Zoltán Á. Nagy - Search Results

Year	Number of Results
2002	1
2003	2
2004	1
2006	1
2013	1
2016	1
2018	1
2019	1
2020	1
2022	3
2023	2
2024	1

1

Signals of Systemic Immunity in Plants: Progress and Open Questions.

Ádám AL, Nagy ZÁ, Kátay G, Mergenthaler E, Viczián O. Ádám AL, et al. Among authors: nagy za. Int J Mol Sci. 2018 Apr 10;19(4):1146. doi: 10.3390/ijms19041146. Int J Mol Sci. 2018. PMID: 29642641 Free PMC article. Review.

2

Substrate specificity of human chymotrypsin-like protease (CTRL) characterized by phage display-selected small-protein inhibitors.

Németh BZ, Nagy ZA, Kiss B, Gellén G, Schlosser G, Demcsák A, Geisz A, Hegyi E, Sahin-Tóth M, Pál G. Németh BZ, et al. Pancreatology. 2023 Sep;23(6):742-749. doi: 10.1016/j.pan.2023.08.004. Epub 2023 Aug 17. Pancreatology. 2023. PMID: 37604733 Free article.

3

A novel, alternative pathway of apoptosis triggered through class II major histocompatibility complex molecules.

Nagy ZA, Mooney NA. Nagy ZA, et al. J Mol Med (Berl). 2003 Dec;81(12):757-65. doi: 10.1007/s00109-003-0489-9. Epub 2003 Oct 9. J Mol Med (Berl). 2003. PMID: 14551703 Review.

4

Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.

Nagy ZA, Héja D, Bencze D, Kiss B, Boros E, Szakács D, Fodor K, Wilmanns M, Kocsis A, Dobó J, Gál P, Harmat V, Pál G. Nagy ZA, et al. J Biol Chem. 2022 Jun;298(6):101985. doi: 10.1016/j.jbc.2022.101985. Epub 2022 Apr 25. J Biol Chem. 2022. PMID: 35483450 Free PMC article.

5

Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides.

Dürvanger Z, Boros E, Nagy ZA, Hegedüs R, Megyeri M, Dobó J, Gál P, Schlosser G, Ángyán AF, Gáspári Z, Perczel A, Harmat V, Mező G, Menyhárd DK, Pál G. Dürvanger Z, et al. ACS Chem Biol. 2022 Apr 15;17(4):969-986. doi: 10.1021/acschembio.2c00114. Epub 2022 Apr 4. ACS Chem Biol. 2022. PMID: 35378038 Free PMC article.

6

Correction: Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation.

Nagy ZA, Héja D, Bencze D, Kiss B, Boros E, Szakács D, Fodor K, Wilmanns M, Kocsis A, Dobó J, Gál P, Harmat V, Pál G. Nagy ZA, et al. J Biol Chem. 2023 Jan;299(1):102807. doi: 10.1016/j.jbc.2022.102807. Epub 2022 Dec 21. J Biol Chem. 2023. PMID: 36563463 Free PMC article. No abstract available.

7

Ecotin, a microbial inhibitor of serine proteases, blocks multiple complement dependent and independent microbicidal activities of human serum.

Nagy ZA, Szakács D, Boros E, Héja D, Vígh E, Sándor N, Józsi M, Oroszlán G, Dobó J, Gál P, Pál G. Nagy ZA, et al. PLoS Pathog. 2019 Dec 20;15(12):e1008232. doi: 10.1371/journal.ppat.1008232. eCollection 2019 Dec. PLoS Pathog. 2019. PMID: 31860690 Free PMC article.

8

Genetic Diversity and Origins of the Homoploid-Type Hybrid Phytophthora ×alni.

Aguayo J, Halkett F, Husson C, Nagy ZÁ, Szigethy A, Bakonyi J, Frey P, Marçais B. Aguayo J, et al. Among authors: nagy za. Appl Environ Microbiol. 2016 Nov 21;82(24):7142-7153. doi: 10.1128/AEM.02221-16. Print 2016 Dec 15. Appl Environ Microbiol. 2016. PMID: 27736786 Free PMC article.

9

Second-generation peptidomimetic inhibitors of antigen presentation effectively treat autoimmune diseases in HLA-DR-transgenic mouse models.

Rosloniec EF, Brandstetter T, Leyer S, Schwaiger FW, Nagy ZA. Rosloniec EF, et al. Among authors: nagy za. J Autoimmun. 2006 Nov;27(3):182-95. doi: 10.1016/j.jaut.2006.09.005. Epub 2006 Nov 1. J Autoimmun. 2006. PMID: 17081730 Free PMC article.

10

Virulence Spectra of Hungarian Pyrenophora teres f. teres Isolates Collected from Experimental Fields Show Continuous Variation without Specific Isolate × Barley Differential Interactions.

Bakonyi J, Seress D, Nagy ZÁ, Csorba I, Cséplő M, Marton TA, Martin A, Mészáros K. Bakonyi J, et al. Among authors: nagy za. J Fungi (Basel). 2024 Feb 28;10(3):184. doi: 10.3390/jof10030184. J Fungi (Basel). 2024. PMID: 38535192 Free PMC article.

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