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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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Natural Substrates and Inhibitors of Mannan-Binding Lectin-Associated Serine Protease-1 and -2: A Study on Recombinant Catalytic Fragments

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)

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

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

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.