Zobrazeno 1 - 10 of 69 pro vyhledávání: '"Endopeptidases/ metabolism"'
1
Mapping prohormone processing by proteases in human enteroendocrine cells using genetically engineered organoid models
Autor: Joep Beumer, Julia Bauzá-Martinez, Tim S. Veth, Veerle Geurts, Charelle Boot, Hannah Gilliam-Vigh, Steen S. Poulsen, Filip K. Knop, Wei Wu, Hans Clevers
Publikováno v: Beumer, J, Bauzá-Martinez, J, Veth, T S, Geurts, V, Boot, C, Gilliam-Vigh, H, Poulsen, S S, Knop, F K, Wu, W & Clevers, H 2022, ' Mapping prohormone processing by proteases in human enteroendocrine cells using genetically engineered organoid models ', Proceedings of the National Academy of Sciences of the United States of America, vol. 119, no. 46, e2212057119 . https://doi.org/10.1073/pnas.2212057119
Proceedings of the National Academy of Sciences of the United States of America, 119(46). National Academy of Sciences
Enteroendocrine cells (EECs) secrete hormones in response to ingested nutrients to control physiological processes such as appetite and insulin release. EEC hormones are synthesized as large proproteins that undergo proteolytic processing to generate
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::266b5fb4e15516660a7b245ba371ce25
https://pubmed.ncbi.nlm.nih.gov/36343264
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2
A systematic approach for evaluating the role of surface-exposed loops in trypsin-like serine proteases applied to the 170 loop in coagulation factor VIIa
Autor: Anders B. Sorensen, Per Greisen, Jesper J. Madsen, Jacob Lund, Gorm Andersen, Pernille G. Wulff-Larsen, Anette A. Pedersen, Prafull S. Gandhi, Michael T. Overgaard, Henrik Østergaard, Ole H. Olsen
Publikováno v: Sorensen, A B, Greisen, P J, Madsen, J J, Lund, J, Andersen, G, Wulff-Larsen, P G, Pedersen, A A, Gandhi, P S, Overgaard, M T, Østergaard, H & Olsen, O H 2022, ' A systematic approach for evaluating the role of surface-exposed loops in trypsin-like serine proteases applied to the 170 loop in coagulation factor VIIa ', Scientific Reports, vol. 12, no. 1, 3747 . https://doi.org/10.1038/s41598-022-07620-7
Proteases play a major role in many vital physiological processes. Trypsin-like serine proteases (TLPs), in particular, are paramount in proteolytic cascade systems such as blood coagulation and complement activation. The structural topology of TLPs
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f76db24a5a1ef10c061682678804cfa1
https://vbn.aau.dk/ws/files/482458848/s41598_022_07620_7.pdf
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3
Nafamostat reduces systemic inflammation in TLR7-mediated virus-like illness
Autor: Abi G. Yates, Caroline M. Weglinski, Yuxin Ying, Isobel K. Dunstan, Tatyana Strekalova, Daniel C. Anthony
Publikováno v: Journal of Neuroinflammation, Vol 19, Iss 1, Pp 1-16 (2022)
Yates, A G, Weglinski, C M, Ying, Y, Dunstan, I K, Strekalova, T & Anthony, D C 2022, ' Nafamostat reduces systemic inflammation in TLR7-mediated virus-like illness ', Journal of Neuroinflammation, vol. 19, 8 . https://doi.org/10.1186/s12974-021-02357-y
Journal of Neuroinflammation
Background The serine protease inhibitor nafamostat has been proposed as a treatment for COVID-19, by inhibiting TMPRSS2-mediated viral cell entry. Nafamostat has been shown to have other, immunomodulatory effects, which may be beneficial for treatme
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ff4d7186f1eedb509337a7370816993
https://doi.org/10.1186/s12974-021-02357-y
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4
Identification of cell lines CL-14, CL-40 and CAL-51 as suitable models for SARS-CoV-2 infection studies
