@{MTMT:34560558,
	title = {Hibalehetőségek az analitikus obszervációs tanulmányok tervezése és kivitelezése során; a hibák csökkentésének módszerei},
	url = {https://m2.mtmt.hu/api/publication/34560558},
	author = {Bereczky, Zsuzsanna and Muszbek, László},
	booktitle = {Klinikai kutatások - átfogó ismeretek a tervezéstől a közlésig},
	unique-id = {34560558},
	year = {2024},
	pages = {73-84},
	orcid-numbers = {Bereczky, Zsuzsanna/0000-0002-1483-3703; Muszbek, László/0000-0002-3798-9962}
}

@article{MTMT:33683540,
	title = {Cellular FXIII in Human Macrophage-Derived Foam Cells},
	url = {https://m2.mtmt.hu/api/publication/33683540},
	author = {Somodi, Laura and Horváth, Emőke and Bárdos, Helga and Baráth, Barbara and Pethő, Dávid and Katona, Éva and Balla, József and Mutch, Nicola J. and Muszbek, László},
	doi = {10.3390/ijms24054802},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33683540},
	issn = {1661-6596},
	abstract = {Macrophages express the A subunit of coagulation factor XIII (FXIII-A), a transglutaminase which cross-links proteins through Nε-(γ-L-glutamyl)-L-lysyl iso-peptide bonds. Macrophages are major cellular constituents of the atherosclerotic plaque; they may stabilize the plaque by cross-linking structural proteins and they may become transformed into foam cells by accumulating oxidized LDL (oxLDL). The combination of oxLDL staining by Oil Red O and immunofluorescent staining for FXIII-A demonstrated that FXIII-A is retained during the transformation of cultured human macrophages into foam cells. ELISA and Western blotting techniques revealed that the transformation of macrophages into foam cells elevated the intracellular FXIII-A content. This phenomenon seems specific for macrophage-derived foam cells; the transformation of vascular smooth muscle cells into foam cells fails to induce a similar effect. FXIII-A containing macrophages are abundant in the atherosclerotic plaque and FXIII-A is also present in the extracellular compartment. The protein cross-linking activity of FXIII-A in the plaque was demonstrated using an antibody labeling the iso-peptide bonds. Cells showing combined staining for FXIII-A and oxLDL in tissue sections demonstrated that FXIII-A-containing macrophages within the atherosclerotic plaque are also transformed into foam cells. Such cells may contribute to the formation of lipid core and the plaque structurization.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Somodi, Laura/0000-0002-3210-7430; Pethő, Dávid/0000-0001-7549-5691; Katona, Éva/0000-0003-3476-794X; Mutch, Nicola J./0000-0002-7452-0813; Muszbek, László/0000-0002-3798-9962}
}

@article{MTMT:33532648,
	title = {KESZTYŰS LÓRÁND KÓRÉLETTAN PROFESSZOR, AZ 1951-BEN FÜGGETLENNÉ VÁLT DEBRECENI ORVOSTUDOMÁNYI EGYETEMNEK DÉKÁNKÉNT ELSŐ VEZETŐJE, MAJD KÉTSZER (1959-1963, 1967-1973) ANNAK REKTORA.},
	url = {https://m2.mtmt.hu/api/publication/33532648},
	author = {Csaba, Béla and Sipka, Sándor and Muszbek, László and Fésüs, László},
	doi = {10.29116/gerundium/2022/3-4/2},
	journal-iso = {GERUNDIUM},
	journal = {GERUNDIUM: EGYETEMTÖRTÉNETI KÖZLEMÉNYEK},
	volume = {13},
	unique-id = {33532648},
	issn = {2061-5132},
	year = {2022},
	eissn = {2061-7097},
	pages = {22-53},
	orcid-numbers = {Muszbek, László/0000-0002-3798-9962}
}

