@article{MTMT:34819821,
	title = {In situ captured antibacterial action of membrane-incising peptide lamellae},
	url = {https://m2.mtmt.hu/api/publication/34819821},
	author = {el Battioui, Kamal and Chakraborty, Sohini and Wacha, András and Molnár, Dániel and Quemé-Peña, Mayra and Szigyártó, Imola Cs. and Szabó, Csenge Lilla and Bodor, Andrea and Horváti, Kata and Gyulai, Gergő and Bősze, Szilvia and Mihály, Judith and Jezsó, Bálint and Románszki, Loránd and Tóth, Judit and Varga, Zoltán and Mándity, István and Juhász, Tünde and Beke-Somfai, Tamás},
	doi = {10.1038/s41467-024-47708-4},
	journal-iso = {NAT COMMUN},
	journal = {NATURE COMMUNICATIONS},
	volume = {15},
	unique-id = {34819821},
	issn = {2041-1723},
	abstract = {Developing unique mechanisms of action are essential to combat the growing issue of antimicrobial resistance. Supramolecular assemblies combining the improved biostability of non-natural compounds with the complex membrane-attacking mechanisms of natural peptides are promising alternatives to conventional antibiotics. However, for such compounds the direct visual insight on antibacterial action is still lacking. Here we employ a design strategy focusing on an inducible assembly mechanism and utilized electron microscopy (EM) to follow the formation of supramolecular structures of lysine-rich heterochiral β 3 -peptides, termed lamellin-2K and lamellin-3K, triggered by bacterial cell surface lipopolysaccharides. Combined molecular dynamics simulations, EM and bacterial assays confirmed that the phosphate-induced conformational change on these lamellins led to the formation of striped lamellae capable of incising the cell envelope of Gram-negative bacteria thereby exerting antibacterial activity. Our findings also provide a mechanistic link for membrane-targeting agents depicting the antibiotic mechanism derived from the in-situ formation of active supramolecules.},
	year = {2024},
	eissn = {2041-1723},
	orcid-numbers = {Wacha, András/0000-0002-9609-0893; Szabó, Csenge Lilla/0000-0002-6508-3439; Bodor, Andrea/0000-0002-7422-298X; Gyulai, Gergő/0000-0002-1352-2014; Jezsó, Bálint/0000-0002-1306-4797; Románszki, Loránd/0000-0002-6347-5228; Tóth, Judit/0000-0002-0965-046X; Varga, Zoltán/0000-0002-5741-2669; Mándity, István/0000-0003-2865-6143; Beke-Somfai, Tamás/0000-0002-4788-3758}
}

@article{MTMT:34724516,
	title = {A GFP inspired 8-methoxyquinoline-derived fluorescent molecular sensor for the detection of Zn2+ by two-photon microscopy},
	url = {https://m2.mtmt.hu/api/publication/34724516},
	author = {Csomos, Attila and Madarász, Miklós and Turczel, Gábor and Cseri, Levente and Bodor, Andrea and Anett, Matuscsák and Katona, Gergely and Kovács, Ervin and Rózsa J., Balázs and Mucsi, Zoltán},
	doi = {10.1002/chem.202400009},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	unique-id = {34724516},
	issn = {0947-6539},
	abstract = {An effective, GFP-inspired fluorescent Zn2+ sensor is developed for two-photon microscopy and related biological application that featured an 8-methoxyquinoline moiety. Excellent photophysical characteristics including a 37-fold fluorescence enhancement with excitation and emission maxima at 440 nm and 505 nm, respectively, as well as a high two-photon cross-section of 73 GM at 880 nm are reported. Based on the experimental data, the relationship between the structure and properties was elucidated and explained backed up by DFT calculations, particularly to the observed PeT phenomenon for the turn-on process. Biological validation and detailed experimental and theoretical characterization of the free and the zinc-bound compounds are presented.},
	year = {2024},
	eissn = {1521-3765},