Autor: Ivan-Christian Kurolt, Laura Steenpass, Peggy Riese, Cord C. Uphoff, Corinna Meyer, Zeljka Macak Safranko, Stefan Nagel, Claudia Pommerenke, Vivien Hauer, Sabine A. Denkmann, Luka Cicin-Sain, Ulfert Rand, Margarete Zaborski, Alemka Markotić, Yeonsu Kim, Kathrin Eschke, Maren Kaufmann
Publikováno v: PLoS ONE, Vol 16, Iss 8 (2021)
e0255622
PloS one
United States
PLoS ONE
PLoS ONE, Vol 16, Iss 8, p e0255622 (2021)
The SARS-CoV-2 pandemic is a major global threat that sparked global research efforts. Pre-clinical and biochemical SARS-CoV-2 studies firstly rely on cell culture experiments where the importance of choosing an appropriate cell culture model is ofte
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32f77c7e2f957bf7e5d628013ded7c18
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8328321/?tool=EBI
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5
The multidomain architecture of a bacteriophage endolysin enables intramolecular synergism and regulation of bacterial lysis
Autor: Philippe Moreillon, Carmen Menzi, Frank Oechslin, Grégory Resch
Publikováno v: The Journal of Biological Chemistry
The Journal of biological chemistry, vol. 296, pp. 100639
Endolysins are peptidoglycan hydrolases produced at the end of the bacteriophage (phage) replication cycle to lyse the host cell. Endolysins in Gram-positive phages come in a variety of multimodular forms that combine different catalytic and cell wal
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e24dbb612b488ac79661b29c64ee8caa
https://pubmed.ncbi.nlm.nih.gov/33838182
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6
Protease-activatable scaffold proteins as versatile molecular hubs in synthetic signaling networks
Autor: Maarten Merkx, Simone F A Wouters, Sja Stijn Aper, Luc Brunsveld, Christian Ottmann, Lenne J M Lemmens, Anniek den Hamer
Publikováno v: ACS Synthetic Biology, 7(9), 2216-2225. American Chemical Society
Protease signaling and scaffold-induced control of protein-protein interactions represent two important mechanisms for intracellular signaling. Here we report a generic and modular approach to control the activity of scaffolding proteins by protease
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c6ac65384945c3297a56d5b8f6fd16d
https://doi.org/10.1021/acssynbio.8b00217
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7
SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues
Autor: Alex K. Shalek, Kun Zhang, Christopher W. Peterson, Orit Rosen, Alison Yu, Robert Lafyatis, Samuel W. Kazer, Oliver Eickelberg, Sarah A. Teichmann, Mauricio Rojas, Martijn C. Nawijn, Colin D. Bingle, Thu Elizabeth Duong, Manuel Garber, Magali Plaisant, Philana Ling Lin, Christine S. Falk, Jennifer P. Wang, Xin Sun, Hengqi Betty Zheng, G. James Gatter, Sarah K. Nyquist, Malte Kühnemund, Joachim L. Schultze, Mark A. Krasnow, Maarten van den Berge, Yan Xu, Samuel J. Allon, Daniel F. Dwyer, Peter Horvath, Benjamin Doran, Brian M. Lin, Herbert B. Schiller, Blake M. Hauser, Fabian J. Theis, Avrum Spira, Paul A. Reyfman, Hans-Peter Kiem, Shaina L. Carroll, Zhiru Guo, Douglas P. Shepherd, Michael von Papen, Ian M. Mbano, Michael Farzan, Daniel Lingwood, JoAnne L. Flynn, Christoph Muus, Dana Pe'er, Stephen R. Quake, Travis K. Hughes, Sarah M. Fortune, Sten Linnarson, Chase J. Taylor, Tanya M. Laidlaw, Emma L. Rawlins, Bonnie Berger, Ashraf S. Yousif, Joakim Lundeberg, Jeffrey A. Whitsett, Ian A. Glass, Delphine Gras, Max A. Seibold, Jay Rajagopal, Jared Feldman, Victor Tkachev, Benjamin E. Mead, Joseph E. Powell, Aviv Regev, Alasdair Leslie, Robert W. Finberg, Yuming Cao, Jennifer M.S. Sucre, Marko Vukovic, Scott B. Snapper, Vincent N. Miao, Naftali Kaminski, Laure-Emmanuelle Zaragosi, Caylin G. Winchell, Faith Taliaferro, Marko Nikolic, Ilias