Zoltan A. Nagy

Budapest, BU 1117, Hungary

Last Updated: 09/26/2026

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Found 9 publications

Pancreatitis-associated chymotrypsin C (CTRC) variant p.R240Q selectively impairs trypsinogen degradation through disruption of long-range electrostatic interactions.

Pancreatitis-associated chymotrypsin C (CTRC) variant p.R240Q selectively impairs trypsinogen degradation through disruption of long-range electrostatic interactions.

Journal: Scientific reports

Published: January 11, 2026

Targeting the complement lectin pathway with a highly specific MASP-2 inhibitor protects against renal ischemia-reperfusion injury.

Targeting the complement lectin pathway with a highly specific MASP-2 inhibitor protects against renal ischemia-reperfusion injury.

Journal: Proceedings of the National Academy of Sciences of the United States of America

Published: April 14, 2025

To be, or not to be cleaved: Directed evolution of a canonical serine protease inhibitor against active and inactive protease pair identifies binding loop residue critical for prevention of proteolytic cleavage.

To be, or not to be cleaved: Directed evolution of a canonical serine protease inhibitor against active and inactive protease pair identifies binding loop residue critical for prevention of proteolytic cleavage.

Journal: Protein science : a publication of the Protein Society

Published: December 22, 2024

Misfolding PRSS1 variant p.Ala61Val in a case of suspected intrauterine pancreatitis.

Misfolding PRSS1 variant p.Ala61Val in a case of suspected intrauterine pancreatitis.

Journal: Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.]

Published: August 12, 2024

Substrate specificity of human chymotrypsin-like protease (CTRL) characterized by phage display-selected small-protein inhibitors.

Substrate specificity of human chymotrypsin-like protease (CTRL) characterized by phage display-selected small-protein inhibitors.

Journal: Pancreatology : official journal of the International Association of Pancreatology (IAP) ... [et al.]

Published: August 04, 2023

Correction: Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.

Correction: Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.

Journal: The Journal of biological chemistry

Published: December 23, 2022

Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides.

Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides.

Journal: ACS chemical biology

Published: April 04, 2022

Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.

Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.

Journal: The Journal of biological chemistry

Published: October 06, 2021

Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum.

Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum.

Journal: PLoS pathogens

Published: July 22, 2019

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Last Updated: 09/26/2026