Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Júlia Balczer"'
Autor:
Andrea Kocsis, Dalma Bartus, Edit Hirsch, Mihály Józsi, István Hajdú, József Dobó, Júlia Balczer, Gábor Pál, Péter Gál
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 13, p 7343 (2024)
The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a viral structural protein that is abundant in the circulation of infected individuals. Previous published studies reported controversial data about the r
Externí odkaz:
https://doaj.org/article/3fc5f7407bbc43f2a7ab4e1b37043726
Autor:
Katalin Szilágyi, István Hajdú, Beáta Flachner, Zsolt Lőrincz, Júlia Balczer, Péter Gál, Péter Závodszky, Chiara Pirli, Balázs Balogh, István M. Mándity, Sándor Cseh, György Dormán
Publikováno v:
Molecules, Vol 24, Iss 20, p 3641 (2019)
The complement system is associated with various diseases such as inflammation or auto-immune diseases. Complement-targeted drugs could provide novel therapeutic intervention against the above diseases. C1s, a serine protease, plays an important role
Externí odkaz:
https://doaj.org/article/3ce5a0ddd5dc4f4ca2722c57e2d07a73
Autor:
Sándor Cseh, István Hajdú, Péter Závodszky, Júlia Balczer, Katalin Szilágyi, István M. Mándity, Chiara Pirli, György Dormán, Zsolt Lőrincz, Péter Gál, Beáta Flachner, Balázs Balogh
Publikováno v:
Molecules
Volume 24
Issue 20
Molecules, Vol 24, Iss 20, p 3641 (2019)
Volume 24
Issue 20
Molecules, Vol 24, Iss 20, p 3641 (2019)
The complement system is associated with various diseases such as inflammation or auto-immune diseases. Complement-targeted drugs could provide novel therapeutic intervention against the above diseases. C1s, a serine protease, plays an important role
Autor:
Katalin Szilágyi, Ádám Végh, Péter Gál, Márton Megyeri, Péter Závodszky, Balázs Major, Veronika Harmat, Dávid Héja, József Dobó, Júlia Balczer, Gábor Pál, Dániel Datz
Publikováno v:
Journal of Biological Chemistry. 288:8922-8934
Mannan-binding lectin (MBL)-associated serine proteases, MASP-1 and MASP-2, have been thought to autoactivate when MBL/ficolin.MASP complexes bind to pathogens triggering the complement lectin pathway. Autoactivation of MASPs occurs in two steps: 1)
Autor:
Barbara M. Végh, Andrea Kocsis, Júlia Balczer, Péter Závodszky, Gábor Pál, Katalin A. Kékesi, Róbert Szász, József Dobó, Péter Gál
Publikováno v:
The Journal of Immunology. 185:4169-4178
The complement system, an essential part of the innate immune system, can be activated through three distinct routes: the classical, the alternative, and the lectin pathways. The contribution of individual activation pathways to different biological
Autor:
Barbara M. Végh, Péter Gál, Tünde Bián, Veronika Harmat, Andrea Kocsis, Júlia Balczer, László Barna, Robert B. Sim, Géza Ambrus, Gábor Náray-Szabó, Péter Závodszky
Publikováno v:
Journal of Biological Chemistry. 280:33435-33444
Few reports have described in detail a true autoactivation process, where no extrinsic cleavage factors are required to initiate the autoactivation of a zymogen. Herein, we provide structural and mechanistic insight into the autoactivation of a multi
Autor:
Péter, Gál, Veronika, Harmat, Andrea, Kocsis, Tünde, Bián, László, Barna, Géza, Ambrus, Barbara, Végh, Júlia, Balczer, Robert B, Sim, Gábor, Náray-Szabó, Péter, Závodszky
Publikováno v:
The Journal of biological chemistry. 280(39)
Few reports have described in detail a true autoactivation process, where no extrinsic cleavage factors are required to initiate the autoactivation of a zymogen. Herein, we provide structural and mechanistic insight into the autoactivation of a multi
Autor:
Robert B. Sim, Mayumi Kojima, Péter Závodszky, Júlia Balczer, A. Laich, Géza Ambrus, László Gráf, Katalin Szilágyi, Beryl E. Moffatt, József Antal, Péter Gál, Wilhelm J. Schwaeble
Publikováno v:
Scopus-Elsevier
Mannan-binding lectin-associated serine protease (SP) (MASP)-1 and MASP-2 are modular SP and form complexes with mannan-binding lectin, the recognition molecule of the lectin pathway of the complement system. To characterize the enzymatic properties