@article{MTMT:34075046,
	title = {Structural and Biochemical Investigation of Selected Pathogenic Mutants of the Human Dihydrolipoamide Dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/34075046},
	author = {Szabó, Eszter and Nemes-Nikodém, Éva and Vass, Krisztina Rubina and Zámbó, Zsófia Melinda and Zrupko, E. and Törőcsik, Beáta and Ozohanics, Olivér and Nagy, Bálint and Ambrus, Attila},
	doi = {10.3390/ijms241310826},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34075046},
	issn = {1661-6596},
	abstract = {Clinically relevant disease-causing variants of the human dihydrolipoamide dehydrogenase (hLADH, hE3), a common component of the mitochondrial α-keto acid dehydrogenase complexes, were characterized using a multipronged approach to unravel the molecular pathomechanisms that underlie hLADH deficiency. The G101del and M326V substitutions both reduced the protein stability and triggered the disassembly of the functional/obligate hLADH homodimer and significant FAD losses, which altogether eventually manifested in a virtually undetectable catalytic activity in both cases. The I12T-hLADH variant proved also to be quite unstable, but managed to retain the dimeric enzyme form; the LADH activity, both in the forward and reverse catalytic directions and the affinity for the prosthetic group FAD were both significantly compromised. None of the above three variants lent themselves to an in-depth structural analysis via X-ray crystallography due to inherent protein instability. Crystal structures at 2.89 and 2.44 Å resolutions were determined for the I318T- and I358T-hLADH variants, respectively; structure analysis revealed minor conformational perturbations, which correlated well with the residual LADH activities, in both cases. For the dimer interface variants G426E-, I445M-, and R447G-hLADH, enzyme activities and FAD loss were determined and compared against the previously published structural data. © 2023 by the authors.},
	keywords = {Reactive oxygen species; X-RAY CRYSTALLOGRAPHY; Lipoamide Dehydrogenase; disease-causing mutation; alpha-keto acid dehydrogenase complexes},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Vass, Krisztina Rubina/0000-0002-1584-7154; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Törőcsik, Beáta/0000-0002-9838-3710; Ozohanics, Olivér/0000-0002-2705-9921; Nagy, Bálint/0000-0003-3669-7041; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:31917407,
	title = {Structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and cross-linking mass spectrometry. Implications for the overall hKGDHc structure.},
	url = {https://m2.mtmt.hu/api/publication/31917407},
	author = {Nagy, Bálint and Polak, Martin and Ozohanics, Olivér and Zámbó, Zsófia Melinda and Szabó, Eszter and Hubert, Ágnes and Jordan, Frank and Novaček, Jiří and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1016/j.bbagen.2021.129889},
	journal-iso = {BBA-GEN SUBJECTS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS},
	volume = {1865},
	unique-id = {31917407},
	issn = {0304-4165},
	abstract = {The human mitochondrial alpha-ketoglutarate dehydrogenase complex (hKGDHc) converts KG to succinyl-CoA and NADH. Malfunction of and reactive oxygen species generation by the hKGDHc as well as its E1-E2 subcomplex are implicated in neurodegenerative disorders, ischemia-reperfusion injury, E3-deficiency and cancers.We performed cryo-EM, cross-linking mass spectrometry (CL-MS) and molecular modeling analyses to determine the structure of the E2 component of the hKGDHc (hE2k); hE2k transfers a succinyl group to CoA and forms the structural core of hKGDHc. We also assessed the overall structure of the hKGDHc by negative-stain EM and modeling.We report the 2.9 Å resolution cryo-EM structure of the hE2k component. The cryo-EM map comprises density for hE2k residues 151-386 - the entire (inner) core catalytic domain plus a few additional residues -, while residues 1-150 are not observed due to the inherent flexibility of the N-terminal region. The structure of the latter segment was also determined by CL-MS and homology modeling. Negative-stain EM on in vitro assembled hKGDHc and previous data were used to build a putative overall structural model of the hKGDHc.The E2 core of the hKGDHc is composed of 24 hE2k chains organized in octahedral (8 × 3 type) assembly. Each lipoyl domain is oriented towards the core domain of an adjacent chain in the hE2k homotrimer. hE1k and hE3 are most likely tethered at the edges and faces, respectively, of the cubic hE2k assembly.The revealed structural information will support the future pharmacologically targeting of the hKGDHc.},
