@article{MTMT:35176626,
	title = {Novel method for detecting frequent TERT promoter hot spot mutations in bladder cancer samples.},
	url = {https://m2.mtmt.hu/api/publication/35176626},
	author = {Kovács, Ákos and Sükösd, Farkas and Kuthi, Levente and Boros, Imre Miklós and Vedelek, Balázs},
	doi = {10.1007/s10238-024-01464-3},
	journal-iso = {CLIN EXP MED},
	journal = {CLINICAL AND EXPERIMENTAL MEDICINE},
	volume = {24},
	unique-id = {35176626},
	issn = {1591-8890},
	abstract = {Telomerase reverse transcriptase promoter (TERTp) mutations are frequently targeted tumor markers, however, they reside in regions with high GC content, which poses challenges when examined with simple molecular techniques or even with next-generation sequencing (NGS). In bladder cancer (BC), TERTp mutations are particularly frequent, however, none of the available tools have demonstrated efficacy in detecting TERTp mutations via a simple noninvasive technique. Therefore, we developed a novel PCR-based method for the detection of the two most common TERTp mutations and demonstrated its use for the analysis of BC samples. The developed SHARD-PCR TERTp mutation detection technique requires PCR and restriction digestion steps that are easily implementable even in less well-equipped laboratories. Cell lines with known mutational status were utilized for method development. Matching urine and tumor tissue samples from BC patients were analyzed, and the results were validated by next-generation sequencing. Analysis of eighteen urine and corresponding tumor tissue samples by SHARD-PCR revealed perfect matches in sample pairs, which paralleled the corresponding NGS results: fourteen samples exhibited mutations at the -124 position, two samples showed mutations at the -146 position, and no mutations were detected in two samples. Our study serves as a proof-of-concept and is limited by its small sample size, nonetheless, it demonstrates that SHARD-PCR is a simple, economic and highly reliable method for detecting TERTp mutations, which are common in different cancer types. For bladder cancer, SHARD-PCR can be performed with the use of noninvasive samples and could replace or complement currently used techniques.},
	keywords = {bladder cancer; TELOMERASE; telomerase reverse transcriptase; novel method; TERTp mutations},
	year = {2024},
	eissn = {1591-9528},
	pages = {192},
	orcid-numbers = {Kuthi, Levente/0000-0001-9247-6679; Boros, Imre Miklós/0000-0001-8504-9687; Vedelek, Balázs/0000-0001-6981-0026}
}

@article{MTMT:34743202,
	title = {A bipartite NLS motif mediates the nuclear import of Drosophila moesin},
	url = {https://m2.mtmt.hu/api/publication/34743202},
	author = {Kovács, Zoltán and Bajusz, Csaba and Szabó, Anikó and Borkúti, Péter and Vedelek, Balázs and Benke, Reka and Lipinszki, Zoltán and Kristó, Ildikó and Vilmos, Péter},
	doi = {10.3389/fcell.2024.1206067},
	journal-iso = {FRONT CELL DEV BIOL},
	journal = {FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY},
	volume = {12},
	unique-id = {34743202},
	issn = {2296-634X},
	abstract = {The ERM protein family, which consists of three closely related proteins in vertebrates, ezrin, radixin, and moesin (ERM), is an ancient and important group of cytoplasmic actin-binding and organizing proteins. With their FERM domain, ERMs bind various transmembrane proteins and anchor them to the actin cortex through their C-terminal F-actin binding domain, thus they are major regulators of actin dynamics in the cell. ERMs participate in many fundamental cellular processes, such as phagocytosis, microvilli formation, T-cell activation and tumor metastasis. We have previously shown that, besides its cytoplasmic activities, the single ERM protein of Drosophila melanogaster, moesin, is also present in the cell nucleus, where it participates in gene expression and mRNA export. Here we study the mechanism by which moesin enters the nucleus. We show that the nuclear import of moesin is an NLS-mediated, active process. The nuclear localization sequence of the moesin protein is an evolutionarily highly conserved, conventional bipartite motif located on the surface of the FERM domain. Our experiments also reveal that the nuclear import of moesin does not require PIP2 binding or protein activation, and occurs in monomeric form. We propose, that the balance between the phosphorylated and non-phosphorylated protein pools determines the degree of nuclear import of moesin.},
	keywords = {PHOSPHORYLATION; BINDING; LOCALIZATION; IDENTIFICATION; NUCLEUS; STRUCTURAL BASIS; DROSOPHILA; CELL BIOLOGY; ERM PROTEINS; ezrin; moesin; CYTOPLASMIC TAIL; ERM; PIP2; importin; MERLIN; LINKS ACTIN},
	year = {2024},
	eissn = {2296-634X},
	orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026; Lipinszki, Zoltán/0000-0002-2067-0832}
}

