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personal data approved: 2023. XII. 01.
Personal data
József Dobó
name József Dobó
name of institution
doctoral school
BME George A. Olah Doctoral School of Chemistry and Chemical Technology (Academic staff member)
ELTE Doctoral School of Biology (Supervisor)
the share of work in the different doctoral schools. BME George A. Olah Doctoral School of Chemistry and Chemical Technology 25%
ELTE Doctoral School of Biology 75%
accreditation statement submitted to: Pázmány Péter Catholic University, Budapest
Contact details
E-mail address dobo.jozsefttk.mta.hu
phone number +36 1 382-6768
own web page
Academic title
scientific degree, title Ph.D.
year degree was obtained 2002
discipline to which degree belongs biology
institution granting the degree Eötvös Loránd University
Employment
2005 - Természettudományi Kutatóközpont, Enzimológiai Intézet (research institute, not university)
other (not specified) (tudományos főmunkatárs)
Thesis topic supervisor
number of doctoral students supervised until now 2.5
number of students who fulfilled course requirements 2
students who obtained their degrees:
(50%) Ráhel Dani PhD 2022  DSB-ELTE
(50%) Gábor Oroszlán PhD 2018  DSB-ELTE
Ráchel Sajó PhD 2016  GAODSCC

completed course requirement:
(50%) Ráhel Dani (PhD) 2016/08  
present PhD students:
(50%) Bence Farkas (PhD) (2025/08)  DSB-ELTE
  Thesis topic proposals
Research
research area Complement System Molecular Immunology Serine Proteases Serpins
research field in which current research is conducted biology
Publications
2023

Dani Ráhel, Oroszlán Gábor, Martinusz Róbert, Farkas Bence, Dobos Bernadett, Vadas Evelin, Závodszky Péter, Gál Péter, Dobó József: Quantification of the zymogenicity and the substrate-induced activity enhancement of complement factor D, FRONTIERS IN IMMUNOLOGY 14: 1197023
type of document: Journal paper/Article
language: English
URL 
2022

Dobó József, Kocsis Andrea, Dani Ráhel, Gál Péter: Proprotein Convertases and the Complement System, FRONTIERS IN IMMUNOLOGY 13: 958121
type of document: Journal paper/Review paper
number of independent citations: 7
language: English
URL 
2021

Oroszlán Gábor, Dani Ráhel, Végh Barbara M., Varga Dóra, Ács Andrea V., Pál Gábor, Závodszky Péter, Farkas Henriette, Gál Péter, Dobó József: Proprotein Convertase Is the Highest-Level Activator of the Alternative Complement Pathway in the Blood, JOURNAL OF IMMUNOLOGY 206: (9) pp. 2198-2205.
type of document: Journal paper/Article
number of independent citations: 9
language: English
URL 
2021

Pihl R., Jensen R.K., Poulsen E.C., Jensen L., Hansen A.G., Thøgersen I.B., Dobó J., Gál P., Andersen G.R., Enghild J.J., Thiel S.: ITIH4 acts as a protease inhibitor by a novel inhibitory mechanism, SCIENCE ADVANCES 7: (2) aba7381
type of document: Journal paper/Article
number of independent citations: 16
language: English
URL 
2019

Nagy Zoltán Attila, Szakács Dávid, Boros Eszter, Héja Dávid, Vígh Eszter, Sándor Noémi, Józsi Mihály, Oroszlán Gábor, Dobó József, Gál Péter, Pál Gábor: Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum., PLOS PATHOGENS 15: (12) e1008232
type of document: Journal paper/Article
number of independent citations: 21
language: English
URL 
2016

Dobó József, Pál Gábor, Cervenak László, Gál Péter: The emerging roles of mannose-binding lectin-associated serine proteases (MASPs) in the lectin pathway of complement and beyond, IMMUNOLOGICAL REVIEWS 274: pp. 98-111.
type of document: Journal paper/Review paper
number of independent citations: 73
language: English
URL 
2016

Dobó József, Szakács Dávid, Oroszlán Gábor, Kortvely Elod, Kiss Bence, Boros Eszter, Szász Róbert, Závodszky Péter, Gál Péter, Pál Gábor: MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked, SCIENTIFIC REPORTS 6: 31877
type of document: Journal paper/Article
number of independent citations: 79
language: English
URL 
2013

Megyeri M, Harmat V, Major B, Vegh A, Balczer J, Heja D, Szilagyi K, Datz D, Pal G, Zavodszky P, Gal P, Dobo J: 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) pp. 8922-8934.
type of document: Journal paper/Article
number of independent citations: 39
language: English
URL 
2011

Dobo J, Major B, Kekesi KA, Szabo I, Megyeri M, Hajela K, Juhasz G, Zavodszky P, Gal P: Cleavage of kininogen and subsequent bradykinin release by the complement component: mannose-binding lectin-associated serine protease (MASP)-1., PLOS ONE 6: (5) p. e20036.
type of document: Journal paper/Article
number of independent citations: 80
language: English
URL 
2009

Dobó J, Harmat V, Beinrohr L, Sebestyén E, Závodszky P, Gál P: MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity., JOURNAL OF IMMUNOLOGY 183: (2) pp. 1207-1214.
type of document: Journal paper/Article
number of independent citations: 65
language: English
URL 
Number of independent citations to these publications:389 
Scientometric data
list of publications and citations
number of scientific publications that meet accreditation criteria:
87
number of scientific publications:
82
monographs and professional books:
0
monographs/books in which chapters/sections were contributed:
6 
scientific publications published abroad that meet the accreditation criteria:
78
publications not in Hungarian, published in Hungary, meeting the accreditation criteria:
2
number of independent citations to scientific publications and creative works:
1821


2024. IV. 17.
ODT ülés
Az ODT következő ülésére 2024. június 14-én, pénteken 10.00 órakor kerül sor a Semmelweis Egyetem Szenátusi termében (Bp. Üllői út 26. I. emelet).

 
All rights reserved © 2007, Hungarian Doctoral Council. Doctoral Council registration number at commissioner for data protection: 02003/0001. Program version: 2.2358 ( 2017. X. 31. )