	keywords = {cryo-electron microscopy; cross-linking mass spectrometry; 2-Oxoglutarate dehydrogenase complex; Dihydrolipoamide succinyltransferase; α-Ketoglutarate dehydrogenase complex},
	year = {2021},
	eissn = {1872-8006},
	orcid-numbers = {Nagy, Bálint/0000-0003-3669-7041; Ozohanics, Olivér/0000-0002-2705-9921; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Szabó, Eszter/0000-0002-9634-2771; Hubert, Ágnes/0000-0001-6452-299X; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:33081530,
	title = {Structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and cross-linking mass spectrometry: Implications for the overall hKGDHc structure},
	url = {https://m2.mtmt.hu/api/publication/33081530},
	author = {Nagy, Bálint and Martin, Polak and Ozohanics, Olivér and Zámbó, Zsófia Melinda and Szabó, Eszter and Hubert, Ágnes and Frank, Jordan and Jiri, Novacek and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1002/pro.4191},
	journal-iso = {PROTEIN SCI},
	journal = {PROTEIN SCIENCE},
	volume = {30},
	unique-id = {33081530},
	issn = {0961-8368},
	year = {2021},
	eissn = {1469-896X},
	pages = {171-171},
	orcid-numbers = {Nagy, Bálint/0000-0003-3669-7041; Ozohanics, Olivér/0000-0002-2705-9921; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Szabó, Eszter/0000-0002-9634-2771; Hubert, Ágnes/0000-0001-6452-299X; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:33081442,
	title = {Structure of the Dihydrolipoamide Succinyltransferase (E2) Component of the Human α-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and Cross-linking mass spectrometry: Implications for the overall hKGDHc structure},
	url = {https://m2.mtmt.hu/api/publication/33081442},
	author = {Nagy, Bálint and Polak, Martin and Ozohanics, Olivér and Zámbó, Zsófia Melinda and Szabó, Eszter and Hubert, Ágnes and Jordan, Frank and Novacek, Jiri and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1016/j.freeradbiomed.2020.10.088},
	journal-iso = {FREE RADICAL BIO MED},
	journal = {FREE RADICAL BIOLOGY AND MEDICINE},
	volume = {159},
	unique-id = {33081442},
	issn = {0891-5849},
	year = {2020},
	eissn = {1873-4596},
	pages = {S29-S30},
	orcid-numbers = {Nagy, Bálint/0000-0003-3669-7041; Ozohanics, Olivér/0000-0002-2705-9921; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Szabó, Eszter/0000-0002-9634-2771; Hubert, Ágnes/0000-0001-6452-299X; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:31138483,
	title = {CRYO-EM STRUCTURE OF THE DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE (E2) COMPONENT OF THE HUMAN ALPHA-KETOGLUTARATE DEHYDROGENASE COMPLEX},
	url = {https://m2.mtmt.hu/api/publication/31138483},
	author = {Nagy, Bálint and Ambrus, Attila and Zámbó, Zsófia Melinda and Hubert, Ágnes and Polak, Martin and Szabó, Eszter and Novacek, Jiri and Jordan, Frank and Ádám, Veronika},
	journal-iso = {PROTEIN SCI},
	journal = {PROTEIN SCIENCE},
	volume = {28},
	unique-id = {31138483},
	issn = {0961-8368},
	year = {2019},
	eissn = {1469-896X},
	pages = {155-155},
	orcid-numbers = {Nagy, Bálint/0000-0003-3669-7041; Ambrus, Attila/0000-0001-6014-3175; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Hubert, Ágnes/0000-0001-6452-299X; Szabó, Eszter/0000-0002-9634-2771; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:31138484,
	title = {MOLECULAR MECHANISMS GIVING RISE TO HUMAN DIHYDROLIPOAMIDE DEHYDROGENASE DEFICIENCY - STRUCTURAL ANALYSIS OF SEVEN DISEASE-RELEVANT ENZYME VARIANTS},
	url = {https://m2.mtmt.hu/api/publication/31138484},
	author = {Szabó, Eszter and Wilk, Piotr and Nagy, Bálint and Mizsei, Reka and Zámbó, Zsófia Melinda and Bui, David and Weichsel, Andrzej and Arjunan, Palaniappa and Torocsik, Beata and Hubert, Ágnes and Furey, William and Monfort, William and Jordan, Frank and Weiss, Manfred and Ádám, Veronika and Ambrus, Attila},
	journal-iso = {PROTEIN SCI},
	journal = {PROTEIN SCIENCE},
	volume = {28},
	unique-id = {31138484},
	issn = {0961-8368},
	year = {2019},
	eissn = {1469-896X},
