Academic literature on the topic 'Cathepsin proteases'
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Journal articles on the topic "Cathepsin proteases"
Munger, J. S., C. Haass, C. A. Lemere, G. P. Shi, W. S. F. Wong, D. B. Teplow, D. J. Selkoe, and H. A. Chapman. "Lysosomal processing of amyloid precursor protein to Aβ peptides: a distinct role for cathepsin S." Biochemical Journal 311, no. 1 (October 1, 1995): 299–305. http://dx.doi.org/10.1042/bj3110299.
Full textJane, Derek T., and Michael J. Dufresne. "Expression and regulation of three lysosomal cysteine protease activities during growth of a differentiating L6 rat myoblast cell line and its nonfusing variant." Biochemistry and Cell Biology 72, no. 7-8 (July 1, 1994): 267–74. http://dx.doi.org/10.1139/o94-038.
Full textShi, Guo-Ping, Rebecca A. R. Bryant, Richard Riese, Steven Verhelst, Christoph Driessen, Zhenqiang Li, Dieter Bromme, Hidde L. Ploegh, and Harold A. Chapman. "Role for Cathepsin F in Invariant Chain Processing and Major Histocompatibility Complex Class II Peptide Loading by Macrophages." Journal of Experimental Medicine 191, no. 7 (April 3, 2000): 1177–86. http://dx.doi.org/10.1084/jem.191.7.1177.
Full textSloan, Sarah, Caitlin Jenvey, Callum Cairns, and Michael Stear. "Cathepsin F of Teladorsagia circumcincta is a recently evolved cysteine protease." Evolutionary Bioinformatics 16 (January 2020): 117693432096252. http://dx.doi.org/10.1177/1176934320962521.
Full textFerrall-Fairbanks, Meghan C., Chris A. Kieslich, and Manu O. Platt. "Reassessing enzyme kinetics: Considering protease-as-substrate interactions in proteolytic networks." Proceedings of the National Academy of Sciences 117, no. 6 (January 24, 2020): 3307–18. http://dx.doi.org/10.1073/pnas.1912207117.
Full textJames, Ian E., Robert W. Marquis, Simon M. Blake, Shing Mei Hwang, Catherine J. Gress, Yu Ru, Denise Zembryki, et al. "Potent and Selective Cathepsin L Inhibitors Do Not Inhibit Human Osteoclast Resorptionin Vitro." Journal of Biological Chemistry 276, no. 15 (January 8, 2001): 11507–11. http://dx.doi.org/10.1074/jbc.m010684200.
Full textMASON, Robert W., Carolyn A. BERGMAN, Guizhen LU, Jennifer FRENCK HOLBROOK, and Katia SOL-CHURCH. "Expression and characterization of cathepsin P." Biochemical Journal 378, no. 2 (March 1, 2004): 657–63. http://dx.doi.org/10.1042/bj20031548.
Full textBevec, T., V. Stoka, G. Pungercic, I. Dolenc, and V. Turk. "Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L." Journal of Experimental Medicine 183, no. 4 (April 1, 1996): 1331–38. http://dx.doi.org/10.1084/jem.183.4.1331.
Full textDurán-Pérez, Sergio Alonso, Héctor Samuel López-Moreno, Maribel Jiménez-Edeza, Jesús Ricardo Parra-Unda, Edgar Rangel-López, and José Guadalupe Rendón-Maldonado. "Upregulation of Cathepsin B-like Protease Activity During Apoptosis inGiardia duodenalis." Current Proteomics 16, no. 4 (April 25, 2019): 330–37. http://dx.doi.org/10.2174/1570164616666190204112452.
Full textPlatt, Manu O., Randall F. Ankeny, Guo-Ping Shi, Daiana Weiss, J. D. Vega, W. R. Taylor, and Hanjoong Jo. "Expression of cathepsin K is regulated by shear stress in cultured endothelial cells and is increased in endothelium in human atherosclerosis." American Journal of Physiology-Heart and Circulatory Physiology 292, no. 3 (March 2007): H1479—H1486. http://dx.doi.org/10.1152/ajpheart.00954.2006.
Full textDissertations / Theses on the topic "Cathepsin proteases"
Gewies, Andreas. "Investigation of the ubiquitin-specific protease UBP41 and of the lysosomal cysteine proteases cathepsin-L and cathepsin-B as potential mediators of proapoptotic signalling." Diss., lmu, 2004. http://nbn-resolving.de/urn:nbn:de:bvb:19-16836.