Angelidis, Leslie S. Kean, Lucrezia Colonna, Kathleen M. Buchheit, Aaron G. Schmidt, Ramnik J. Xavier, Tushar J. Desai, Marc H. Wadsworth, Joshua A. Boyce, Alexander M. Tsankov, Nora A. Barrett, Pascal Barbry, Muzlifah Haniffa, Heiko Adler, Alvis Brazma, Hannah P. Gideon, Meshal Ansari, Jason R. Spence, Avinash Waghray, Constantine N. Tzouanas, Jose Ordovas-Montanes, Jonathan A. Kropski, Nicholas E. Banovich, Purushothama Rao Tata, Kerstin B. Meyer, Christos Samakovlis, Haeock Lee, Carly G. K. Ziegler, Alexander V. Misharin, Deborah T. Hung, Sylvie Leroy, Julia Bals, Vanessa Mitsialis, Kourosh Saeb-Parsy
Publikováno v: Cell
Cell, 2020, 181 (5), pp.1016-1035.e19. ⟨10.1016/j.cell.2020.04.035⟩
Cell, Elsevier, 2020, 181 (5), pp.1016-1035.e19. ⟨10.1016/j.cell.2020.04.035⟩
Cell 181, 1016-1035 (2020)
Elsevier
Cell, 181(5), 1016-1035.e19. CELL PRESS
Summary There is pressing urgency to understand the pathogenesis of the severe acute respiratory syndrome coronavirus clade 2 (SARS-CoV-2), which causes the disease COVID-19. SARS-CoV-2 spike (S) protein binds angiotensin-converting enzyme 2 (ACE2),
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::727543612f7db162539d6c42ca832836
https://doi.org/10.1016/j.cell.2020.04.035
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8
The conserved threonine-rich region of the HCF-1PRO repeat activates promiscuous OGT:UDP-GlcNAc glycosylation and proteolysis activities
Autor: Daan M. F. van Aalten, Vladimir S. Borodkin, Vincent Zoete, Ute F. Röhrig, Fabienne Lammers, Patrice Waridel, Winship Herr, Vaibhav Kapuria
Publikováno v: The Journal of biological chemistry, vol. 293, no. 46, pp. 17754-17768
O-Linked GlcNAc transferase (OGT) possesses dual glycosyltransferase-protease activities. OGT thereby stably glycosylates serines and threonines of numerous proteins and, via a transient glutamate glycosylation, cleaves a single known substrate-the s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68ed876b3531baab7bad629e97b6180b
https://serval.unil.ch/resource/serval:BIB_2C5B11AB86FD.P001/REF.pdf
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9
HCoV-229E spike protein fusion activation by trypsin-like serine proteases is mediated by proteolytic processing in the S2' region
Autor: Sandrine Belouzard, Anne Goffard, Ariane Bonnin, Adeline Danneels, Jean Dubuisson
Publikováno v: Journal of General Virology
Journal of General Virology, Microbiology Society, 2018, 99 (7), pp.908-912. ⟨10.1099/jgv.0.001074⟩
Journal of General Virology, 2018, 99 (7), pp.908-912. ⟨10.1099/jgv.0.001074⟩
International audience; Human coronavirus 229E (HCoV-229E) is responsible for common colds. Like other coronaviruses, HCoV-229E exploits cellular proteases to activate fusion mediated by the spike protein. We analysed the proteolytic processing of th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::661d23c643601e9472a60b21ac68ecb9
https://pubmed.ncbi.nlm.nih.gov/29786498
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10
Fibroblast activation protein-α in fibrogenic disorders and cancer: more than a prolyl-specific peptidase?
Autor: Juillerat-Jeanneret, L., Tafelmeyer, P., Golshayan, D.
Publikováno v: Expert opinion on therapeutic targets, vol. 21, no. 10, pp. 977-991
Fibroblast activation protein-α (FAP-α) belongs to the family of prolyl-specific serine proteases. FAP-α displays both exopeptidase and endopeptidase/gelatinase/collagenase activities. FAP-α protein and/or activity have been associated with fibro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______1900::2abb17606b4e6f7d411a0586b9ced913
https://serval.unil.ch/resource/serval:BIB_243D1EA3FB5F.P001/REF.pdf
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