was degraded by a soluble, ATP-dependent serine protease, which are also the characteristics of Clp protease. In search of other homologues of bacterial proteases, we found that chloroplasts contain a homologue of the FtsH protease. It is an ATP-dependent metallo-protease, bound to the stromal side of the thylakoid membrane, whose expression is dependent on light. The gene encodig this protease was cloned and characterized. In attempt to generate Arabidopsis mutant plants impaired in their capability to degrade abnormal chloroplast proteins, we fused the gene for mistargeted OEE33 to the streptomycin-detoxifying gene. This chimeric gene was introduced into Arabodipsis plants, to generate transformed plants. This transformants plants were sensitive to streptomycin due to the rapid turn-over of the chimeric protein. Seeds from these plants were then chemically mutagenised, and seedlings were selected for their capability to grow on streptomycin. The ability of these mutant transformants to grow on streptomycin is presumably due to stabilization of the chimeric protein. These plants will allow us in the future to identify the effected genes, which are likely to be involved in the protein degradation process.
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Chen, Emily. Diagnosing Breast Cancer Using Protease Fingerprint. Fort Belvoir, VA: Defense Technical Information Center, June 2000. http://dx.doi.org/10.21236/ada383309.

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Rogers, J. (Processing and targeting of the thiol protease aleurain). Office of Scientific and Technical Information (OSTI), January 1990. http://dx.doi.org/10.2172/6995327.

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Rogers, J. C. [Processing and targeting of the thiol protease aleurain]. Office of Scientific and Technical Information (OSTI), January 1993. http://dx.doi.org/10.2172/6619862.

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Barkan, Alice, and Zach Adam. The Role of Proteases in Regulating Gene Expression and Assembly Processes in the Chloroplast. United States Department of Agriculture, January 2003. http://dx.doi.org/10.32747/2003.7695852.bard.

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Chloroplasts house many biochemical processes that are essential for plant viability. Foremost, among these is photosynthesis, which requires the protein-rich thylakoid membrane system. The activation of chloroplast genes encoding thylakoid membrane proteins and the targeting and assembly of these proteins together with their nuclear-encoded partners are essential for the elaboration of the thylakoid membrane. Several nuclear-encoded proteins that regulate chloroplast gene expression and that mediate the targeting of proteins to the thylakoid membrane have been identified in recent years, and many more remain to be discovered. The abundance of such proteins is critical and is likely to be determined to a significant extent by their stability, which in turn, is influenced by chloroplast protease activities. The primary goal of this project was to link specific proteases to specific substrates, and in particular, to specific regulatory and assembly proteins. We proposed a two-pronged approach, involving genetic analysis of the consequences of the mutational loss of chloroplast proteases, and biochemical analysis of the degradation pathways of specific proteins that have been shown to control chloroplast gene expression. Our initial bioinformatic analysis of chloroplast proteases allowed us to identify the set of pro teases that is targeted to the chloroplast. We used that information to recover three Arabidopsis mutants with T - DNA insertions in specific chloroplast protease genes. We carried out the first analysis of the stability of a regulator of chloroplast gene expression (CRS2), and found that the protein is much less stable than are typical components of the photosynthetic apparatus. Genetic reagents and analytical methods were developed that have set the stage for a rapid advancement of our understanding of chloroplast proteolysis. The results obtained may be useful for manipulating the expression of transgenes in the chloroplast and for engineering plants whose photosynthetic activity is optimized under harsh environmental conditions.
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Liu, Cheng. Synergism of Selective Tumor Vascular Thrombosis and Protease Activated Prodrug. Fort Belvoir, VA: Defense Technical Information Center, May 2008. http://dx.doi.org/10.21236/ada494207.

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Rogers, J. C. [Processing and targeting of the thiol protease aleurain]. Progress report. Office of Scientific and Technical Information (OSTI), April 1993. http://dx.doi.org/10.2172/10139404.

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