@article{MTMT:34046199,
	title = {Chlorotoxin binds to both matrix metalloproteinase 2 and neuropilin 1},
	url = {https://m2.mtmt.hu/api/publication/34046199},
	author = {Farkas, Sándor and Cioca, Daniel and Murányi, József and Hornyák, Péter and Brunyánszki, Attila and Szekér, Patrik and Boros, Eszter and Horváth, Patrik and Hujber, Zoltán and Rácz, Gábor Z. and Nagy, Noémi and Tóth, Rebeka and Nyitray, László and Péterfi, Zalán},
	doi = {10.1016/j.jbc.2023.104998},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {299},
	unique-id = {34046199},
	issn = {0021-9258},
	year = {2023},
	eissn = {1083-351X},
	orcid-numbers = {Farkas, Sándor/0000-0001-6666-3112; Murányi, József/0000-0001-5672-6482; Nyitray, László/0000-0003-4717-5994}
}

@article{MTMT:31966884,
	title = {Lehetőségek és buktatók a SARS-CoV-2-antigén és az ellene termelt antitestek kimutatásában = Possibilities and pitfalls of virus antigen and antibody detection of SARS-CoV-2},
	url = {https://m2.mtmt.hu/api/publication/31966884},
	author = {Medgyaszai, Melinda and Péterfi, Zalán and Valkó, Anna},
	doi = {10.1556/650.2021.32210},
	journal-iso = {ORV HETIL},
	journal = {ORVOSI HETILAP},
	volume = {162},
	unique-id = {31966884},
	issn = {0030-6002},
	abstract = {Összefoglaló. A koronavírus-betegség 2019 (COVID–19)-pandémia komoly kihívás elé állította nemcsak a mikrobiológiai laboratóriumokat, hanem az eredmények interpretálásában a klinikumban dolgozó kollégákat is. Az orvostudomány specializált világában az immunológiai és a fertőző betegségekkel kapcsolatos ismeretek az antimikrobás terápiás megoldások sikeressége, valamint a széles körű vakcináció miatt az idők folyamán számos szakterületen háttérbe szorultak, felfrissítésük sürgető és elengedhetetlen része a pandémiával való megküzdésnek. A diagnosztikai vizsgálatok fontos eszközei a járvány megfékezésének, illetve a betegek ellátásának, azonban a vírus és az emberi szervezet interakciójának megértése elengedhetetlenül szükséges a korrekt epidemiológiai és gyógyászati véleményalkotáshoz. Jelen cikkünk az orvosi gyakorlat számára foglalja össze a súlyos akut légzőszervi szindrómát okozó koronavírus-2 (SARS-CoV-2) kimutatására, valamint az immunrendszer specifikus immunválaszának szerológiai vizsgálatára irányuló, gyakorlatban használatos módszereket, azok helyét, szerepét és értékelésük szempontjait a tudomány jelen állása szerint. Orv Hetil. 2021; 162(15): 563–570. Summary. The coronavirus disease 2019 (COVID-19) pandemic posed a serious challenge not only for microbiology laboratories, but also for the clinicians in interpretation of the results. In the specialized world of medicine, knowledge of immunological and infectious diseases has been relegated to the background in many disciplines over time due to the success of antimicrobial therapies and widespread vaccination, so updating them is an urgent and essential part of the fight against the pandemic. Diagnostic tests are important tools for controlling the epidemic and caring for patients, but understanding the interaction between the virus and the human body is essential to form a correct epidemiological and medical opinion. This paper summarizes the medical methods for the detection of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the serological testing of the specific immune response of the immune system, their place, role and criteria of their evaluation according to current scientific knowledge. Orv Hetil. 2021; 162(15): 563–570.},
	year = {2021},
	eissn = {1788-6120},
	pages = {563-570}
}