	pages = {163-164},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Nagy, Bálint/0000-0003-3669-7041; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Hubert, Ágnes/0000-0001-6452-299X; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:30799456,
	title = {Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants},
	url = {https://m2.mtmt.hu/api/publication/30799456},
	author = {Szabó, Eszter and Wilk, Piotr and Nagy, Bálint and Zámbó, Zsófia Melinda and Bui, Dávid and Weichsel, Andrzej and Arjunan, Palaniappa and Törőcsik, Beáta and Hubert, Agnes and Furey, William and Montfort, William R and Jordan, Frank and Weiss, Manfred S and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1093/hmg/ddz177},
	journal-iso = {HUM MOL GENET},
	journal = {HUMAN MOLECULAR GENETICS},
	volume = {28},
	unique-id = {30799456},
	issn = {0964-6906},
	abstract = {Human dihydrolipoamide dehydrogenase (hLADH, hE3) deficiency (OMIM# 246900) is an often prematurely lethal genetic disease usually caused by inactive or partially inactive hE3 variants. Here we report the crystal structure of wild-type hE3 at an unprecedented high resolution of 1.75 Å and the structures of six disease-causing hE3 variants at resolutions ranging from 1.44 to 2.34 Å. P453L proved to be the most deleterious substitution in structure as aberrations extensively compromised the active site. The most prevalent G194C-hE3 variant primarily exhibited structural alterations close to the substitution site, whereas the nearby cofactor-binding residues were left unperturbed. The G426E substitution mainly interfered with the local charge distribution introducing dynamics to the substitution site in the dimer interface; G194C and G426E both led to minor structural changes. The R460G, R447G, and I445M substitutions all perturbed a solvent accessible channel, the so-called H+/H2O channel, leading to the active site. Molecular pathomechanisms of enhanced reactive oxygen species (ROS) generation and impaired binding to multienzyme complexes were also addressed according to the structural data for the relevant mutations. In summary, we present here for the first time a comprehensive study that links three-dimensional structures of disease-causing hE3 variants to residual hLADH activities, altered capacities for ROS generation, compromised affinities for multienzyme complexes, and eventually clinical symptoms. Our results may serve as useful starting points for future therapeutic intervention approaches.},
	year = {2019},
	eissn = {1460-2083},
	pages = {3339-3354},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Nagy, Bálint/0000-0003-3669-7041; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Bui, Dávid/0000-0003-3726-2031; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:3407990,
	title = {Crystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/3407990},
	author = {Szabó, Eszter and Mizsei, Réka and Wilk, P and Zámbó, Zsófia Melinda and Törőcsik, Beáta and Weiss, MS and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1016/j.freeradbiomed.2018.06.008},
	journal-iso = {FREE RADICAL BIO MED},
	journal = {FREE RADICAL BIOLOGY AND MEDICINE},
	volume = {124},
	unique-id = {3407990},
	issn = {0891-5849},
	abstract = {We report the crystal structures of the human (dihydro)lipoamide dehydrogenase (hLADH, hE3) and its disease-causing homodimer interface mutant D444V-hE3 at 2.27 and 1.84 Å resolution, respectively. The wild type structure is a unique uncomplexed, unliganded hE3 structure with the true canonical sequence. Based on the structural information a novel molecular pathomechanism is proposed for the impaired catalytic activity and enhanced capacity for reactive oxygen species generation of the pathogenic mutant. The mechanistic model involves a previously much ignored solvent accessible channel leading to the active site that might be perturbed also by other disease-causing homodimer interface substitutions of this enzyme. © 2018 Elsevier Inc.},
	keywords = {Reactive oxygen species; X-RAY CRYSTALLOGRAPHY; protein structure; Lipoamide Dehydrogenase; Pyruvate Dehydrogenase Complex; Pathogenic mutation; E3 deficiency; Alpha-ketoglutarate dehydrogenase complex; Oxidative stress},
	year = {2018},
	eissn = {1873-4596},
	pages = {214-220},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Mizsei, Réka/0000-0003-4519-4307; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:3114546,