	orcid-numbers = {Madarász, Miklós/0000-0001-7057-303X; Bodor, Andrea/0000-0002-7422-298X; Katona, Gergely/0000-0002-4173-0355; Kovács, Ervin/0000-0002-3939-6925; Mucsi, Zoltán/0000-0003-3224-8847}
}

@CONFERENCE{MTMT:34236962,
	title = {A rendezetlen fehérjék és az NMR spektroszkópia},
	url = {https://m2.mtmt.hu/api/publication/34236962},
	author = {Sebák, Fanni and Szabó, Csenge Lilla and Ecsédi, Péter and Burkhard, LUY and Nyitray, László and Bodor, Andrea},
	booktitle = {XXIX. Nemzetközi Vegyészkonferencia / 29th International Conference on Chemistry},
	unique-id = {34236962},
	year = {2023},
	pages = {1-2},
	orcid-numbers = {Sebák, Fanni/0000-0001-9252-9961; Szabó, Csenge Lilla/0000-0002-6508-3439; Ecsédi, Péter/0000-0002-4700-125X; Nyitray, László/0000-0003-4717-5994; Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:34213192,
	title = {Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein using 1HN and 1Hα-detected NMR measurements},
	url = {https://m2.mtmt.hu/api/publication/34213192},
	author = {Sebák, Fanni and Ecsédi, Péter and Nyitray, László and Bodor, Andrea},
	doi = {10.1007/s12104-023-10160-4},
	journal-iso = {BIOMOL NMR ASSIGM},
	journal = {BIOMOLECULAR NMR ASSIGNMENTS},
	volume = {17},
	unique-id = {34213192},
	issn = {1874-2718},
	abstract = {Protein p53 is mostly known for playing a key role in tumour suppression, and mutations in the p53 gene are amongst the most frequent genomic events accompanying oncogenic transformation. Continuous research is conducted to target disordered proteins/protein regions for cancer therapy, for which atomic level information is also necessary. The disordered N-terminal part of p53 contains the transactivation and the proline-rich domains—which besides being abundant in proline residues—contains repetitive Pro-Ala motifs. NMR assignment of such repetitive, proline-rich regions is challenging due to the lack of amide protons in the 1 H N -detected approaches, as well as due to the small chemical shift dispersion. In the present study we perform the full assignment of the p53 1–100 region by applying a combination of 1 H N - and 1 H α -detected NMR experiments. We also show the increased information content when using real-time homo- and heteronuclear decoupled acquisition schemes. On the other hand, we highlight the presence of minor proline species, and using Pro-selective experiments we determine the corresponding cis or trans conformation. Secondary chemical shifts for (C α –C β ) atoms indicate the disordered nature of this region, with expected helical tendency for the TAD1 region. As the role of the proline-rich domain is yet not well understood our results can contribute to further successful investigations.},
	year = {2023},
	eissn = {1874-270X},
	pages = {309-314},
	orcid-numbers = {Sebák, Fanni/0000-0001-9252-9961; Ecsédi, Péter/0000-0002-4700-125X; Nyitray, László/0000-0003-4717-5994; Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:34043118,
	title = {Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides},
	url = {https://m2.mtmt.hu/api/publication/34043118},
	author = {Sebák, Fanni and Szolomájer, János and Papp, Nándor and Tóth, Gábor and Bodor, Andrea},
	doi = {10.31083/j.fbl2806127},
	journal-iso = {FRONT BIOSCI-LANDMARK},
	journal = {FRONTIERS IN BIOSCIENCE-LANDMARK},
	volume = {28},
	unique-id = {34043118},
	issn = {2768-6701},
	year = {2023},
	eissn = {2768-6698},
	orcid-numbers = {Sebák, Fanni/0000-0001-9252-9961; Szolomájer, János/0000-0003-1458-6156; Tóth, Gábor/0000-0002-3604-4385; Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:33729542,
	title = {The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs},
	url = {https://m2.mtmt.hu/api/publication/33729542},
	author = {Kovács, Dániel and Bodor, Andrea},
	doi = {10.1039/D3RA00977G},