@article{MTMT:3324695,
	title = {Interaction between p22(phox) and Nox4 in the endoplasmic reticulum suggests a unique mechanism of NADPH oxidase complex formation.},
	url = {https://m2.mtmt.hu/api/publication/3324695},
	author = {Zana, Melinda and Péterfi, Zalán and Kovács, Hajnal Anna and Tóth, Zsuzsanna and Enyedi, Balázs and Morel, F and Paclet, MH and Donkó, Ágnes and Morand, S and Leto, TL and Geiszt, Miklós},
	doi = {10.1016/j.freeradbiomed.2017.12.031},
	journal-iso = {FREE RADICAL BIO MED},
	journal = {FREE RADICAL BIOLOGY AND MEDICINE},
	volume = {116},
	unique-id = {3324695},
	issn = {0891-5849},
	abstract = {The p22(phox) protein is an essential component of the phagocytic- and inner ear NADPH oxidases but its relationship to other Nox proteins is less clear. We have studied the role of p22(phox) in the TGF-beta1-stimulated H2O2 production of primary human and murine fibroblasts. TGF-beta1 induced H2O2 release of the examined cells, and the response was dependent on the expression of both Nox4 and p22(phox). Interestingly, the p22(phox) protein was present in the absence of any detectable Nox/Duox expression, and the p22(phox) level was unaffected by TGF-beta1. On the other hand, Nox4 expression was dependent on the presence of p22(phox), establishing an asymmetrical relationship between the two proteins. Nox4 and p22(phox) proteins localized to the endoplasmic reticulum and their distribution was unaffected by TGF-beta1. We used a chemically induced protein dimerization method to study the orientation of p22(phox) and Nox4 in the endoplasmic reticulum membrane. This technique is based on the rapamycin-mediated heterodimerization of the mammalian FRB domain with the FK506 binding protein. The results of these experiments suggest that the enzyme complex produces H2O2 into the lumen of the endoplasmic reticulum, indicating that Nox4 contributes to the development of the oxidative milieu within this organelle.},
	year = {2018},
	eissn = {1873-4596},
	pages = {41-49},
	orcid-numbers = {Kovács, Hajnal Anna/0000-0001-7928-7531; Tóth, Zsuzsanna/0000-0002-0628-1320; Enyedi, Balázs/0000-0001-5713-3785}
}

@article{MTMT:2891430,
	title = {Structure-function analysis of peroxidasin provides insight into the mechanism of collagen IV crosslinking},
	url = {https://m2.mtmt.hu/api/publication/2891430},
	author = {Lázár, Enikő and Péterfi, Zalán and Sirokmány, Gábor and Kovács, Hajnal Anna and Klement, Éva and Medzihradszky F., Katalin and Geiszt, Miklós},
	doi = {10.1016/j.freeradbiomed.2015.02.015},
	journal-iso = {FREE RADICAL BIO MED},
	journal = {FREE RADICAL BIOLOGY AND MEDICINE},
	volume = {83},
	unique-id = {2891430},
	issn = {0891-5849},
	abstract = {Basement membranes provide structural support and convey regulatory signals to cells in diverse tissues. Assembly of collagen IV into a sheet-like network is a fundamental mechanism during the formation of basement membranes. Peroxidasin (PXDN) was recently described to catalyze crosslinking of collagen IV through the formation of sulfilimine bonds. Despite the significance of this pathway in tissue genesis, our understanding of PXDN function is far from complete. In this work we demonstrate that collagen IV crosslinking is a physiological function of mammalian PXDN. Moreover, we carried out structure-function analysis of PXDN to gain a better insight into its role in collagen IV synthesis. We identify conserved cysteines in PXDN that mediate the oligomerization of the protein into a trimeric complex. We also demonstrate that oligomerization is not an absolute requirement for enzymatic activity, but optimal collagen IV coupling is only catalyzed by the PXDN trimers. Localization experiments of different PXDN mutants in two different cell models revealed that PXDN oligomers, but not monomers, adhere on the cell surface in "hot spots," which represent previously unknown locations of collagen IV crosslinking. ©2015 Published by Elsevier Inc.},
	keywords = {PEROXIDASE; Reactive oxygen species; Collagen IV; crosslink; Peroxidasin},
	year = {2015},
	eissn = {1873-4596},
	pages = {273-282},
	orcid-numbers = {Sirokmány, Gábor/0000-0002-9473-2434; Kovács, Hajnal Anna/0000-0001-7928-7531}
}

