Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Cathepsin L2"'
Publikováno v:
Balkan Medical Journal, Vol 28, Iss 03, Pp 269-273 (2011)
Objective: This study describes cloning and sequence analysis of the gene coding for the cathepsin L2 gene from a F. hepatica isolate from Turkey. Methods: The adult form of F. hepatica was collected from the infected cattle liver and cDNA was obtain
Externí odkaz:
https://doaj.org/article/ade6b040525542f9bfaa77ffb5b7c73b
Autor:
Sebastian Springer, Klaudia Brix, Matthew Bogyo, Dagmar Führer, Ekkehard Weber, Maren Rehders, Zeynep Hein, Alaa Al-Hashimi, Naphannop Sereesongsaeng, Christopher J. Scott, Roberta E. Burden, Vaishnavi Venugopalan
Publikováno v:
Al-Hashimi, A, Venugopalan, V, Rehders, M, Sereesongsaeng, N, Hein, Z, Springer, S, Weber, E, Führer, D, Bogyo, M S, Scott, C J, Burden, R E & Brix, K 2020, ' Procathepsin V is secreted in a TSH regulated manner from human thyroid epithelial cells and is accessible to an activity-based probe ', International Journal of Molecular Sciences, vol. 21, no. 23, 9140 . https://doi.org/10.3390/ijms21239140
International Journal of Molecular Sciences
Volume 21
Issue 23
International Journal of Molecular Sciences, Vol 21, Iss 9140, p 9140 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 23
International Journal of Molecular Sciences, Vol 21, Iss 9140, p 9140 (2020)
The significance of cysteine cathepsins for the liberation of thyroid hormones from the precursor thyroglobulin was previously shown by in vivo and in vitro studies. Cathepsin L is most important for thyroglobulin processing in mice. The present stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dab146593ba8d70e597d8be483ff7976
https://pure.qub.ac.uk/en/publications/231eee71-80bc-4361-aac9-8c8dd36b44fa
https://pure.qub.ac.uk/en/publications/231eee71-80bc-4361-aac9-8c8dd36b44fa
Autor:
Rolf T. Urbanus, Heather Jewhurst, Aaron G. Maule, Krystyna Cwiklinski, John P. Dalton, Carolina De Marco Verissimo, Irina G. Tikhonova
Publikováno v:
PLoS Neglected Tropical Diseases, Vol 14, Iss 8, p e0008510 (2020)
PLoS Neglected Tropical Diseases
De Marco Verissimo, C, Jewhurst, H L, Tikhonova, I G, Urbanus, R T, Maule, A G, Dalton, J P & Cwiklinski, K 2020, ' Fasciola hepatica serine protease inhibitor family (serpins) Purposely crafted for regulating host proteases ', PLoS Neglected Tropical Diseases, vol. 14, no. 8, pp. e0008510 . https://doi.org/10.1371/journal.pntd.0008510
PLoS Neglected Tropical Diseases
De Marco Verissimo, C, Jewhurst, H L, Tikhonova, I G, Urbanus, R T, Maule, A G, Dalton, J P & Cwiklinski, K 2020, ' Fasciola hepatica serine protease inhibitor family (serpins) Purposely crafted for regulating host proteases ', PLoS Neglected Tropical Diseases, vol. 14, no. 8, pp. e0008510 . https://doi.org/10.1371/journal.pntd.0008510
Serine protease inhibitors (serpins) regulate proteolytic events within diverse biological processes, including digestion, coagulation, inflammation and immune responses. The presence of serpins in Fasciola hepatica excretory-secretory products indic
Publikováno v:
Journal of Molecular Modeling. 23
Cathepsin S has been demonstrated to play a crucial role in the remodeling of extracellular matrix proteins such as elastin and collagen, which in turn contribute to the structural integrity of the cardiovascular wall. Atherosclerotic lesions, aneury
Autor:
Christina Stoeckle, Eva Tolosa, Thomas Reinheckel, Christoph Peters, Sascha Hagemann, Lisa Sevenich
Publikováno v:
Biochimie; Vol 92
A genetic deficiency of the cysteine protease cathepsin L (Ctsl) in mice results in impaired positive selection of conventional CD4+ T helper cells as a result of an incomplete processing of the MHC class II associated invariant chain or incomplete p
Autor:
Sai Chetan K. Sukuru, Zhan Deng, Natasja Brooijmans, Jean Quancard, Florian Nigsch, Meir Glick, Martin Renatus, Jeremy L. Jenkins, John W. Davies, Rajiv Chopra, Ulrich Hommel, Dmitri Mikhailov, Allen Cornett
Publikováno v:
Protein Science. 19:2096-2109
We present here a comprehensive analysis of proteases in the peptide substrate space and demonstrate its applicability for lead discovery. Aligned octapeptide substrates of 498 proteases taken from the MEROPS peptidase database were used for the in s
Autor:
Stefan Gerhardt, Andrew David Morley, Peter W. Kenny, Hannes Simader, Emma V. Jones, Galith Karoutchi, Stephan Krapp, Neil Rankine, Keith Oldham, Paul A. Bethel, Stefan Steinbacher, Martin Augustin
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:4622-4625
A number of molecular recognition features have been exploited in structure-based design of selective Cathepsin inhibitors.
Autor:
Neil Rankine, Linda J. Wood, Galith Karoutchi, Michelle Coulson, Keith Oldham, Emma V. Jones, Paul A. Bethel, Stephan Krapp, Susannah J. Ford, Stefan Gerhardt, David Ryan, Matthew Grist, Peter W. Kenny, Hannes Simader, Andrew David Morley, Stuart L. Wells, Gordon A. Hamlin, Stefan Steinbacher, Jack E. Dawson, Nabil Asaad, Martin Augustin, Michael James
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:4280-4283
A series of potent Cathepsin L inhibitors with good selectivity with respect to other cysteine Cathepsins is described and SAR is discussed with reference to the crystal structure of a protein-ligand complex.
Publikováno v:
Food Chemistry. 111:879-886
Cathepsin L2 was purified to homogeneity from silver carp muscle using an array of chromatography methods. The enzyme showed affinity to con A-sepharose. Although it appeared to be 78 kDa on non-reducing SDS–PAGE and gel–substrate-activity SDS–
Autor:
Sheila Donnelly, Jonathan Lowther, Conor R. Caffrey, José F. Tort, John P. Dalton, Linda S. Brinen, Sebastian R. Geiger, Weibo Xu, Mark W. Robinson, Colin M. Stack, Charles S. Craik, Rachel Marion, James H. McKerrow, Amritha Seshaadri, Peter R. Collins
Publikováno v:
Journal of Biological Chemistry. 283:9896-9908
The helminth parasite Fasciola hepatica secretes cysteine proteases to facilitate tissue invasion, migration, and development within the mammalian host. The major proteases cathepsin L1 (FheCL1) and cathepsin L2 (FheCL2) were recombinantly produced a