	journal-iso = {RSC ADV},
	journal = {RSC ADVANCES},
	volume = {13},
	unique-id = {33729542},
	issn = {2046-2069},
	abstract = {In studying secondary structural propensities of proteins by nuclear magnetic resonance (NMR) spectroscopy, secondary chemical shifts (SCSs) are the primary atomic scale observables. But which random coil chemical shift (RCCS) values to choose?},
	year = {2023},
	eissn = {2046-2069},
	pages = {10182-10203},
	orcid-numbers = {Bodor, Andrea/0000-0002-7422-298X}
}

@mastersthesis{MTMT:34396850,
	title = {Az NMR spektroszkópia sokszínűsége fehérjék és kismolekulák világában},
	url = {https://m2.mtmt.hu/api/publication/34396850},
	author = {Bodor, Andrea},
	unique-id = {34396850},
	year = {2022},
	orcid-numbers = {Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:34034694,
	title = {Conformational diversity of membrane active beta[sup]3[/sup]-peptide foldamers},
	url = {https://m2.mtmt.hu/api/publication/34034694},
	author = {Beke-Somfai, Tamas and El, Battioui Kamal and Juhasz, Tunde and Queme-Pena, Mayra and Szigyarto, Imola and Molnar, Daniel and Toth, Judit and Szabo, Lilla and Bodor, Andrea and Wacha, András Ferenc and Mandity, Istvan},
	journal-iso = {J PEPT SCI},
	journal = {JOURNAL OF PEPTIDE SCIENCE},
	volume = {28},
	unique-id = {34034694},
	issn = {1075-2617},
	keywords = {Biochemistry & Molecular Biology},
	year = {2022},
	eissn = {1099-1387},
	orcid-numbers = {Bodor, Andrea/0000-0002-7422-298X; Wacha, András Ferenc/0000-0002-9609-0893}
}

@article{MTMT:33258560,
	title = {Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins},
	url = {https://m2.mtmt.hu/api/publication/33258560},
	author = {Haller, Jens D. and Bodor, Andrea and Luy, Burkhard},
	doi = {10.1007/s10858-022-00406-z},
	journal-iso = {J BIOMOL NMR},
	journal = {JOURNAL OF BIOMOLECULAR NMR},
	volume = {76},
	unique-id = {33258560},
	issn = {0925-2738},
	abstract = {Large coupling networks in uniformly 13 C, 15 N-labeled biomolecules induce broad multiplets that even in flexible proteins are frequently not recognized as such. The reason is that given multiplets typically consist of a large number of individual resonances that result in a single broad line, in which individual components are no longer resolved. We here introduce a real-time pure shift acquisition scheme for the detection of amide protons which is based on 13 C-BIRD r,X . As a result the full homo- and heteronuclear coupling network can be suppressed at low power leading to real singlets at substantially improved resolution and uncompromised sensitivity. The method is tested on a small globular and an intrinsically disordered protein (IDP) where the average spectral resolution is increased by a factor of ~ 2 and higher. Equally important, the approach works without saturation of water magnetization for solvent suppression and exchanging amide protons are not affected by saturation transfer.},
	year = {2022},
	eissn = {1573-5001},
	pages = {213-221},
	orcid-numbers = {Haller, Jens D./0000-0002-7764-2816; Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:32853030,
	title = {The Disordered EZH2 Loop: Atomic Level Characterization by 1HN- and 1Hα-Detected NMR Approaches, Interaction with the Long Noncoding HOTAIR RNA},
	url = {https://m2.mtmt.hu/api/publication/32853030},
	author = {Szabó, Csenge Lilla and Szabó, Beáta and Sebák, Fanni and Bermel, Wolfgang and Tantos, Ágnes and Bodor, Andrea},
	doi = {10.3390/ijms23116150},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {32853030},
	issn = {1661-6596},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Szabó, Csenge Lilla/0000-0002-6508-3439; Sebák, Fanni/0000-0001-9252-9961; Tantos, Ágnes/0000-0003-1273-9841; Bodor, Andrea/0000-0002-7422-298X}
}