@article{MTMT:34334193,
	title = {Biofilm formation initiating rotifer-specific biopolymer and its predicted components},
	url = {https://m2.mtmt.hu/api/publication/34334193},
	author = {Datki, Zsolt László and Darula, Zsuzsanna and Vedelek, Viktor and Hunyadi-Gulyás Éva, Csilla and Dingmann, Brian J. and Vedelek, Balázs and Kalman, Janos and Urbán, Péter and Gyenesei, Attila and Galik-Olah, Zita and Gálik, Bence and Sinka, Rita},
	doi = {10.1016/j.ijbiomac.2023.127157},
	journal-iso = {INT J BIOL MACROMOL},
	journal = {INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES},
	volume = {253},
	unique-id = {34334193},
	issn = {0141-8130},
	abstract = {The rotifer-specific biopolymer, namely Rotimer, is a recently discovered group of the biomolecule family. Rotimer has an active role in the biofilm formation initiated by rotifers (e.g., Euchlanis dilatata or Adineta vaga) or in the female-male sexual interaction of monogononts. To understand the Ca2+- and polarity-dependent formation of this multifunctional viscoelastic material, it is essential to explore its molecular composition. The investigation of the rotifer-enhanced biofilm and Rotimer-inductor conglomerate (RIC) formation yielded several protein candidates to predict the Rotimer-specific main components. The exudate of E. dilatata males was primarily applied from different biopolimer-containing samples (biofilm or RIC). The advantage of males over females lies in their degenerated digestive system and simple anatomy. Thus, their exudate is less contaminated with food and endosymbiont elements. The sequenced and annotated genome and transcriptome of this species opened the way for identifying Rotimer proteins by mass spectrometry. The predicted rotifer-biopolymer forming components are SCO-spondins and 14-3-3 protein. The characteristics of Rotimer are similar to Reissner's fiber, which is found in the central nervous system of vertebrates and is mainly formed from SCO-spondins. This molecular information serves as a starting point for its interdisciplinary investigation and application in biotechnology, biomedicine, or neurodegeneration-related drug development.},
	keywords = {IN-VIVO; PROTEINS; 14-3-3 PROTEIN; ANTIBODY; Biofilm; Ecotoxicology; Clearance; Chemistry, Applied; Biochemistry & Molecular Biology; Rotimer; SCO-spondin},
	year = {2023},
	eissn = {1879-0003},
	orcid-numbers = {Datki, Zsolt László/0000-0002-2537-4741; Vedelek, Balázs/0000-0001-6981-0026; Sinka, Rita/0000-0003-4040-4184}
}

@article{MTMT:34239207,
	title = {A comparative analysis of fruit fly and human glutamate dehydrogenases in Drosophila melanogaster sperm development},
	url = {https://m2.mtmt.hu/api/publication/34239207},
	author = {Vedelek, Viktor and Vedelek, Balázs and Lőrincz, Péter and Juhász, Gábor and Sinka, Rita},
	doi = {10.3389/fcell.2023.1281487},
	journal-iso = {FRONT CELL DEV BIOL},
	journal = {FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY},
	volume = {11},
	unique-id = {34239207},
	issn = {2296-634X},
	abstract = {Glutamate dehydrogenases are enzymes that take part in both amino acid and energy metabolism. Their role is clear in many biological processes, from neuronal function to cancer development. The putative testis-specific Drosophila glutamate dehydrogenase, Bb8, is required for male fertility and the development of mitochondrial derivatives in spermatids. Testis-specific genes are less conserved and could gain new functions, thus raising a question whether Bb8 has retained its original enzymatic activity. We show that while Bb8 displays glutamate dehydrogenase activity, there are significant functional differences between the housekeeping Gdh and the testis-specific Bb8. Both human GLUD1 and GLUD2 can rescue the bb8 ms mutant phenotype, with superior performance by GLUD2. We also tested the role of three conserved amino acids observed in both Bb8 and GLUD2 in Gdh mutants, which showed their importance in the glutamate dehydrogenase function. The findings of our study indicate that Drosophila Bb8 and human GLUD2 could be novel examples of convergent molecular evolution. Furthermore, we investigated the importance of glutamate levels in mitochondrial homeostasis during spermatogenesis by ectopic expression of the mitochondrial glutamate transporter Aralar1, which caused mitochondrial abnormalities in fly spermatids. The data presented in our study offer evidence supporting the significant involvement of glutamate metabolism in sperm development.},
	year = {2023},
	eissn = {2296-634X},
	orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026; Lőrincz, Péter/0000-0001-7374-667X; Juhász, Gábor/0000-0001-8548-8874; Sinka, Rita/0000-0003-4040-4184}
}

