{"id":36,"date":"2016-05-11T13:36:25","date_gmt":"2016-05-11T11:36:25","guid":{"rendered":"http:\/\/scholar.semmelweis.hu\/ambrusattila\/?page_id=36"},"modified":"2026-03-09T17:15:04","modified_gmt":"2026-03-09T16:15:04","slug":"publications","status":"publish","type":"page","link":"https:\/\/scholar.semmelweis.hu\/ambrusattila\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"
    \n
  1. Ambrus A,<\/u> F\u00e9s\u00fcs L, Polyethylene glycol enhanced refolding of the recombinant human tissue transglutaminase. Prep. Biochem. Biotechnol.<\/em> 31(1): 59-70 (2001)<\/li>\n
  2. Ambrus A<\/u>, Banyai I, Weiss M, Hilgenfeld R, Keresztessy Z, Muszbek L, Fesus L, Calcium binding of transglutaminases: a 43<\/sup>Ca NMR study combined with surface polarity analysis. J. Biomol. Struct. Dyn.<\/em> 19(1): 59-74 (2001)<\/li>\n
  3. Ambrus A<\/u>, Batta G, K\u00f6v\u00e9r K, Groves P, Palczewska M, Kuznicki J, An NMR study of calretinin, a calcium binding protein. The first two domains. Biok\u00e9mia<\/em> (Hungarian) 25(2): 37-39 (2001)<\/li>\n
  4. Palczewska M, Groves P, Ambrus A<\/u>, Kaleta A, Kover K, Batta G, Kuznicki J, Structural and biochemical characterization of neuronal calretinin domain I-II (residues 1-100). Comparison to homologous calbindin D28k domain I-II (residues 1-93). Eur.<\/em> J. Biochem.<\/em> 268(23): 6229-37 (2001)<\/li>\n
  5. Roberts S, Wildner G, Grass G, Weichsel A, Ambrus A<\/u>, Rensing C, Montfort W, A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO. J. Biol. Chem.<\/em> 278 (34): 31958-63 (2003)<\/li>\n
  6. Ambrus A<\/u>, Chen D, Dai J, Jones R, Yang D, Solution structure of the biologically relevant G-quadruplex element in the human c-MYC promoter. Implications for G-quadruplex stabilization. Biochemistry-US<\/em> 44 (6): 2048-2058 (2005) [featured on the cover of Biok\u00e9mia 31(1), 2007]<\/li>\n
  7. Ambrus A<\/u>, Chen D, Whatcott C, Somogyi A, Yang D, Matrix-assisted laser desorption\/ ionization time-of-flight mass spectrometry protocol for monitoring the progress of enzymatic C-13\/N-15-labeled DNA syntheses. Anal.<\/em>\u00a0 Biochem.<\/em> 342 (2): 246-53 (2005)<\/li>\n
  8. Tangirala R, Dixon R, Yang D, Ambrus A<\/u>, Antony S, Agama K, Pommier Y, Curran D, Total and semisynthesis and in vitro<\/em> studies of both enantiomers of 20-fluorocamptothecin. Bioorg. Med. Chem. Lett.<\/em> 15(21): 4736-40 (2005)<\/li>\n
  9. Dai J, Dexheimer T, Chen D, Carver M, Ambrus A<\/u>, Jones R, Yang D, An intramolecular G-quadruplex structure with mixed parallel\/antiparallel G-strands formed in the human Bcl-2 promoter region in solution. J. Am. Chem. Soc.<\/em> 128 (4): 1096-98 (2006) [ISI Web of Knowledge Essential Science Indicators Highly Cited Paper<\/u>]<\/li>\n
  10. Ambrus A<\/u>, Friedrich K, Somogyi A, Oligomerization of nitrophorins. Anal. Biochem<\/em>. 352 (2): 286-95 (2006)<\/li>\n
  11. Ambrus A<\/u>, Chen D, Dai J, Bialis T, Jones R, Yang D, Human telomeric sequence forms a hybrid-type intramolecular G-quadruplex structure with mixed parallel\/antiparallel strands in potassium solution. Nucleic Acids Res.<\/em> 34 (9): 2723-35 (2006) [ISI Web of Knowledge Essential Science Indicators Highly Cited Paper<\/u>; featured in Chemical & Engineering News (C&EN, ACS), July 31, 2006]<\/li>\n