@article{MTMT:32879331,
	title = {The Effect of Activated FXIII, a Transglutaminase, on Vascular Smooth Muscle Cells},
	url = {https://m2.mtmt.hu/api/publication/32879331},
	author = {Kissné Bogáti, Réka and Katona, Éva and Shemirani, Amir Houshang and Balogh, Enikő and Bárdos, Helga and Jeney, Viktória and Muszbek, László},
	doi = {10.3390/ijms23105845},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {32879331},
	issn = {1661-6596},
	abstract = {Plasma factor XIII (pFXIII) is a heterotetramer of FXIII-A and FXIII-B subunits. The cellular form (cFXIII), a dimer of FXIII-A, is present in a number of cell types. Activated FXIII (FXIIIa), a transglutaminase, plays an important role in clot stabilization, wound healing, angiogenesis and maintenance of pregnancy. It has a direct effect on vascular endothelial cells and fibroblasts, which have been implicated in the development of atherosclerotic plaques. Our aim was to explore the effect of FXIIIa on human aortic smooth muscle cells (HAoSMCs), another major cell type in the atherosclerotic plaque. Osteoblastic transformation induced by Pi and Ca2+ failed to elicit the expression of cFXIII in HAoSMCs. EZ4U, CCK-8 and CytoSelect Wound Healing assays were used to investigate cell proliferation and migration. The Sircol Collagen Assay Kit was used to monitor collagen secretion. Thrombospondin-1 (TSP-1) levels were measured by ELISA. Cell-associated TSP-1 was detected by the immunofluorescence technique. The TSP-1 mRNA level was estimated by RT-qPCR. Activated recombinant cFXIII (rFXIIIa) increased cell proliferation and collagen secretion. In parallel, a 67% decrease in TSP-1 concentration in the medium and a 2.5-fold increase in cells were observed. TSP-1 mRNA did not change significantly. These effects of FXIIIa might contribute to the pathogenesis of atherosclerotic plaques.},
	keywords = {cell proliferation; Factor XIII; vascular smooth muscle cell; thrombospondin-1; Collagen secretion},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Katona, Éva/0000-0003-3476-794X; Muszbek, László/0000-0002-3798-9962}
}

@article{MTMT:32841642,
	title = {Activation mechanism dependent surface exposure of cellular factor XIII on activated platelets and platelet microparticles},
	url = {https://m2.mtmt.hu/api/publication/32841642},
	author = {Somodi, Laura and Bekéné Debreceni, Ildikó and Kis, Nikoletta Gréta and Cozzolino, Marco and Kappelmayer, János and Antal, Miklós and Panyi, György and Bárdos, Helga and Mutch, Nicola J. and Muszbek, László},
	doi = {10.1111/jth.15668},
	journal-iso = {J THROMB HAEMOST},
	journal = {JOURNAL OF THROMBOSIS AND HAEMOSTASIS},
	volume = {20},
	unique-id = {32841642},
	issn = {1538-7933},
	abstract = {Background Platelets contain a high amount of potentially active A subunit dimer of coagulation factor XIII (cellular FXIII; cFXIII). It is of cytoplasmic localization, not secreted, but becomes translocated to the surface of platelets activated by convulxin and thrombin (CVX+Thr). Objective To explore the difference in cFXIII translocation between receptor mediated and non-receptor mediated platelet activation and if translocation can also be detected on platelet-derived microparticles. Our aim was also to shed some light on the mechanism of cFXIII translocation. Methods Gel-filtered platelets were activated by CVX+Thr or Ca2+-ionophore (calcimycin). The translocation of cFXIII and phosphatidylserine (PS) to the surface of activated platelets and platelet-derived microparticles was investigated by flow cytometry, immunofluorescence, and immune electron microscopy. Fluo-4-AM fluorescence was used for the measurement of intracellular Ca2+ concentration. Results Receptor mediated activation by CVX+Thr exposed cFXIII to the surface of more than 60% of platelets. Electron microscopy revealed microparticles with preserved membrane structure and microparticles devoid of labeling for membrane glycoprotein CD41a. cFXIII was observed on both types of microparticles but was more abundant in the absence of CD41a. Rhosin, a RhoA inhibitor, significantly decreased cFXIII translocation. Non-receptor mediated activation of platelets by calcimycin elevated intracellular Ca2+ concentration, induced the translocation of PS to the surface of platelets and microparticles, but failed to expose cFXIII. Conclusions The elevation of intracellular Ca2+ concentration is sufficient for the translocation of PS from the internal layer of the membrane, while the translocation of cFXIII from the platelet cytoplasm requires additional receptor mediated mechanism(s).},
	keywords = {Flow Cytometry; platelet activation; Factor XIII; Cell-Derived Microparticles; immune electron microscopy},
	year = {2022},
	eissn = {1538-7836},
	pages = {1223-1235},
	orcid-numbers = {Somodi, Laura/0000-0002-3210-7430; Panyi, György/0000-0001-6227-3301; Muszbek, László/0000-0002-3798-9962}
}

