@article{MTMT:33699950,
	title = {Phosphorylated Peptide Derived from the Myosin Phosphatase Target Subunit Is a Novel Inhibitor of Protein Phosphatase-1},
	url = {https://m2.mtmt.hu/api/publication/33699950},
	author = {Kónya, Zoltán and Tamás, István and Bécsi, Bálint and Lontay, Beáta and Hadháziné Raics, Mária and Timári, István and E Kövér, Katalin and Erdődi, Ferenc},
	doi = {10.3390/ijms24054789},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33699950},
	issn = {1661-6596},
	abstract = {Identification of specific protein phosphatase-1 (PP1) inhibitors is of special importance regarding the study of its cellular functions and may have therapeutic values in diseases coupled to signaling processes. In this study, we prove that a phosphorylated peptide of the inhibitory region of myosin phosphatase (MP) target subunit (MYPT1), R690QSRRS(pT696)QGVTL701 (P-Thr696-MYPT1690−701), interacts with and inhibits the PP1 catalytic subunit (PP1c, IC50 = 3.84 µM) and the MP holoenzyme (Flag-MYPT1-PP1c, IC50 = 3.84 µM). Saturation transfer difference NMR measurements established binding of hydrophobic and basic regions of P-Thr696-MYPT1690−701 to PP1c, suggesting interactions with the hydrophobic and acidic substrate binding grooves. P-Thr696-MYPT1690−701 was dephosphorylated by PP1c slowly (t1/2 = 81.6–87.9 min), which was further impeded (t1/2 = 103 min) in the presence of the phosphorylated 20 kDa myosin light chain (P-MLC20). In contrast, P-Thr696-MYPT1690−701 (10–500 µM) slowed down the dephosphorylation of P-MLC20 (t1/2 = 1.69 min) significantly (t1/2 = 2.49–10.06 min). These data are compatible with an unfair competition mechanism between the inhibitory phosphopeptide and the phosphosubstrate. Docking simulations of the PP1c-P-MYPT1690−701 complexes with phosphothreonine (PP1c-P-Thr696-MYPT1690−701) or phosphoserine (PP1c-P-Ser696-MYPT1690−701) suggested their distinct poses on the surface of PP1c. In addition, the arrangements and distances of the surrounding coordinating residues of PP1c around the phosphothreonine or phosphoserine at the active site were distinct, which may account for their different hydrolysis rate. It is presumed that P-Thr696-MYPT1690−701 binds tightly at the active center but the phosphoester hydrolysis is less preferable compared to P-Ser696-MYPT1690−701 or phosphoserine substrates. Moreover, the inhibitory phosphopeptide may serve as a template to synthesize cell permeable PP1-specific peptide inhibitors.},
	keywords = {Molecular docking; saturation transfer difference NMR; protein phosphatase-1 (PP1); myosin phosphatase (MP); myosin phosphatase target subunit-1 (MYPT1); MYPT1 inhibitory peptide (P-Thr696-MYPT1690-701)},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Timári, István/0000-0003-0504-6967}
}

@article{MTMT:33554482,
	title = {A Fucosylated Lactose-Presenting Tetravalent Glycocluster Acting as a Mutual Ligand of Pseudomonas aeruginosa Lectins A (PA-IL) and B (PA-IIL)-Synthesis and Interaction Studies},
	url = {https://m2.mtmt.hu/api/publication/33554482},
	author = {Csávás, Magdolna and Kalmár, László and Szoke, Petronella and Farkas, László Bence and Bécsi, Bálint and Kónya, Zoltán and Kerékgyártó, János and Borbás, Anikó and Erdődi, Ferenc and E Kövér, Katalin},
	doi = {10.3390/ijms232416194},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {33554482},
	issn = {1661-6596},
	abstract = {The Gram-negative bacterium Pseudomonas aeruginosa is an important opportunistic human pathogen associated with cystic fibrosis. P. aeruginosa produces two soluble lectins, the d-galactose-specific lectin PA-IL (LecA) and the l-fucose-specific lectin PA-IIL (LecB), among other virulence factors. These lectins play an important role in the adhesion to host cells and biofilm formation. Moreover, PA-IL is cytotoxic to respiratory cells in the primary culture. Therefore, these lectins are promising therapeutic targets. Specifically, carbohydrate-based compounds could inhibit their activity. In the present work, a 3-O-fucosyl lactose-containing tetravalent glycocluster was synthesized and utilized as a mutual ligand of galactophilic and fucophilic lectins. Pentaerythritol equipped with azido ethylene glycol-linkers was chosen as a multivalent scaffold and the glycocluster was constructed by coupling the scaffold with propargyl 3-O-fucosyl lactoside using an azide-alkyne 1,3-dipolar cycloaddition reaction. The interactions between the glycocluster and PA-IL or PA-IIL were investigated by isothermal titration microcalorimetry and saturation transfer difference NMR spectroscopy. These results may assist in the development of efficient anti-adhesion therapy for the treatment of a P. aeruginosa infection.},
	keywords = {lectin; Pseudomonas aeruginosa; Multivalency; saturation transfer difference NMR; fucosylated lactose},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Borbás, Anikó/0000-0001-8462-4547}
}

