G
Géza Ambrus
Researcher at Hungarian Academy of Sciences
Publications - 33
Citations - 1172
Géza Ambrus is an academic researcher from Hungarian Academy of Sciences. The author has contributed to research in topics: Proteases & Serine protease. The author has an hindex of 13, co-authored 26 publications receiving 1090 citations. Previous affiliations of Géza Ambrus include University of Oxford & Scripps Research Institute.
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Journal ArticleDOI
Natural Substrates and Inhibitors of Mannan-Binding Lectin-Associated Serine Protease-1 and -2: A Study on Recombinant Catalytic Fragments
Géza Ambrus,Péter Gál,Mayumi Kojima,Katalin Szilágyi,Júlia Balczer,József Antal,László Gráf,A. Laich,Beryl E. Moffatt,Wilhelm J. Schwaeble,Robert B. Sim,Péter Závodszky +11 more
TL;DR: It is demonstrated that the SP domain alone can autoactivate and cleave C2 as efficiently as the entire catalytic region of MASP-2, while the second complement control protein module is necessary for efficient C4 cleavage.
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The Biological Functions of MBL-Associated Serine Proteases (MASPs)
Krishnan Hajela,Mayumi Kojima,Géza Ambrus,K.H. Nicky Wong,Beryl E. Moffatt,Janez Ferluga,Sumati Hajela,Péter Gál,Robert B. Sim +8 more
TL;DR: MASP1 and MASP2 appear not to have such a narrow specificity as C1r and C1s, and may have significant substrates other than complement proteins.
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Differential substrate and inhibitor profiles for human MASP-1 and MASP-2.
TL;DR: The ancient origin of MASP-1 and its thrombin-like activity suggests its involvement in a coagulation-based defense mechanism in the early evolution of innate immunity.
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Host Cell Interactome of HIV-1 Rev Includes RNA Helicases Involved in Multiple Facets of Virus Production
Souad Naji,Géza Ambrus,Peter Cimermancic,Jason R. Reyes,Jeffrey R. Johnson,Rebecca Filbrandt,Michael D. Huber,Paul Vesely,Nevan J. Krogan,John R. Yates,Andrew C. S. Saphire,Larry Gerace +11 more
TL;DR: Proteomics and statistical analysis are employed to identify candidate host cell factors that interact with HIV-1 Rev and suggest a complex set of functions for the helicases in regulation of HIV mRNAs.
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A true autoactivating enzyme: Structural insight into mannose-binding lectin-associated serine protease-2 activations
Péter Gál,Veronika Harmat,Andrea Kocsis,Tünde Bián,László Barna,Géza Ambrus,Barbara M. Végh,Júlia Balczer,Robert B. Sim,Gábor Náray-Szabó,Péter Závodszky +10 more
TL;DR: Comparison of the zymogen and active structures of MASP-2 reveals that, in addition to the activation domain, other loops of the serine protease domain undergo significant conformational changes, which could play a key role in the transition of zymogenesis into a proteolytically active form.