@article{MTMT:32531612,
	title = {An international collaborative study to assign value for Total Factor XIII-B Subunit Antigen to the WHO 1st International Standard for Factor XIII Plasma, (02/206): Communication from the ISTH SSC Subcommittee on Factor XIII and Fibrinogen},
	url = {https://m2.mtmt.hu/api/publication/32531612},
	author = {Raut, Sanj and Katona, Éva and Riches-Duit, Andrew and Coxon, Carmen and Muszbek, László and Schroeder, Verena and Rigsby, Peter},
	doi = {10.1111/jth.15596},
	journal-iso = {J THROMB HAEMOST},
	journal = {JOURNAL OF THROMBOSIS AND HAEMOSTASIS},
	volume = {20},
	unique-id = {32531612},
	issn = {1538-7933},
	abstract = {Background Factor XIII (FXIII)-B subunit measurements are required for the diagnosis and characterization of the type of FXIII deficiency. Furthermore, therapy for FXIII-A deficiency with recombinant FXIII (rFXIII-A) relies on available FXIII-B. Objective To carry out a collaborative study to calibrate and assign value to the current WHO 1st International Standard (IS) FXIII Plasma for Total FXIII-B subunit, relative to locally collected normal plasma pools. Methods Laboratories were instructed to use a validated method (specific ELISA antibodies provided) for assessment of Total FXIII-B subunit antigen potency. All laboratories used this method with one laboratory using an additional in-house method. Nine data sets were received from seven laboratories (37 assays in total), which provided a total of 35 valid estimates for this new assignment. Total FXIII-B subunit estimates were calculated relative to locally collected normal plasma pools, using an arbitrary value of 1.00 unit of Total FXIII-B subunit per ml, for each pool. Results Combination of results produced an overall mean of 0.98 units/mL with an inter-laboratory variability (geometric coefficients of variation - GCV%) of 18.3% [95% confidence interval: 0.86-1.11]. Real-time and bench stability studies indicated good stability and preservation of the FXIII-B subunit analyte in the WHO 1st IS FXIII Plasma (02/206). Conclusion Following agreement by study participants, ISTH/SSC Experts, WHO-ISTH Liaison Group and the SSC Board, the WHO/ECBS established the current WHO 1st IS Factor XIII plasma (NIBSC code 02/206) by additionally assigning it with a Total FXIII-B subunit antigen value of 0.98 IU/ampoule, in October 2019.},
	keywords = {monoclonal antibody; Factor XIII; FXIII-B subunit; International Unit; WHO International Standard},
	year = {2022},
	eissn = {1538-7836},
	pages = {525-531},
	orcid-numbers = {Raut, Sanj/0000-0001-5896-2569; Katona, Éva/0000-0003-3476-794X; Riches-Duit, Andrew/0000-0002-9413-8558; Coxon, Carmen/0000-0001-8694-4894; Muszbek, László/0000-0002-3798-9962; Rigsby, Peter/0000-0002-8954-9475}
}

@article{MTMT:32218883,
	title = {Genetic Background of Inherited Factor XIII-A Subunit Deficiency: Review of the Literature and Description of Two New Cases},
	url = {https://m2.mtmt.hu/api/publication/32218883},
	author = {Plamenova, Ivana and Zolkova, Jana and Sokol, Juraj and Kolkova, Zuzana and Bereczky, Zsuzsanna and Katona, Éva and Muszbek, László and Kubisz, Peter and Stasko, Jan},
	doi = {10.1055/s-0041-1725170},
	journal-iso = {SEMIN THROMB HEMOST},
	journal = {SEMINARS IN THROMBOSIS AND HEMOSTASIS},
	volume = {47},
	unique-id = {32218883},
	issn = {0094-6176},
	year = {2021},
	eissn = {1098-9064},
	pages = {885-889},
	orcid-numbers = {Bereczky, Zsuzsanna/0000-0002-1483-3703; Katona, Éva/0000-0003-3476-794X; Muszbek, László/0000-0002-3798-9962}
}