	title = {Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency},
	url = {https://m2.mtmt.hu/api/publication/3114546},
	author = {Ambrus, Attila and Wang, J and Mizsei, Réka and Zámbó, Zsófia Melinda and Törőcsik, Beáta and Jordan, F and Ádám, Veronika},
	doi = {10.1016/j.bbadis.2016.08.013},
	journal-iso = {BBA-MOL BASIS DIS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE},
	volume = {1862},
	unique-id = {3114546},
	issn = {0925-4439},
	abstract = {Pathogenic amino acid substitutions of the common E3 component (hE3) of the human alpha-ketoglutarate dehydrogenase and the pyruvate dehydrogenase complexes lead to severe metabolic diseases (E3 deficiency), which usually manifest themselves in cardiological and/or neurological symptoms and often cause premature death. To date, 14 disease-causing amino acid substitutions of the hE3 component have been reported in the clinical literature. None of the pathogenic protein variants has lent itself to high-resolution structure elucidation by X-ray or NMR. Hence, the structural alterations of the hE3 protein caused by the disease-causing mutations and leading to dysfunction, including the enhanced generation of reactive oxygen species by selected disease-causing variants, could only be speculated. Here we report results of an examination of the effects on the protein structure of ten pathogenic mutations of hE3 using hydrogen/deuterium-exchange mass spectrometry (HDX-MS), a new and state-of-the-art approach of solution structure elucidation. On the basis of the results, putative structural and mechanistic conclusions were drawn regarding the molecular pathogenesis of each disease-causing hE3 mutation addressed in this study. © 2016 Elsevier B.V.},
	keywords = {Mass spectrometry; Dihydrolipoamide dehydrogenase; Hydrogen/deuterium exchange; Pathogenic mutation; E3 deficiency},
	year = {2016},
	eissn = {1879-260X},
	pages = {2098-2109},
	orcid-numbers = {Ambrus, Attila/0000-0001-6014-3175; Mizsei, Réka/0000-0003-4519-4307; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701}
}

@article{MTMT:3262089,
	title = {Isolation and crystallization of the pathological mutants of human dihydrolipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/3262089},
	author = {Nagy, Bálint and Hubert, Ágnes and Szabó, Eszter and Zámbó, Zsófia Melinda and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1016/j.bbabio.2016.04.311},
	journal-iso = {BBA-BIOENERGETICS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS},
	volume = {1857},
	unique-id = {3262089},
	issn = {0005-2728},
	year = {2016},
	eissn = {1879-2650},
	pages = {e42},
	orcid-numbers = {Nagy, Bálint/0000-0003-3669-7041; Hubert, Ágnes/0000-0001-6452-299X; Szabó, Eszter/0000-0002-9634-2771; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:3262113,
	title = {Crystal structure of the D444V disease-causing mutant of human dihydrolipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/3262113},
	author = {Szabó, Eszter and Mizsei, R and Zámbó, Zsófia Melinda and Torocsik, B and Weiss, MS and Adam-Vizi, V and Ambrus, Attila},
	journal-iso = {PROTEIN SCI},
	journal = {PROTEIN SCIENCE},
	volume = {25},
	unique-id = {3262113},
	issn = {0961-8368},
	year = {2016},
	eissn = {1469-896X},
	pages = {162-162},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:3262509,
	title = {Crystal structure of the D444V disease-causing mutant of human dihydrolipoamide dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/3262509},
	author = {Szabó, Eszter and Mizsei, Réka and Zámbó, Zsófia Melinda and Törőcsik, Beáta and Weiss, Manfred S and Ádám, Veronika and Ambrus, Attila},
	doi = {10.1016/j.bbabio.2016.04.337},
	journal-iso = {BBA-BIOENERGETICS},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS},
	volume = {1857},
	unique-id = {3262509},
	issn = {0005-2728},
	year = {2016},
	eissn = {1879-2650},
	pages = {e100},
	orcid-numbers = {Szabó, Eszter/0000-0002-9634-2771; Mizsei, Réka/0000-0003-4519-4307; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Törőcsik, Beáta/0000-0002-9838-3710; Ádám, Veronika/0000-0002-8350-8701; Ambrus, Attila/0000-0001-6014-3175}
}

@article{MTMT:3003992,
	title = {Targeted tumor therapy by Rubia tinctorum L.: analytical characterization of hydroxyanthraquinones and investigation of their selective cytotoxic, adhesion and migration modulator effects on melanoma cell lines (A2058 and HT168‑M1)},
