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personal data approved: 2021. II. 11.
Personal data
Péter Gál
name Péter Gál
name of institution
doctoral school
ELTE Doctoral School of Biology (Announcer of research topic)
PPKE Roska Tamás Doctoral School of Sciences and Technology (Academic staff member)
accreditation statement submitted to: Pázmány Péter Catholic University, Budapest
Contact details
E-mail address gal.peterttk.mta.hu
phone number +36 1 382-6768
Academic title
scientific degree, title Ph.D.
year degree was obtained 1996
discipline to which degree belongs biology
institution granting the degree ELTE (to be translated)
scientific degree, title DSc
year degree was obtained 2014
discipline to which degree belongs biology
institution granting the degree HAS
Employment
1988 - MTA Természettudományi Kutatóközpont Enzimológiai Intézet (research institute, not university)
other (not specified) (csoportvezető)
Thesis topic supervisor
number of doctoral students supervised until now 2
number of students who fulfilled course requirements 1.5
students who obtained their degrees:
(50%) Gábor Oroszlán PhD 2018  DSB-ELTE
(50%) Katalin Paréj PhD 2015  DSB-ELTE
(50%) Andrea Párisné Kocsis PhD 2012  DSB-ELTE
Márton Megyeri PhD 2012  DSB-ELTE

completed course requirement:
Tamás Horváth (PhD) 2014/08  DSB-ELTE
(50%) Ráhel Dani (PhD) 2016/08  
  Thesis topic proposals
Research
research area structural biochemistry
research field in which current research is conducted biology
Publications
2020

Hajdú István, Szilágyi András, Végh Barbara M, Wacha András, Györffy Dániel, Gráczer Éva, Somogyi Márk, Gál Péter, Závodszky Péter: Ligand-induced conformational rearrangements regulate the switch between membrane-proximal and distal functions of Rho kinase 2., COMMUNICATIONS BIOLOGY 3: (1) 721
type of document: Journal paper/Article
language: English
URL 
2019

Szakács Dávid, Kocsis Andrea, Szász Róbert, Gál Péter, Pál Gábor: Novel MASP-2 inhibitors developed via directed evolution of human TFPI1 are potent lectin pathway inhibitors, JOURNAL OF BIOLOGICAL CHEMISTRY 294: (20) pp. 8227-8237.
type of document: Journal paper/Article
number of independent citations: 1
language: English
URL 
2018

Dobo J, Kocsis A, Gal P: Be on Target: Strategies of Targeting Alternative and Lectin Pathway Components in Complement-Mediated Diseases., FRONTIERS IN IMMUNOLOGY 9: (AUG) 1851
type of document: Journal paper/Review paper
number of independent citations: 21
language: English
URL 
2018

Parej K, Kocsis A, Enyingi C, Dani R, Oroszlan G, Beinrohr L, Dobo J, Zavodszky P, Pal G, Gal P: Cutting Edge: A New Player in the Alternative Complement Pathway, MASP-1 Is Essential for LPS-Induced, but Not for Zymosan-Induced, Alternative Pathway Activation., JOURNAL OF IMMUNOLOGY 200: (7) pp. 2247-2252.
type of document: Journal paper/Article
number of independent citations: 10
language: English
URL 
2017

Oroszlan G, Dani R, Szilagyi A, Zavodszky P, Thiel S, Gal P, Dobo J: Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic Modeling of Lectin Pathway Activation Provides Possible Mechanism, FRONTIERS IN IMMUNOLOGY 8: (DEC) 1821
type of document: Journal paper/Article
number of independent citations: 5
language: English
URL 
2012

Dávid Héja, Andrea Kocsis, József Dobó, Katalin Szilágyi, Róbert Szász, Péter Závodszky, Gábor Pál, Péter Gál: Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 109: (26) pp. 10498-10503.
type of document: Journal paper/Article
number of independent citations: 96
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: 55
language: English
URL 
2009

Megyeri M, Makó V, Beinrohr L, Doleschall Z, Prohászka Z, Cervenak L, Závodszky P, Gál P: Complement protease MASP-1 activates human endothelial cells: PAR4 activation is a link between complement and endothelial function., JOURNAL OF IMMUNOLOGY 183: (5) pp. 3409-3416.
type of document: Journal paper/Article
number of independent citations: 60
language: English
URL 
2005

Gál Péter, Harmat Veronika, Kocsis Andrea, Bian T, Barna László, Ambrus Géza, Végh Barbara, Balczer Júlia, Sim R B, Náray-Szabó Gábor, Závodszky Péter: A true autoactivating enzyme - Structural insight into mannose-binding lectin-associated serine protease-2 activations, JOURNAL OF BIOLOGICAL CHEMISTRY 280: (39) pp. 33435-33444.
type of document: Journal paper/Article
number of independent citations: 63
language: English
URL 
2003

Ambrus Géza, Gál Péter, Kojima M, Szilágyi Katalin, Balczer Júlia, Antal J, Gráf László, Laich A, Moffatt BE, Schwaeble W, Sim RB, Závodszky Péter: Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and-2: A study on recombinant catalytic fragments, JOURNAL OF IMMUNOLOGY 170: (3) pp. 1374-1382.
type of document: Journal paper/Article
number of independent citations: 101
language: English
URL 
Number of independent citations to these publications:412 
Scientometric data
list of publications and citations
number of scientific publications that meet accreditation criteria:
143
number of scientific publications:
138
monographs and professional books:
0
monographs/books in which chapters/sections were contributed:
1 
scientific publications published abroad that meet the accreditation criteria:
129
publications not in Hungarian, published in Hungary, meeting the accreditation criteria:
2
number of independent citations to scientific publications and creative works:
2402


2021. X. 14.
ODT online ülés
Az ODT következő, online ülésére 2021. november 19-én 10.00 órakor kerül sor.

 
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. )