@article{MTMT:32517518,
	title = {Evolutionary mode for the functional preservation of fast-evolving Drosophila telomere capping proteins},
	url = {https://m2.mtmt.hu/api/publication/32517518},
	author = {Vedelek, Balázs and Kovács, Ákos and Boros, Imre Miklós},
	doi = {10.1098/rsob.210261},
	journal-iso = {OPEN BIOL},
	journal = {OPEN BIOLOGY},
	volume = {11},
	unique-id = {32517518},
	abstract = {DNA end protection is fundamental for the long-term preservation of the genome. In vertebrates the Shelterin protein complex protects telomeric DNA ends, thereby contributing to the maintenance of genome integrity. In the Drosophila genus, this function is thought to be performed by the Terminin complex, an assembly of fast-evolving subunits. Considering that DNA end protection is fundamental for successful genome replication, the accelerated evolution of Terminin subunits is counterintuitive, as conservation is supposed to maintain the assembly and concerted function of the interacting partners. This problem extends over Drosophila telomere biology and provides insight into the evolution of protein assemblies. In order to learn more about the mechanistic details of this phenomenon we have investigated the intra- and interspecies assemblies of Verrocchio and Modigliani, two Terminin subunits using in vitro assays. Based on our results and on homology-based three-dimensional models for Ver and Moi, we conclude that both proteins contain Ob-fold and contribute to the ssDNA binding of the Terminin complex. We propose that the preservation of Ver function is achieved by conservation of specific amino acids responsible for folding or localized in interacting surfaces. We also provide here the first evidence on Moi DNA binding.},
	keywords = {IDENTIFICATION; GENES; PREDICTION; SINGLE-STRANDED-DNA; POSITIVE SELECTION; Verrocchio; OB-FOLD; Retrotransposons; Fast evolution; shelterin; VÉR; terminin; MOI; HOAP},
	year = {2021},
	eissn = {2046-2441},
	orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:31677445,
	title = {TERT promoter alterations could provide a solution for Peto’s paradox in rodents},
	url = {https://m2.mtmt.hu/api/publication/31677445},
	author = {Vedelek, Balázs and Maddali, Asha Kiran and Davenova, Nurgul and Vedelek, Viktor and Boros, Imre Miklós},
	doi = {10.1038/s41598-020-77648-0},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {10},
	unique-id = {31677445},
	year = {2020},
	eissn = {2045-2322},
	orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026; Boros, Imre Miklós/0000-0001-8504-9687}
}

@article{MTMT:31397830,
	title = {Alternative linker histone permits fast paced nuclear divisions in early Drosophila embryo},
	url = {https://m2.mtmt.hu/api/publication/31397830},
	author = {Henn, László and Szabó, Anikó and Imre, László and Román, Ádám and Ábrahám, Andrea and Vedelek, Balázs and Nánási, Péter Pál and Boros, Imre Miklós},
	doi = {10.1093/nar/gkaa624},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {48},
	unique-id = {31397830},
	issn = {0305-1048},
	abstract = {In most animals, the start of embryogenesis requires specific histones. In Drosophila linker histone variant BigH1 is present in early embryos. To uncover the specific role of this alternative linker histone at early embryogenesis, we established fly lines in which domains of BigH1 have been replaced partially or completely with that of H1. Analysis of the resulting Drosophila lines revealed that at normal temperature somatic H1 can substitute the alternative linker histone, but at low temperature the globular and C-terminal domains of BigH1 are essential for embryogenesis. In the presence of BigH1 nucleosome stability increases and core histone incorporation into nucleosomes is more rapid, while nucleosome spacing is unchanged. Chromatin formation in the presence of BigH1 permits the fast-paced nuclear divisions of the early embryo. We propose a model which explains how this specific linker histone ensures the rapid nucleosome reassembly required during quick replication cycles at the start of embryogenesis.},
	year = {2020},
	eissn = {1362-4962},
	pages = {9007-9018},
	orcid-numbers = {Román, Ádám/0000-0003-2007-3269; Vedelek, Balázs/0000-0001-6981-0026; Boros, Imre Miklós/0000-0001-8504-9687}
}

@book{MTMT:30969581,
	title = {Macromolecule design and manipulation - practical textbook},
	url = {https://m2.mtmt.hu/api/publication/30969581},
	author = {Borsos, Barbara Nikolett and Vedelek, Balázs},
	editor = {Boros, Imre Miklós},
	publisher = {Szegedi Tudományegyetem},
	unique-id = {30969581},
	year = {2018},
	orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026; Boros, Imre Miklós/0000-0001-8504-9687}
}

@{MTMT:3415003,
	title = {A possible mechanism explaining the telomerase promoter inactivation in mammalian somatic cells},
	url = {https://m2.mtmt.hu/api/publication/3415003},
	author = {Vedelek, Balázs and Asha, Maddali Kiran and Boros, Imre Miklós},
	booktitle = {FEBS3+: From molecules to living systems},
	unique-id = {3415003},
	year = {2018},
	pages = {68-68},
	orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026; Boros, Imre Miklós/0000-0001-8504-9687}
}

@mastersthesis{MTMT:3267993,
	title = {A Drosophila telomer védelmét szolgáló fehérjék fajképzésben betöltött lehetséges szerepének vizsgálata},
	url = {https://m2.mtmt.hu/api/publication/3267993},
	author = {Vedelek, Balázs},
	doi = {10.14232/phd.3926},
	publisher = {SZTE},
	unique-id = {3267993},
	year = {2017},
	orcid-numbers = {Vedelek, Balázs/0000-0001-6981-0026}
}