József Dobó

3.3k total citations
78 papers, 2.6k citations indexed

About

József Dobó is a scholar working on Immunology, Hematology and Genetics. According to data from OpenAlex, József Dobó has authored 78 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 55 papers in Immunology, 40 papers in Hematology and 21 papers in Genetics. Recurrent topics in József Dobó's work include Complement system in diseases (54 papers), Blood Coagulation and Thrombosis Mechanisms (30 papers) and Coagulation, Bradykinin, Polyphosphates, and Angioedema (20 papers). József Dobó is often cited by papers focused on Complement system in diseases (54 papers), Blood Coagulation and Thrombosis Mechanisms (30 papers) and Coagulation, Bradykinin, Polyphosphates, and Angioedema (20 papers). József Dobó collaborates with scholars based in Hungary, United States and Denmark. József Dobó's co-authors include Péter Gál, Péter Závodszky, Gábor Pál, Andrea Kocsis, László Cervenak, Verena Schroeder, Peter G.W. Gettins, László Beinrohr, Veronika Harmat and Steffen Thiel and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The Journal of Immunology.

In The Last Decade

József Dobó

77 papers receiving 2.5k citations

Peers

József Dobó
Andrew P. Herbert United Kingdom
D T Fearon United States
Gábor Pál Hungary
Thomas F. Lint United States
Viviana P. Ferreira United States
József Dobó
Citations per year, relative to József Dobó József Dobó (= 1×) peers Matthias Ballmaier

Countries citing papers authored by József Dobó

Since Specialization
Citations

This map shows the geographic impact of József Dobó's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by József Dobó with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites József Dobó more than expected).

Fields of papers citing papers by József Dobó

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by József Dobó. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by József Dobó. The network helps show where József Dobó may publish in the future.

Co-authorship network of co-authors of József Dobó

This figure shows the co-authorship network connecting the top 25 collaborators of József Dobó. A scholar is included among the top collaborators of József Dobó based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with József Dobó. József Dobó is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Kocsis, Andrea, Edit Hirsch, Mihály Józsi, et al.. (2024). SARS-CoV-2 Nucleocapsid Protein Is Not Responsible for Over-Activation of Complement Lectin Pathway. International Journal of Molecular Sciences. 25(13). 7343–7343. 1 indexed citations
2.
Závodszky, Péter, et al.. (2023). Quantification of the zymogenicity and the substrate-induced activity enhancement of complement factor D. Frontiers in Immunology. 14. 1197023–1197023. 2 indexed citations
3.
Héja, Dávid, Bence Kiss, Eszter Boros, et al.. (2022). 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. 298(6). 101985–101985. 4 indexed citations
4.
Boros, Eszter, Márton Megyeri, József Dobó, et al.. (2022). Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides. ACS Chemical Biology. 17(4). 969–986. 1 indexed citations
5.
Hardy, Elaissa T., József Dobó, Péter Gál, et al.. (2022). Complement lectin pathway components MBL and MASP-1 promote haemostasis upon vessel injury in a microvascular bleeding model. Frontiers in Immunology. 13. 948190–948190. 9 indexed citations
6.
Pihl, Rasmus, Rasmus K. Jensen, Lisbeth Jensen, et al.. (2021). ITIH4 acts as a protease inhibitor by a novel inhibitory mechanism. Science Advances. 7(2). 40 indexed citations
7.
Székács, Inna, András Saftics, Sándor Kurunczi, et al.. (2020). Human primary endothelial label-free biochip assay reveals unpredicted functions of plasma serine proteases. Scientific Reports. 10(1). 3303–3303. 13 indexed citations
8.
Boros, Eszter, Dávid Héja, Noémi Sándor, et al.. (2019). Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum. PLoS Pathogens. 15(12). e1008232–e1008232. 24 indexed citations
9.
Jani, Péter K., Erika Kajdácsi, Zoltán Doleschall, et al.. (2017). Transcriptome analysis of inflammation-related gene expression in endothelial cells activated by complement MASP-1. Scientific Reports. 7(1). 10462–10462. 15 indexed citations
10.
Dobó, József, et al.. (2015). MASP-1 of the complement system promotes clotting via prothrombin activation. Molecular Immunology. 65(2). 398–405. 51 indexed citations
11.
Liliom, Károly, et al.. (2014). Soluble components of the flagellar export apparatus, FliI, FliJ, and FliH, do not deliver flagellin, the major filament protein, from the cytosol to the export gate. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1843(11). 2414–2423. 14 indexed citations
12.
Megyeri, Márton, Veronika Harmat, Balázs Major, et al.. (2013). Quantitative Characterization of the Activation Steps of Mannan-binding Lectin (MBL)-associated Serine Proteases (MASPs) Points to the Central Role of MASP-1 in the Initiation of the Complement Lectin Pathway. Journal of Biological Chemistry. 288(13). 8922–8934. 57 indexed citations
13.
Varga, Lilian & József Dobó. (2013). C1 Inhibitor: Quantification and Purification. Methods in molecular biology. 1100. 189–205. 4 indexed citations
14.
Dobó, József, Balázs Major, Katalin A. Kékesi, et al.. (2011). Cleavage of Kininogen and Subsequent Bradykinin Release by the Complement Component: Mannose-Binding Lectin-Associated Serine Protease (MASP)-1. PLoS ONE. 6(5). e20036–e20036. 94 indexed citations
15.
Vonderviszt, Ferenc, et al.. (2011). The Use of a Flagellar Export Signal for the Secretion of Recombinant Proteins in Salmonella. Methods in molecular biology. 824. 131–143. 2 indexed citations
16.
Dobó, József, Veronika Harmat, László Beinrohr, et al.. (2009). MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity. The Journal of Immunology. 183(2). 1207–1214. 100 indexed citations
17.
Gál, Péter, József Dobó, Péter Závodszky, & Robert B. Sim. (2009). Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions. Molecular Immunology. 46(14). 2745–2752. 55 indexed citations
18.
Dementiev, Alexey, József Dobó, & Peter G.W. Gettins. (2005). Active Site Distortion Is Sufficient for Proteinase Inhibition by Serpins. Journal of Biological Chemistry. 281(6). 3452–3457. 111 indexed citations
19.
Lacroix, Monique, Christine Ebel, József Kardos, et al.. (2001). Assembly and Enzymatic Properties of the Catalytic Domain of Human Complement Protease C1r. Journal of Biological Chemistry. 276(39). 36233–36240. 33 indexed citations
20.
Lőrincz, Zsolt, Péter Gál, József Dobó, et al.. (2000). The Cleavage of Two C1s Subunits by a Single Active C1r Reveals Substantial Flexibility of the C1s-C1r-C1r-C1s Tetramer in the C1 Complex. The Journal of Immunology. 165(4). 2048–2051. 6 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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