@article{MTMT:32015002,
	title = {Effect of α2-plasmin inhibitor heterogeneity on the risk of venous thromboembolism},
	url = {https://m2.mtmt.hu/api/publication/32015002},
	author = {Baráth, Barbara and Kissné Bogáti, Réka and Miklós, Tünde and Kállai, Judit and Mezei, Zoltán András and Bereczky, Zsuzsanna and Muszbek, László and Katona, Éva},
	doi = {10.1016/j.thromres.2021.05.003},
	journal-iso = {THROMB RES},
	journal = {THROMBOSIS RESEARCH},
	volume = {203},
	unique-id = {32015002},
	issn = {0049-3848},
	year = {2021},
	eissn = {1879-2472},
	pages = {110-116},
	orcid-numbers = {Mezei, Zoltán András/0000-0002-7886-8665; Bereczky, Zsuzsanna/0000-0002-1483-3703; Muszbek, László/0000-0002-3798-9962; Katona, Éva/0000-0003-3476-794X}
}

@article{MTMT:31676571,
	title = {Terminal Phase Components of the Clotting Cascade in Patients with End-Stage Renal Disease Undergoing Hemodiafiltration or Hemodialysis Treatment.},
	url = {https://m2.mtmt.hu/api/publication/31676571},
	author = {Pénzes-Daku, Krisztina and Hurják, Boglárka and Katona, Éva and Becs, Gergely and Balla, József and Muszbek, László},
	doi = {10.3390/ijms21228426},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {21},
	unique-id = {31676571},
	issn = {1661-6596},
	abstract = {Hemostasis disorder in patients with end-stage renal disease (ESRD) is frequently associated with bleeding diathesis but it may also manifest in thrombotic complications. Analysis of individual coagulation and fibrinolytic factors may shed light on the background of this paradox situation. Here we explored components essential for fibrin formation/stabilization in ESRD patients being on maintenance hemodiafiltration (HDF) or hemodialysis (HD). Pre-dialysis fibrinogen, factor XIII (FXIII) antigen concentrations and FXIII activity were elevated, while α2-plasmin inhibitor (α2PI) activity decreased. The inflammatory status, as characterized by C-reactive protein (CRP) was a key determinant of fibrinogen concentration, but not of FXIII and α2PI levels. During a 4-h course of HDF or HD, fibrinogen concentration and FXIII levels gradually elevated. When compensated for the change in plasma water, i.e., normalized for plasma albumin concentration, only FXIII elevation remained significant. There was no difference between HDF and HD treatments. Individual HDF treatment did not influence α2PI activity, however after normalization it decreased significantly. HD treatment had a different effect, α2PI activities became elevated but the elevation disappeared after normalization. Elevated fibrinogen and FXIII levels in ESRD patients might contribute to the increased thrombosis risk, while decreased α2PI activity might be associated with elevated fibrinolytic potential.},
	keywords = {FIBRINOGEN; hemodialysis; hemodiafiltration; Factor XIII; End-stage renal disease; α2-plasmin inhibitor},
	year = {2020},
	eissn = {1422-0067},
	orcid-numbers = {Pénzes-Daku, Krisztina/0000-0003-0334-7571; Katona, Éva/0000-0003-3476-794X; Muszbek, László/0000-0002-3798-9962}
}

@article{MTMT:31335055,
	title = {Autoimmune factor XIII deficiency with unusual laboratory and clinical phenotype},
	url = {https://m2.mtmt.hu/api/publication/31335055},
	author = {Bovet, Julien and Hurják, Boglárka and De Maistre, Emmanuel and Katona, Éva and Pénzes-Daku, Krisztina and Muszbek, László},
	doi = {10.1111/jth.14811},
	journal-iso = {J THROMB HAEMOST},
	journal = {JOURNAL OF THROMBOSIS AND HAEMOSTASIS},
	volume = {18},
	unique-id = {31335055},
	issn = {1538-7933},
	year = {2020},
	eissn = {1538-7836},
	pages = {1330-1334},
	orcid-numbers = {Katona, Éva/0000-0003-3476-794X; Pénzes-Daku, Krisztina/0000-0003-0334-7571; Muszbek, László/0000-0002-3798-9962}
}