@article{MTMT:2706633,
	title = {Peroxidasins: novel players in tissue genesis},
	url = {https://m2.mtmt.hu/api/publication/2706633},
	author = {Péterfi, Zalán and Geiszt, Miklós},
	doi = {10.1016/j.tibs.2014.05.005},
	journal-iso = {TRENDS BIOCHEM SCI},
	journal = {TRENDS IN BIOCHEMICAL SCIENCES},
	volume = {39},
	unique-id = {2706633},
	issn = {0968-0004},
	abstract = {Stabilization of extracellular matrix by protein crosslinking is a universal and essential process in multicellular organisms. Recent findings revealed that peroxidasin, a unique heme-peroxidase, produces hypohalides to support matrix synthesis. Unexpectedly, the highly reactive and potentially damaging hypohalides mediate the formation of sulfilimine bonds between adjacent collagen IV protomers. This crosslink is a fundamental feature of basal membranes, defining peroxidasin-dependent oxidant generation and sulfilimine crosslink formation as an elemental mechanism of tissue biogenesis. © 2014 Elsevier Ltd. All rights reserved.},
	keywords = {PEROXIDASE; extracellular matrix; ROS; Collagen IV; Peroxidasin; sulfilimine},
	year = {2014},
	eissn = {1362-4326},
	pages = {305-307}
}

@article{MTMT:2553231,
	title = {Peroxidasin-like protein: A novel peroxidase homologue in the human heart},
	url = {https://m2.mtmt.hu/api/publication/2553231},
	author = {Péterfi, Zalán and Tóth, Zsuzsanna and Kovács, Hajnal Anna and Lázár, Enikő and Sum, A and Donkó, Ágnes and Sirokmány, Gábor and Shah, AM and Geiszt, Miklós},
	doi = {10.1093/cvr/cvt256},
	journal-iso = {CARDIOVASC RES},
	journal = {CARDIOVASCULAR RESEARCH},
	volume = {101},
	unique-id = {2553231},
	issn = {0008-6363},
	abstract = {AimsPeroxidases serve diverse biological functions including well-characterized activities in host defence and hormone biosynthesis. More recently, peroxidasin (PXDN) was found to be involved in collagen IV cross-linking in the extracellular matrix (ECM). The aim of this study was to characterize the expression and function of peroxidasin-like protein (PXDNL), a previously unknown peroxidase homologue.Methods and resultsWe cloned the PXDNL cDNA from the human heart and identified its expression pattern by northern blot, in situ hybridization, and immunohistochemistry. PXDNL is expressed exclusively in the heart and it has evolved to lose its peroxidase activity. The protein is produced by cardiomyocytes and localizes to cell-cell junctions. We also demonstrate that PXDNL can form a complex with PXDN and antagonizes its peroxidase activity. Furthermore, we show an increased expression of PXDNL in the failing myocardium.ConclusionPXDNL is a unique component of the heart with a recently evolved inactivation of peroxidase function. The elevation of PXDNL levels in the failing heart may contribute to ECM dysregulation due to its antagonism of PXDN function. © 2013 The Author.},
	keywords = {PEROXIDASE; Reactive oxygen species; extracellular matrix; Peroxidasin-like protein; Peroxidasin},
	year = {2014},
	eissn = {1755-3245},
	pages = {393-399},
	orcid-numbers = {Tóth, Zsuzsanna/0000-0002-0628-1320; Kovács, Hajnal Anna/0000-0001-7928-7531; Sirokmány, Gábor/0000-0002-9473-2434}
}

@mastersthesis{MTMT:2786895,
	title = {Új molekulák és jelátviteli folyamatok fibrotikus elváltozásokban},
	url = {https://m2.mtmt.hu/api/publication/2786895},
	author = {Péterfi, Zalán},
	doi = {10.14753/SE.2013.1798},
	unique-id = {2786895},
	year = {2013}
}

@article{MTMT:2397639,
	title = {EGF regulates tyrosine phosphorylation and membrane-translocation of the scaffold protein Tks5},
	url = {https://m2.mtmt.hu/api/publication/2397639},
	author = {Fekete, Anna and Bőgel, Gábor and Pesti, Szabolcs and Péterfi, Zalán and Geiszt, Miklós and Buday, László},
	doi = {10.1186/1750-2187-8-8},
	journal-iso = {JOURNAL OF MOLECULAR SIGNALING},
	journal = {JOURNAL OF MOLECULAR SIGNALING},
	volume = {8},
	unique-id = {2397639},
	abstract = {Background: Tks5/FISH is a scaffold protein comprising of five SH3 domains and one PX domain. Tks5 is a substrate of the tyrosine kinase Src and is required for the organization of podosomes/invadopodia implicated in invasion of tumor cells. Recent data have suggested that a close homologue of Tks5, Tks4, is implicated in the EGF signaling.Results: Here, we report that Tks5 is a component of the EGF signaling pathway. In EGF-treated cells, Tks5 is tyrosine phosphorylated within minutes and the level of phosphorylation is sustained for at least 2 hours. Using specific kinase inhibitors, we demonstrate that tyrosine phosphorylation of Tks5 is catalyzed by Src tyrosine kinase. We show that treatment of cells with EGF results in plasma membrane translocation of Tks5. In addition, treatment of cells with LY294002, an inhibitor of PI 3-kinase, or mutation of the PX domain reduces tyrosine phosphorylation and membrane translocation of Tks5.Conclusions: Our results identify Tks5 as a novel component of the EGF signaling pathway. © 2013 Fekete et al.; licensee BioMed Central Ltd.},
	keywords = {EGF RECEPTOR; SRC; PX DOMAIN; Tks5; Tks4; PI 3-kinase},
	year = {2013},
	eissn = {1750-2187},
	orcid-numbers = {Bőgel, Gábor/0000-0002-7677-6855; Buday, László/0000-0003-3518-5757}
}

