Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Mirosław Książęk"'
Autor:
Krzysztof M. Zak, Mark J. Bostock, Irena Waligorska, Ida B. Thøgersen, Jan J. Enghild, Grzegorz M. Popowicz, Przemyslaw Grudnik, Jan Potempa, Miroslaw Ksiazek
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 36, Iss 1, Pp 1267-1281 (2021)
Mirolysin is a secretory protease of Tannerella forsythia, a member of the dysbiotic oral microbiota responsible for periodontitis. In this study, we show that mirolysin latency is achieved by a “cysteine-switch” mechanism exerted by Cys23 in the
Externí odkaz:
https://doaj.org/article/facc41ee0c7f40019822708c69e05cfb
Autor:
Tibisay Guevara, Arturo Rodriguez-Banqueri, Miroslaw Ksiazek, Jan Potempa, F. Xavier Gomis-Rüth
Publikováno v:
IUCrJ, Vol 7, Iss 1, Pp 18-29 (2020)
Tannerella forsythia is an oral dysbiotic periodontopathogen involved in severe human periodontal disease. As part of its virulence factor armamentarium, at the site of colonization it secretes mirolysin, a metallopeptidase of the unicellular pappaly
Externí odkaz:
https://doaj.org/article/25296af507af4334ad354c0e4cb88394
Autor:
Stanislaw Malicki, Miroslaw Ksiazek, Pawel Majewski, Aleksandra Pecak, Piotr Mydel, Przemyslaw Grudnik, Grzegorz Dubin
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 638-643 (2019)
Inhibitors of serine proteases are not only extremely useful in the basic research but are also applied extensively in clinical settings. Using Systematic Evolution of Ligands by Exponential Enrichment (SELEX) approach we developed a family of novel,
Externí odkaz:
https://doaj.org/article/bdf17d8dea0e4e3a9c78cd0b1d122473
Autor:
Mariusz Madej, Zuzanna Nowakowska, Miroslaw Ksiazek, Anna M. Lasica, Danuta Mizgalska, Magdalena Nowak, Anna Jacula, Monika Bzowska, Carsten Scavenius, Jan J. Enghild, Joseph Aduse-Opoku, Michael A. Curtis, F. Xavier Gomis-Rüth, Jan Potempa
Publikováno v:
mBio, Vol 12, Iss 1 (2021)
Bacteria have evolved multiple systems to transport effector proteins to their surface or into the surrounding milieu. These proteins have a wide range of functions, including attachment, motility, nutrient acquisition, and toxicity in the host. Porp
Externí odkaz:
https://doaj.org/article/da74c30a8ca24a36ba46e4f453049b0e
Autor:
Rielana Wichert, Anna Ermund, Stefanie Schmidt, Matthias Schweinlin, Miroslaw Ksiazek, Philipp Arnold, Katharina Knittler, Frederike Wilkens, Barbara Potempa, Björn Rabe, Marit Stirnberg, Ralph Lucius, Jörg W. Bartsch, Susanna Nikolaus, Maren Falk-Paulsen, Philip Rosenstiel, Marco Metzger, Stefan Rose-John, Jan Potempa, Gunnar C. Hansson, Peter J. Dempsey, Christoph Becker-Pauly
Publikováno v:
Cell Reports, Vol 21, Iss 8, Pp 2090-2103 (2017)
The host metalloprotease meprin β is required for mucin 2 (MUC2) cleavage, which drives intestinal mucus detachment and prevents bacterial overgrowth. To gain access to the cleavage site in MUC2, meprin β must be proteolytically shed from epithelia
Externí odkaz:
https://doaj.org/article/b24e999113e241ad82f86e3fbecdd8d3
Publikováno v:
Frontiers in Cellular and Infection Microbiology, Vol 7 (2017)
Protein secretion systems are vital for prokaryotic life, as they enable bacteria to acquire nutrients, communicate with other species, defend against biological and chemical agents, and facilitate disease through the delivery of virulence factors. I
Externí odkaz:
https://doaj.org/article/d011e1e7524849e881e2321c8b9947ca
Autor:
Danuta Mizgalska, Arturo Rodríguez-Banqueri, Florian Veillard, Mirosław Książęk, Theodoros Goulas, Tibisay Guevara, Ulrich Eckhard, Jan Potempa, F. Xavier Gomis-Rüth
Publikováno v:
Open Biology, Vol 14, Iss 6 (2024)
Gram-negative bacteria from the Bacteroidota phylum possess a type-IX secretion system (T9SS) for protein secretion, which requires cargoes to have a C-terminal domain (CTD). Structurally analysed CTDs are from Porphyromonas gingivalis proteins RgpB,
Externí odkaz:
https://doaj.org/article/ad1a5dec84394926a6901eee7856ddc6
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e48537 (2012)
Tannerella forsythia is a gram-negative bacteria, which is strongly associated with the development of periodontal disease. Karilysin is a newly identified metalloprotease-like enzyme, that is secreted from T. forsythia. Karilysin modulates the host
Externí odkaz:
https://doaj.org/article/45224428fd3e48158a3b929160097668