@article{MTMT:32837061,
	title = {Epigallocatechine-3-gallate Inhibits the Adipogenesis of Human Mesenchymal Stem Cells via the Regulation of Protein Phosphatase-2A and Myosin Phosphatase},
	url = {https://m2.mtmt.hu/api/publication/32837061},
	author = {Bécsi, Bálint and Kónya, Zoltán and Boratkó, Anita and Kovács, Katalin and Erdődi, Ferenc},
	doi = {10.3390/cells11101704},
	journal-iso = {CELLS-BASEL},
	journal = {CELLS},
	volume = {11},
	unique-id = {32837061},
	year = {2022},
	eissn = {2073-4409}
}

@article{MTMT:32242201,
	title = {Smoothelin-like Protein 1 Regulates the Thyroid Hor-Mone-Induced Homeostasis and Remodeling of C2C12 Cells via the Modulation of Myosin Phosphatase},
	url = {https://m2.mtmt.hu/api/publication/32242201},
	author = {Major, Evelin and Keller, Ilka and Horváth, Dániel and Tamás, István and Erdődi, Ferenc and Lontay, Beáta},
	doi = {10.3390/ijms221910293},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {32242201},
	issn = {1661-6596},
	abstract = {The pathological elevation of the active thyroid hormone (T-3) level results in the manifestation of hyperthyroidism, which is associated with alterations in the differentiation and contractile function of skeletal muscle (SKM). Myosin phosphatase (MP) is a major cellular regulator that hydrolyzes the phosphoserine of phosphorylated myosin II light chain. MP consists of an MYPT1/2 regulatory and a protein phosphatase 1 catalytic subunit. Smoothelin-like protein 1 (SMTNL1) is known to inhibit MP by directly binding to MP as well as by suppressing the expression of MYPT1 at the transcriptional level. Supraphysiological vs. physiological concentration of T-3 were applied on C2C12 myoblasts and differentiated myotubes in combination with the overexpression of SMTNL1 to assess the role and regulation of MP under these conditions. In non-differentiated myoblasts, MP included MYPT1 in the holoenzyme complex and its expression and activity was regulated by SMTNL1, affecting the phosphorylation level of MLC20 assessed using semi-quantitative Western blot analysis. SMTNL1 negatively influenced the migration and cytoskeletal remodeling of myoblasts measured by high content screening. In contrast, in myotubes, the expression of MYPT2 but not MYPT1 increased in a T-3-dependent and SMTNL1-independent manner. T-3 treatment combined with SMTNL1 overexpression impeded the activity of MP. In addition, MP interacted with Na+/K+-ATPase and dephosphorylated its inhibitory phosphorylation sites, identifying this protein as a novel MP substrate. These findings may help us gain a better understanding of myopathy, muscle weakness and the disorder of muscle regeneration in hyperthyroid patients.},
	keywords = {Thyroid hormone; myogenesis; Na+/K+-ATPase; MYOSIN PHOSPHATASE; SMTNL1},
	year = {2021},
	eissn = {1422-0067}
}