@article{MTMT:1721813,
	title = {The Homolog of the Five SH3-Domain Protein (HOFI/SH3PXD2B) Regulates Lamellipodia Formation and Cell Spreading},
	url = {https://m2.mtmt.hu/api/publication/1721813},
	author = {Lányi, Árpád and Barath, M and Péterfi, Zalán and Bőgel, Gábor and Orient, Anna and Simon, Tünde and Petrovszki, E and Kis-Tóth, Katalin and Sirokmány, Gábor and Rajnavölgyi, Éva and Terhorst, C and Buday, László and Geiszt, Miklós},
	doi = {10.1371/journal.pone.0023653},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {6},
	unique-id = {1721813},
	issn = {1932-6203},
	abstract = {Motility of normal and transformed cells within and across tissues requires specialized subcellular structures, e. g. membrane ruffles, lamellipodia and podosomes, which are generated by dynamic rearrangements of the actin cytoskeleton. Because the formation of these sub-cellular structures is complex and relatively poorly understood, we evaluated the role of the adapter protein SH3PXD2B [HOFI, fad49, Tks4], which plays a role in the development of the eye, skeleton and adipose tissue. Surprisingly, we find that SH3PXD2B is requisite for the development of EGF-induced membrane ruffles and lamellipodia, as well as for efficient cellular attachment and spreading of HeLa cells. Furthermore, SH3PXD2B is present in a complex with the non-receptor protein tyrosine kinase Src, phosphorylated by Src, which is consistent with SH3PXD2B accumulating in Src-induced podosomes. Furthermore, SH3PXD2B closely follows the subcellular relocalization of cortactin to Src-induced podosomes, EGF-induced membrane ruffles and lamellipodia. Because SH3PXD2B also forms a complex with the C-terminal region of cortactin, we propose that SH3PXD2B is a scaffold protein that plays a key role in regulating the actin cytoskeleton via Src and cortactin.},
	keywords = {PHOSPHORYLATION; INVASION; CANCER-CELLS; MIGRATION; actin cytoskeleton; cortactin; SRC SUBSTRATE; CONTACT SITES; PODOSOME FORMATION; PX DOMAIN},
	year = {2011},
	eissn = {1932-6203},
	orcid-numbers = {Bőgel, Gábor/0000-0002-7677-6855; Sirokmány, Gábor/0000-0002-9473-2434; Buday, László/0000-0003-3518-5757}
}

@article{MTMT:1468050,
	title = {Urothelial cells produce hydrogen peroxide through the activation of Duox1},
	url = {https://m2.mtmt.hu/api/publication/1468050},
	author = {Donkó, Ágnes and Ruisanchez, Éva and Orient, Anna and Enyedi, Balázs and Kapui, Réka and Péterfi, Zalán and de Deken, X and Benyó, Zoltán and Geiszt, Miklós},
	doi = {10.1016/j.freeradbiomed.2010.09.027},
	journal-iso = {FREE RADICAL BIO MED},
	journal = {FREE RADICAL BIOLOGY AND MEDICINE},
	volume = {49},
	unique-id = {1468050},
	issn = {0891-5849},
	year = {2010},
	eissn = {1873-4596},
	pages = {2040-2048},
	orcid-numbers = {Ruisanchez, Éva/0000-0001-7779-226X; Enyedi, Balázs/0000-0001-5713-3785; Kapui, Réka/0000-0002-8670-9963; Benyó, Zoltán/0000-0001-6015-0359}
}