Full textNorbury, Luke James, and s9806495@student rmit edu au. "Structure, Function and Evolutionary Studies of Fasciola Cathepsin L-like Proteases." RMIT University. Applied Science, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081204.160915.
Full textCarrière, Julie. "Characterization of oxyanion hole mutants of the cysteine proteases papain and cathepsin B." Thesis, McGill University, 1992. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=61324.
Full textLockhart, Brent E. "Expression, Purification, and Characterization of the Mast Cell Proteases Chymase and Cathepsin G." Digital Commons @ East Tennessee State University, 2008. https://dc.etsu.edu/etd/1922.
Full textZarella, Bruno Lara. "Papel das proteases na erosão dentinária." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/25/25149/tde-22062017-201442/.
Full textIn the dentine, the demineralized organic matrix has a protector part against the following erosive challenges. Nevertheless, this layer can be degraded by proteases, like the matrix metalloproteinases (MMPS) and cystein cathepsins (CCs). Recently, the use of proteases of the matrix´s inhibitors, emerged as an important preventive tool against the dentinária erosion. However, the exact mechanisms from which the inhibitors of the proteases may prevent the dentin erosion, as much as the kinds of proteases more involved in this process are not completely known yet. Therefore, the general objective of this project was to investigate the part of the two main proteases of the matrix (MMPs and CCs) in the dental erosion. The project was developed in 2 subprojects, with the following objectives: A)Subproject 1: Evaluate the part of the proteases in the progression of the dental erosion; B)subproject 2: To test the NaF inhibitory potencial in the dentin CCs. To accomplish these objectives, human third molar dentin were used for the preparation of the specimens, obtained in the surgery and urgency clinics of FOB-USP (subproject 1) or granted by the University of Oulu (subproject 2). A) Subproject 1: Dentine blocks 4 X 4 X 2 mm) (n=119) were obtained from the roots of the obtained teeth. The specimens were divided in 7 groups according with their treatment. Gels containing inhibitors (E-64, specific cathepsin B inhibitor II, chlorhexidine, galardin NaF, placebo), or without treatment, were produced, applied only one time over the surface and made the erosive challenge (90s, 4x a day for 5 days) and made profilometric analysis. The specimens were incubated in a solution containing collagenase of Clostridium histolyticum type VII for 96 hours and then a second profilometric analysis was made to determine the thickness of the MOD. Two specimens were separated for the electronic microscopy scan analysis. B) Subproject 2: Dentine sticks (6 mm X 2 mm X 1 mm) (n=60) were cut from the medium coronary portion of the teeth and completely demineralized by immersion in EDTA 0,5 M (pH7,4) ifor 30 days and washed in deionized water under constant agitation in 4º C for 72 hours. The specimens were divided in 6 groups (divided by inhibitors: E-64, NaF and negative control, pH 5,5 or 7,2) and incubated in artificial saliva containing their respective inhibitors for 24 hours, 7 days and 21 days; by the end of each period, the specimens were weighted to evaluate the loss of mass and analised the presence of CTX. A)Subproject 1: the loss of demineralized tissue (m, média± SD) was : CHX 8,4±1,7b, Gala 8,6±1,9b, IECB 9,6±1,4a, E64 9,9±1,3a, NaF 9,9±1,7a, P 10,9±2,2a, ST 11,0±1,5a. The loss of demineralized tissue was: CHX 15,4±2,2b, Gala 16,0±1,8b, IECB 17,6±2,4a, E64 17,6±2,0a, NaF 17,3±2,8a, P 19,1±2,1a, ST 18,9±2,4a. The MMP inhibitors reduced significantly the loss of organic matrix and demineralized tissue in comparison with other groups (p<0,05). There was no significant difference found between the thickness of the remaining demineralized organic matrix.(p=0,845). B)Subproject: In the loss of mass, there was a significant difference in relation to the inhibitor (F=20,047, p<0,0001) and incubation time (F=222,462, p<0,0001) with significant interaction between these criteria, in the periods of lesser time of incubation, the loss was similar for all the tested groups, in the period of higher time of incubation, the group containing NaF demonstrated the best results. In the analysis of CTX, there was significant difference in relation the inhibitors (F46,543, p<0,0001), pH (F=14,836, p<0,0004) and time of incubation (F=161,438, p<0,0001)with significant interaction between these criteria, as occurred in the mass loss, there was no statistic difference in the period of lesser incubation. In the period of higher time of incubation, once again, the NaF group demonstrated the best results. The CTX accumulated value, the E64 groups and negative control had the greater accumulated values of CTX, the NaF group, regardlessof the pH, demonstrated significant reduction in relation to the other groups. After the analysisof the results of both subprojects, we can indicate that the MMPs are the proteases of greater importance in the progression of the dentin erosion, thus, its inhibition is of graeter importance for the reduction of this pathology. Even the CCs don´t playing the part directly for the progression of erosion, they are effective in the cascade of the activation of other proteases, like the MMPs themselves. In this manner, its inhibition can also be important for the indirect reduction of the progression of the erosion. In this present study, we can prove that the NaF has inhibiting potential over the dentin CCs, thus, suggesting a new inhibitor of CCs. With the results of this study, we can affirm that the MMPs are the main proteases in the progression of the dentin erosion and that the NaF has inhibiting potential in the dentin CCs.