@article{MTMT:31975664,
	title = {Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods},
	url = {https://m2.mtmt.hu/api/publication/31975664},
	author = {Gindele, Réka and Pénzes-Daku, Krisztina and Balogh, Gábor and Kállai, Judit and Kissné Bogáti, Réka and Bécsi, Bálint and Erdődi, Ferenc and Katona, Éva and Bereczky, Zsuzsanna},
	doi = {10.3390/biom11040544},
	journal-iso = {BIOMOLECULES},
	journal = {BIOMOLECULES},
	volume = {11},
	unique-id = {31975664},
	issn = {2218-273X},
	abstract = {Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin. Mutations at the heparin-binding region lead to functional defect, type II heparin-binding site (IIHBS) AT deficiency. The aim of this study was to investigate and compare the molecular background of AT Budapest 3 (p.Leu131Phe, ATBp3), AT Basel (p.Pro73Leu), and AT Padua (p.Arg79His) mutations. Advanced in silico methods and heparin-binding studies of recombinant AT proteins using surface plasmon resonance method were used. Crossed immunoelectrophoresis and Differential Scanning Fluorimetry (NanoDSF) were performed in plasma samples. Heparin affinity of AT Padua was the lowest (KD = 1.08 x 10(-6) M) and had the most severe consequences affecting the allosteric pathways of activation, moreover significant destabilizing effects on AT were also observed. KD values for AT Basel, ATBp3 and wild-type AT were 7.64 x 10(-7) M, 2.15 x 10(-8) M and 6.4 x 10(-10) M, respectively. Heparin-binding of AT Basel was slower, however once the complex was formed the mutation had only minor effect on the secondary and tertiary structures. Allosteric activation of ATBp3 was altered, moreover decreased thermostability in ATBp3 homozygous plasma and increased fluctuations in multiple regions of ATBp3 were observed by in silico methods suggesting the presence of a quantitative component in the pathogenicity of this mutation due to molecular instability.},
	year = {2021},
	eissn = {2218-273X},
	pages = {544},
	orcid-numbers = {Gindele, Réka/0000-0002-4145-3335; Pénzes-Daku, Krisztina/0000-0003-0334-7571; Katona, Éva/0000-0003-3476-794X; Bereczky, Zsuzsanna/0000-0002-1483-3703}
}

@article{MTMT:31936350,
	title = {Microcystin-LR, a cyanobacterial toxin affects root development by changing levels of PIN proteins and auxin response in Arabidopsis roots},
	url = {https://m2.mtmt.hu/api/publication/31936350},
	author = {Freytag, Csongor and Máthé, Csaba and Rigó, Gábor and Nodzyński, Tomasz and Kónya, Zoltán and Erdődi, Ferenc and Cséplő, Ágnes and Pózer, Erik and Szabados, László and Kelemen, Adrienn and Vasas, Gábor and Garda, Tamás},
	doi = {10.1016/j.chemosphere.2021.130183},
	journal-iso = {CHEMOSPHERE},
	journal = {CHEMOSPHERE},
	volume = {276},
	unique-id = {31936350},
	issn = {0045-6535},
	abstract = {Microcystin-LR (MCY-LR) is a heptapeptide toxin produced mainly by freshwater cyanobacteria. It strongly inhibits protein phosphatases PP2A and PP1. Functioning of the PIN family of auxin efflux carriers is crucial for plant ontogenesis and their functions depend on their reversible phosphorylation. We aimed to reveal the adverse effects of MCY-LR on PIN and auxin distribution in Arabidopsis roots and its consequences for root development.
		
		Relatively short-term (24 h) MCY-LR treatments decreased the levels of PIN1, PIN2 and PIN7, but not of PIN3 in tips of primary roots. In contrast, levels of PIN1 and PIN2 increased in emergent lateral roots and their levels depended on the type of PIN in lateral root primordia. DR5:GFP reporter activity showed that the cyanotoxin-induced decrease of auxin levels/responses in tips of main roots in parallel to PIN levels. Those alterations did not affect gravitropic response of roots. However, MCY-LR complemented the altered gravitropic response of crk5-1 mutants, defective in a protein kinase with essential role in the correct membrane localization of PIN2. For MCY-LR treated Col-0 plants, the number of lateral root primordia but not of emergent laterals increased and lateral root primordia showed early development. In conclusion, inhibition of protein phosphatase activities changed PIN and auxin levels, thus altered root development. Previous data on aquatic plants naturally co-occurring with the cyanotoxin showed similar alterations of root development. Thus, our results on the model plant Arabidopsis give a mechanistic explanation of MCY-LR phytotoxicity in aquatic ecosystems.},
	keywords = {ARABIDOPSIS; microcystin-LR; auxin; Root development; Protein phosphatase PP2A; PIN efflux Carrier},
	year = {2021},
	eissn = {1879-1298},
	orcid-numbers = {Freytag, Csongor/0000-0002-3356-4182; Pózer, Erik/0000-0001-7964-3583}
}