	url = {https://m2.mtmt.hu/api/publication/3003992},
	author = {Lajkó, Eszter and Bányai, Péter and Zámbó, Zsófia Melinda and Kursinszki, László and Szőke, Éva and Kőhidai, László},
	doi = {10.1186/s12935-015-0271-4},
	journal-iso = {CANCER CELL INT},
	journal = {CANCER CELL INTERNATIONAL},
	volume = {15},
	unique-id = {3003992},
	issn = {1475-2867},
	abstract = {Background: Alizarin and purpurin are di- and trihydroxyanthraquinones derived from Rubia tinctorum L. Previous pharmacological studies have demonstrated that they exhibit certain degree of selective inhibitory effects towards cancer cells suggesting their application as a targeted drug for cancer. Our present work was aimed to investigate the suitability of hydroxyanthraquinones of Rubia tinctorum L. for targeted tumor therapy. The effects of alizarin, purpurin and an aqueous extract from transformed hairy root culture of Rubia tinctorum L. were examined on (1) cell proliferation, (2) apoptosis, (3) cell adhesion/morphology and (4) migration (chemotaxis, chemokinesis) of human melanoma cell lines (A2058, HT168-M1) and human fibroblast cells (MRC-5), as well as (5) the aqueous extract was analytically characterized. Methods: The aqueous extract was prepared from R. tinctorum hairy root culture and qualitatively analyzed by HPLC and ESI-MS methods. The cell growth inhibitory activity of anthraquinones was evaluated by MTT-assay and by flow cytometry. The effect of anthraquinones on cell adhesion was measured by an impedance based technique, the xCELLigence SP. For the chemotaxis assay NeuroProbe® chamber was used. Computer based holographic microscopy was applied to analyze chemokinetic responses as well as morphometry. Statistical significance was determined by the one-way ANOVA test. Results: In the aqueous extract, munjistin (Mr = 284, tR = 18.4 min) as a principal component and three minor anthraquinones (pseudopurpurin, rubiadin and nordamnacanthal) were identified. The purpurin elicited a stronger but not apoptosis-mediated antitumor effect in melanoma cells (A2058: 10-6-10-5 M: 90.6-64.1 %) than in normal fibroblasts (10-6-10-5 M: 97.6-84.8 %). The aqueous extract in equimolar concentrations showed the most potent cytotoxicity after 72 h incubation (A2058: 10-6-10-5 M: 87.4-55.0 %). All tested substances elicited chemorepellent effect in melanoma cells, while in MRC-5 fibroblasts, only the alizarin exhibited such a repellent character. Indices of chemokinesis measured by holographic microscopy (migration, migration directness, motility and motility speed) were significantly enhanced by alizarin and purpurin as well, while morphometric changes were weak in the two melanoma cell lines. Conclusions: Our results highlight the effective and selective inhibitory activity of purpurin towards melanoma cells and its possible use as a targeted anticancer agent. The anthraquinones of the cytotoxic extract are suggested to apply in drug delivery systems as an anticancer drug. © 2015 Lajkó et al.},
	keywords = {ARTICLE; human; WATER; Cell Adhesion; high performance liquid chromatography; controlled study; MIGRATION; nonhuman; drug effect; velocity; concentration response; Cell Line; FIBROBLAST; human cell; drug delivery system; unclassified drug; drug cytotoxicity; cell migration; Drug targeting; targeted therapy; qualitative analysis; ANTINEOPLASTIC ACTIVITY; cell structure; electrospray mass spectrometry; Melanoma; cytotoxic agent; incubation time; drug isolation; plant extract; drug potency; cell transformation; drug hydrolysis; cancer inhibition; Hairy root culture; purpurin; rubia tinctorum; Rubia; anthraquinone derivative; cell motility; HPLC-MS/MS; MRC 5 cell; melanoma cell line; HT168 M1 cell line; chemokinesis; A2058 cell line; rubiadin; pseudopurpurin; nordamnacanthal; munjistin; hydroxyanthraquinone derivative; Rubia tinctorum L.; Impedimetry; Hydroxyanthraquinone; Holographic microscope},
	year = {2015},
	eissn = {1475-2867},
	orcid-numbers = {Lajkó, Eszter/0000-0002-4796-4646; Bányai, Péter/0000-0001-7999-2230; Zámbó, Zsófia Melinda/0000-0001-8657-8556; Kursinszki, László/0000-0002-7482-3283; Szőke, Éva/0000-0003-3433-8459; Kőhidai, László/0000-0002-9002-0296}
}