Boscariol, Rya. "Studies on ovine CD4 : genomic sequence analysis and protein cleavage studies with cathepsin proteases." Thesis, McGill University, 2004. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=81601.
Full textOvine CD4 is also of interest to us as a target of F. hepatica cathepsin L activity. Here we confirm a recently reported ovine CD4 cDNA sequence and the existence of a single nucleotide polymorphism (T/C) within this sequence. The polymorphism translates to a serine-proline switch near the hinge region of the protein. Additionally, we have found that this polymorphism is also present in genomic DNA, suggesting that two alleles of CD4 exist in the ovine genome.
Jayaraj, Ramamoorthi, and Jayaraj@menzies edu au. "Expression of stage-specific Fasciola proteases and their evaluation in vaccination trials." RMIT University. Applied Science, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081029.100156.
Full textFlorence, William C. "Increased stability of class II MHC-peptide complexes in macrophages infected with Mycobacterium avium and the examination of a novel role for Cathepsin L in the innate immune response to Francisella Novicida infection." The Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=osu1173298339.
Full textMauricio, Anna Theresa. "Heterocyclic alpha-aminoalkylphosphonate diphenyl esters as inhibitors of serine proteases : Part II: Basic alpha-aminoalkylphosphonate diphenyl esters as inhibitors of cathepsin G." Diss., Georgia Institute of Technology, 1996. http://hdl.handle.net/1853/27157.
Full textHooshdaran, Bahman. "DUAL INHIBITION OF CATHEPSIN G AND CHYMASE AFTER ISCHEMIA REPERFUSION: THE ROLE OF INFLAMMATORY SERINE PROTEASES IN ISCHEMIA REPERFUSION INJURY." Diss., Temple University Libraries, 2017. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/475423.
Full textPh.D.
Acute myocardial infarction (AMI) is a leading cause of morbidity and mortality in the world (4). Restoration of coronary flow to the ischemic myocardium by interventions such as angioplasty, thrombolytic treatment or coronary bypass surgery is the current standard therapy for AMI (5). However, reperfusion of the ischemic myocardium may result in paradoxical cardiomyocyte dysfunction and worsen tissue damage, in a process known as “reperfusion injury” (6). Ischemic reperfusion (IR) injury may intensify pathological processes that contribute to the generation of oxyradicals, disturbances in cation homeostasis, and depletion of cellular energy stores, which may elicit arrhythmias, contractile dysfunction, and ultrastructural damage of the myocardium. These changes can lead to heart failure and ultimately sudden death. The exact mechanisms of IR injury are not fully known (7). Molecular, cellular, and tissue alterations such as cell death, inflammation, neurohumoral activation, and oxidat
Temple University--Theses
Book chapters on the topic "Cathepsin proteases"
Yamamoto, Kenji. "Cathepsin E and cathepsin D." In Proteases New Perspectives, 59–71. Basel: Birkhäuser Basel, 1999. http://dx.doi.org/10.1007/978-3-0348-8737-3_5.
Full textDou, Zhicheng, and Vern B. Carruthers. "Cathepsin Proteases in Toxoplasma gondii." In Advances in Experimental Medicine and Biology, 49–61. Boston, MA: Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-8414-2_4.
Full textBrömme, Dieter. "Bone Remodeling: Cathepsin K in Collagen Turnover." In Matrix Proteases in Health and Disease, 79–97. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527649327.ch4.
Full textReeps, C., F. Lohöfer, H. H. Eckstein, M. Rudelius, and J. Pelisek. "Cellular expression of cathepsin proteases in symptomatic and asymptomatic AAA." In Deutsche Gesellschaft für Chirurgie, 313–15. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-00625-8_115.