@article{MTMT:31899289,
	title = {Myosin Phosphatase Is Implicated in the Control of THP-1 Monocyte to Macrophage Differentiation},
	url = {https://m2.mtmt.hu/api/publication/31899289},
	author = {Tóth, Emese and Erdődi, Ferenc and Kiss, Andrea},
	doi = {10.3390/ijms22052516},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {31899289},
	issn = {1661-6596},
	year = {2021},
	eissn = {1422-0067},
	orcid-numbers = {Tóth, Emese/0000-0003-4519-6134; Kiss, Andrea/0000-0002-0664-5235}
}

@article{MTMT:31879368,
	title = {Activation of Myosin Phosphatase by Epigallocatechin-Gallate Sensitizes THP-1 Leukemic Cells to Daunorubicin},
	url = {https://m2.mtmt.hu/api/publication/31879368},
	author = {Tóth, Emese and Erdődi, Ferenc and Kiss, Andrea},
	doi = {10.2174/1871520620666200717142315},
	journal-iso = {ANTI-CANCER AGENT ME},
	journal = {ANTI-CANCER AGENTS IN MEDICINAL CHEMISTRY},
	volume = {21},
	unique-id = {31879368},
	issn = {1871-5206},
	abstract = {Background: The Myosin Phosphatase (MP) holoenzyme is composed of a Protein Phosphatase type 1 (PP1) catalytic subunit and a regulatory subunit termed Myosin Phosphatase Target subunit 1 (MYPT1). Besides dephosphorylation of myosin, MP has been implicated in the control of cell proliferation via dephosphorylation and activation of the tumor suppressor gene products, retinoblastoma protein (pRb) and merlin. Inhibition of MP was shown to attenuate the drug-induced cell death of leukemic cells by chemotherapeutic agents, while activation of MP might have a sensitizing effect.
		
		Objective: Recently, Epigallocatechin-Gallate (EGCG), a major component of green tea, was shown to activate MP by inducing the dephosphorylation of MYPT1 at phospho-Thr696 (MYPT1(pT696)), which might confer enhanced chemosensitivity to cancer cells.
		
		Methods: THP-1 leukemic cells were treated with EGCG and Daunorubicin (DNR) and cell viability was analyzed. Phosphorylation of tumor suppressor proteins was detected by Western blotting.
		
		Results: EGCG or DNR (at sub-lethal doses) alone had moderate effects on cell viability, while the combined treatment caused a significant decrease in the number of viable cells by enhancing apoptosis and decreasing proliferation. EGCG plus DNR decreased the phosphorylation level of MYPT1(pT696), which was accompanied by prominent dephosphorylation of pRb. In addition, significant dephosphorylation of merlin was observed when EGCG and DNR were applied together.
		
		Conclusion: Our results suggest that EGCG-induced activation of MP might have a regulatory function in mediating the chemosensitivity of leukemic cells via dephosphorylation of tumor suppressor proteins.},
	keywords = {EGCg; Retinoblastoma Protein; chemosensitivity; MYOSIN PHOSPHATASE; 37-KDA/67-KDA LAMININ RECEPTOR; MERLIN},
	year = {2021},
	eissn = {1875-5992},
	pages = {1092-1098},
	orcid-numbers = {Tóth, Emese/0000-0003-4519-6134; Erdődi, Ferenc/0000-0002-5277-3668; Kiss, Andrea/0000-0002-0664-5235}
}

@CONFERENCE{MTMT:33628739,
	title = {Effects of serine-threonine protein phosphatase inhibition and ROS induction on mitotic activity, cytoskeletal and chromatin organization in model higher plants},
	url = {https://m2.mtmt.hu/api/publication/33628739},
	author = {Máthé, Csaba and Garda, Tamás and Freytag, Csongor and Mikóné Hamvas, Márta and Kelemen, Adrienn and Kónya, Zoltán and Erdődi, Ferenc},
	booktitle = {11th International Botanical Microscopy Meeting : Presentation abstract},
	unique-id = {33628739},
	year = {2019},
	pages = {15.10-15.40-15.10-15.40},
	orcid-numbers = {Freytag, Csongor/0000-0002-3356-4182}
}

@article{MTMT:31936361,
	title = {30 éves a debreceni angol nyelvű orvosképzés},
	url = {https://m2.mtmt.hu/api/publication/31936361},
	author = {Erdődi, Ferenc and Matesz, Klára},
	doi = {10.29116/gerundium/2018/2/11},
	journal-iso = {GERUNDIUM},
	journal = {GERUNDIUM: EGYETEMTÖRTÉNETI KÖZLEMÉNYEK},
	volume = {9},
	unique-id = {31936361},
	issn = {2061-5132},
	year = {2019},
	eissn = {2061-7097},
	pages = {173-183}
}