Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Katherine Falkowski"'
Autor:
Paweł Mak, Magdalena Kulczycka, Aleksandra Milewska, Elftherios Diamandis, Antonina Naskalska, Adam Lesner, Krzysztof Pyrc, Ewa Bielecka, Marek Ochman, Maciej Urlik, Ioannis Prassas, Katherine Falkowski, Tomasz Kantyka, Jan Potempa
Publikováno v:
Science Signaling
The protease kallikrein 13 cleaves the spike protein of the human coronavirus HKU1 to facilitate viral entry.
Priming viral entry Unlike SARS-CoV-2, the human coronavirus HKU1 normally causes relatively mild respiratory tract infections; however
Priming viral entry Unlike SARS-CoV-2, the human coronavirus HKU1 normally causes relatively mild respiratory tract infections; however
Autor:
Magdalena Kalinska, Anna Wojtysiak, Adam Lesner, Kamila Sychowska, Malgorzata Magoch, Ewa Bielecka, Katherine Falkowski, Maren Rehders, Andrzej Kozik, Natalia Gruba, Jan Potempa, Klaudia Brix, Oliwia Bochenska, Georgina S. Butler, Christopher M. Overall, Karolina Plaza, Tomasz Kantyka, Ida B. Thøgersen, Jan J. Enghild, Magdalena Wysocka, Magdalena Wiśniewska, Anastasija Pejkovska, Aleksandra Pecak, Laura Sąsiadek, Magdalena Brzezińska-Bodal, Grzegorz Dubin
Kallikrein-related peptidases (KLKs) and matrix metalloproteinases (MMPs) are secretory proteinases known to proteolytically process components of the extracellular matrix (ECM), thus modulating the pericellular environment in physiology and excessiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b58771545f8d7111f0ed3c6f9f4052f6
Autor:
Marek Ochman, Antonina Naskalska, Jan Potempa, Katherine Falkowski, Magdalena Kalinska, Adam Lesner, Ewa Bielecka, Tomasz Kantyka, Krzysztof Pyrc, Aleksandra Milewska, Paweł Mak, Maciej Urlik
Human coronavirus HKU1 (HCoV-HKU1) is associated with respiratory disease and is prevalent worldwide, but in vitro model for virus replication is lacking. Interaction between the coronaviral spike (S) protein and its receptor is the major determinant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65ba32054c69cd61cf4924a3f601e72b
https://doi.org/10.1101/2020.03.01.971499
https://doi.org/10.1101/2020.03.01.971499
Autor:
Katherine Falkowski, Michael Berg, Kristen Oelschlanger, Jason Rogers, Kyle R. Covington, Jennifer J Siegel, Matthew S. Goldberg, Jeffrey Wilkinson, Armineh Kajoian, Trisha Poteet, Sarah J. Kurley, Brooke Russell
Publikováno v:
SKIN The Journal of Cutaneous Medicine. 5:s79
N/A
Autor:
Katherine Falkowski, Ardita Aliko, Espen A Haavardsholm, Tomasz Kantyka, B.-T.S. Fevang, Anna-Birgitte Aga, M.K. Jonsson, Siri Lillegraven, Piotr Mydel, Joseph O. Sexton
Objectives: Peptidylarginine deiminases (PADs) are a family of calcium-dependent enzymes catalysing the conversion of arginine residues to citrulline, which may constitute a risk factor in rheumatoid arthritis (RA) pathogenesis. We investigated PAD a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5ae5445df5b956830e121dfe5a833e3
https://ruj.uj.edu.pl/xmlui/handle/item/153188
https://ruj.uj.edu.pl/xmlui/handle/item/153188
Autor:
Danuta Bryzek, Malgorzata Benedyk-Machaczka, Ardita Aliko, Katherine Falkowski, Piotr Mydel, Joanna Koziel, Stanisław Malicki, Tomasz Kantyka, Marta Kamińska, Ewa Bielecka, Alicia Wong
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 9, p 2174 (2019)
International Journal of Molecular Sciences
Volume 20
Issue 9
International Journal of Molecular Sciences
Volume 20
Issue 9
Citrullination, a posttranslational modification, is catalyzed by peptidylarginine deiminases (PADs), a unique family of enzymes that converts peptidyl-arginine to peptidyl-citrulline. Overexpression and/or increased PAD activity is observed in rheum
Autor:
Jan Potempa, Oliwia Bochenska, Karolina Plaza, Ulf Meyer-Hoffert, Zhihong Wu, Tomasz Kantyka, Laura Sasiadek, Jan A. Fischer, Barbara Potempa, Andrzej Kozik, Katherine Falkowski, Magdalena Kalinska, Ewa Bielecka
Publikováno v:
Journal of Biological Chemistry. 291:18753-18764
Periodontitis, a chronic inflammation driven by dysbiotic subgingival bacterial flora, is linked on clinical levels to the development of a number of systemic diseases and to the development of oral and gastric tract tumors. A key pathogen, Porphyrom
Autor:
Natalia Gruba, Adam Lesner, Jan Potempa, Maren Rehders, Andrzej Kozik, Katherine Falkowski, Laura Sąsiadek, Klaudia Brix, Magdalena Brzezińska-Bodal, Christopher M. Overall, Aleksandra Pecak, Magdalena Wysocka, Magdalena Kalinska, Anna Wojtysiak, Ewa Bielecka, Ida B. Thøgersen, Magdalena Wiśniewska, Georgina S. Butler, Grzegorz Dubin, Oliwia Bochenska, Karolina Plaza, Anastasija Pejkovska, Tomasz Kantyka, Jan J. Enghild, Malgorzata Magoch, Kamila Sychowska
Publikováno v:
Falkowski, K, Bielecka, E, Thøgersen, I B, Bocheńska, O, Płaza, K, Kalińska, M, Sąsiadek, L, Magoch, M, Pęcak, A, Wiśniewska, M, Gruba, N, Wysocka, M, Wojtysiak, A, Brzezińska-Bodal, M, Sychowska, K, Pejkovska, A, Rehders, M, Butler, G, Overall, C M, Brix, K, Dubin, G, Lesner, A, Kozik, A, Enghild, J J, Potempa, J & Kantyka, T 2020, ' Kallikrein-Related Peptidase 14 Activates Zymogens of Membrane Type Matrix Metalloproteinases (MT-MMPs)-A CleavEx Based Analysis ', International Journal of Molecular Sciences, vol. 21, no. 12, 4383 . https://doi.org/10.3390/ijms21124383
International Journal of Molecular Sciences, Vol 21, Iss 4383, p 4383 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 12
International Journal of Molecular Sciences, Vol 21, Iss 4383, p 4383 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 12
Kallikrein-related peptidases (KLKs) and matrix metalloproteinases (MMPs) are secretory proteinases known to proteolytically process components of the extracellular matrix, modulating the pericellular environment in physiology and in pathologies. The
Autor:
Ardita Aliko, Anna-Birgitte Aga, Espen A Haavardsholm, Piotr Mydel, M.K. Jonsson, Katherine Falkowski, B.-T.S. Fevang, Siri Lillegraven, Joseph O. Sexton
Publikováno v:
FRIDAY, 15 JUNE 2018.
Background Peptidylarginine deiminases (PADs) are a family of enzymes catalysing the conversion of arginine residues to citrulline, a post translational modification which has been recognised in the generation of neo-epitopes due to anti-citrullinate