Full textAgarwal, Sudhir K., Shalini Singh, and Samir Sharma. "Structural and Functional Dynamics of Lysosomal Cysteine Proteases with Particular Reference to Cathepsin B and Cathepsin H." In Frontiers in Protein Structure, Function, and Dynamics, 391–424. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-5530-5_16.
Full textShafer, William M. "Antigonococcal Action of Synthetic Peptides from Huaan Proteases Cathepsin G and Granzyme B." In Neisseriae 1990, edited by Mark Achtman, Peter Kohl, Christian Marchal, Giovanna Morelli, Andrea Seiler, and Burghard Thiesen, 633–38. Berlin, Boston: De Gruyter, 1991. http://dx.doi.org/10.1515/9783110867787-109.
Full textKatunuma, 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.
Full textKopec, Maria, and Ksenia Bykowska. "The Effect of Human Granulocytic Neutral Proteases on Hemostasis: Effects of Cathepsin G on Platelets." In Hemostasis and Circulation, 52–56. Tokyo: Springer Japan, 1992. http://dx.doi.org/10.1007/978-4-431-66925-8_10.
Full textErickson, John W., Eric T. Baldwin, T. Narayana Bhat, and Sergei Gulnik. "Structure of Human Cathepsin D: Comparison of Inhibitor Binding and Subdomain Displacement with other Aspartic Proteases." In Aspartic Proteinases, 181–92. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_22.
Full textBrix, Klaudia. "Host Cell Proteases: Cathepsins." In Activation of Viruses by Host Proteases, 249–76. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-75474-1_10.
Full textConference papers on the topic "Cathepsin proteases"
Rayes, Tina E., Raul Catena, Sharrell Lee, Dingcheng Gao, Marcin Stawowczyk, Nasser Altorki, and Vivek Mittal. "Abstract 2073: Neutrophil serine proteases, cathepsin-G and elastase, promote metastasis through cleavage of thrombospondin-1." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2073.
Full textOlson, Oakley C., Tanaya Shree, Benelita T. Elie, Alfred L. Garfall, Katherine M. Bell-McGuinn, Kenisha Simpson, Edi Brogi, Emily C. Zabor, and Johanna A. Joyce. "Abstract 549: Sensitization to chemotherapy by inhibition of cathepsin proteases in a mouse model of metastatic breast cancer." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-549.
Full textNAKAMURA, Shin. "MONOCYTE/MACROPHAGE TISSUE FACTOR: ROLE OF ITS N-GLYCOSYLATED CARBOHYDRATE MOIETY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643286.
Full textFarache Trajano, Luiza, Rebecca Moore, and Quentin Sattentau. "The Presence of Chemical Cross-Linking Stabilises HIV-1 Envelope Glycoprotein Trimer Antigens in a Model of Intramuscular Immunisation." In Building Bridges in Medical Science 2021. Cambridge Medicine Journal, 2021. http://dx.doi.org/10.7244/cmj.2021.03.001.4.
Full textAghdassi, A., D. John, J. Aschenbach, M. Sendler, B. Krüger, U. Weiß, J. Mayerle, and M. Lerch. "Die lysosomale Protease Cathepsin C beeinflusst über Aktivierung von neutrophilen Serinproteasen die akute Pankreatitis." In Viszeralmedizin 2019. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1695209.
Full textO'Brien, Shane W., Fang Xiao, Marsia A. Maglaty, Joshua S. Trinadad, Lainie P. Martin, David A. Proia, and Denise C. Connolly. "Abstract 3916: HSP90 mediates tumor-associated matrix metalloproteinase 2 and Cathepsin L protease activities in ovarian carcinoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3916.
Full textGocheva, Vasilena, Hao-Wei Wang, Bedrick Gadea, Tanaya Shree, Karen Hunter, Alfred Garfall, and Johanna A. Joyce. "Abstract LB-379: IL-4 induces cathepsin protease activity in tumor-associated macrophages to promote cancer growth and invasion." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-lb-379.
Full textYoon, Ju Yoon, David Szwajcer, Ganchimeg Ishdorj, Pat Benjaminson, Rajat Kumar, James B. Johnston, and Spencer B. Gibson. "Abstract 597: The combination of valproic acid and fludarabine treatment induces a synergistic apoptotic response in chronic lymphocytic leukemia (CLL) patients involving the lysosomal protease cathepsin B." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-597.
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