József Dobó

Research Centre for Natural Sciences

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Articles (14)

Collaborators (8)

Gábor Pál

Eötvös Loránd University

Rasmus Kjeldsen Jensen

Aarhus University

Márton Megyeri

Head of CMC Development

VRG Therapeutics

Edit Hirsch

Mihály Józsi

Eötvös Loránd University

Jan Johannes Enghild

Aarhus University

Zoltán Attila Nagy

John Dalton

University of Galway

József Dobó

Research Interests

Explore related searches

Contact this professor

Articles (14)

Collaborators (8)

Gábor Pál

Rasmus Kjeldsen Jensen

Márton Megyeri

Edit Hirsch

Mihály Józsi

Jan Johannes Enghild

Zoltán Attila Nagy

John Dalton

How do I reach out?

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József Dobó

Research Interests

Explore related searches

Contact this professor

Articles (14)

SARS-CoV-2 Nucleocapsid Protein Is Not Responsible for Over-Activation of Complement Lectin Pathway

Complement MASP-1 Modifies Endothelial Wound Healing

The Lectin Pathway of the Complement System—Activation, Regulation, Disease Connections and Interplay with Other (Proteolytic) Systems

Cooperation of Complement MASP-1 with Other Proinflammatory Factors to Enhance the Activation of Endothelial Cells

Correction: Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation (Journal of Biological Chemistry (2022) 298(6), (S0021925822004252), (10.1016/j.jbc.2022.101985))

Quantification of the zymogenicity and the substrate-induced activity enhancement of complement factor D.

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

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

Fasciola hepatica is refractory to complement killing by preventing attachment of mannose binding lectin (MBL) and inhibiting MBL-associated serine proteases (MASPs) with serpins

Complement lectin pathway components MBL and MASP-1 promote haemostasis upon vessel injury in a microvascular bleeding model

Proprotein Convertases and the Complement System

ITIH4 acts as a protease inhibitor by a novel inhibitory mechanism

Proprotein Convertase Is the Highest-Level Activator of the Alternative Complement Pathway in the Blood

Human primary endothelial label-free biochip assay reveals unpredicted functions of plasma serine proteases

Collaborators (8)

Gábor Pál

Rasmus Kjeldsen Jensen

Márton Megyeri

Edit Hirsch

Mihály Józsi

Jan Johannes Enghild

Zoltán Attila Nagy

John Dalton

How do I reach out?

Meet Kite AI