  12. Dai J, Punchihewa C, Ambrus A<\/u>, Chen D, Jones R, Yang D, Structure of the intramolecular human telomeric G-quadruplex in potassium solution: A novel adenine triple formation. Nucleic Acids Res.<\/em> 35(7): 2440-50 (2007) [featured on the cover of Chemical & Engineering News (C&EN, ACS), May 28, 2007]<\/li>\n
  13. Ambrus A,<\/u> Yang D, Diffusion ordered NMR spectroscopy for analysis of DNA secondary structural elements. Anal. Biochem.<\/em> 367(1):56-67 (2007)<\/li>\n
  14. Ambrus A,<\/u> G-quadruplexes: structure and biological significance. Biok\u00e9mia<\/em> (Hungarian) 31(1): 2-8 (2007)<\/li>\n
  15. Ambrus A<\/u>, Torocsik B, Adam-Vizi V, Periplasmic cold expression and one-step purification of human dihydrolipoamide dehydrogenase. Protein Expr. Purif.<\/em>, 63(1): 50-57 (2009)<\/li>\n
  16. Vajda S, Mandi M, Konrad C, Kiss G, Ambrus A<\/u>, Adam-Vizi V, Chinopoulos C, A re-evaluation of the role of matrix acidification in uncoupler-induced Ca2+<\/sup>-release from mitochondria. FEBS J<\/em>. 276(10): 2713-2724 (2009)<\/li>\n
  17. Ambrus A<\/u>, Torocsik B, Adam-Vizi V, Refolding of the human dihydrolipoamide dehydrogenase. Biochem. Eng. J.<\/em> 45(2): 120-125 (2009)<\/li>\n
  18. Ambrus A<\/u>#<\/sup>, Tretter L#<\/sup>, Adam-Vizi V, Inhibition of the alpha-ketoglutarate dehydrogenase-mediated reactive oxygen species generation by lipoic acid. J. Neurochem.<\/em> 109(S1): 222-229 (2009) (#<\/sup>=contributed equally)<\/li>\n
  19. Dai J, Ambrus A<\/u>, Hurley L, Yang D, A direct and nondestructive approach to determine the folding structure of the i-motif DNA secondary structure by NMR. J. Am. Chem. Soc.<\/em> 131(17): 6102-6104 (2009)<\/li>\n
  20. Ambrus A<\/u>, Torocsik B, Tretter L, Ozohanics O, Adam-Vizi V, Stimulation of reactive oxygen species generation by disease-causing mutations of lipoamide dehydrogenase, Hum. Mol. Genet<\/em>. 20(15): 2984-2995 (2011)<\/li>\n
  21. Ambrus A,<\/u> Adam-Vizi V, Molecular dynamics study of the structural basis of dysfunction and the modulation of reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase, Arch.<\/em> Biochem. Biophys<\/em>. 538(2):145-155 (2013)<\/li>\n
  22. Tretter L, Ambrus A<\/u>, Measurement of ROS homeostasis in isolated mitochondria, Method. Enzymol.<\/em> 547: 199\u2013223 (2014)<\/li>\n
  23. Nemeria NS#<\/sup>, Ambrus A<\/u>#<\/sup>, Patel H#<\/sup>, Gerfen G, Adam-Vizi V, Tretter L, Zhou J, Wang J, Jordan F, Human 2-oxoglutarate dehydrogenase complex E1 component forms a thiamin-derived radical by aerobic oxidation of the enamine intermediate, J. Biol. Chem.<\/em> 289: 29859-29873 (2014) (#<\/sup>=contributed equally)<\/li>\n
  24. Ambrus A<\/u>, Mizsei R, Adam-Vizi V, Structural alterations by five disease-causing mutations in the low-pH conformation of human dihydrolipoamide dehydrogenase (hLADH) analyzed by molecular dynamics – implications in functional loss and modulation of reactive oxygen species generation by pathogenic hLADH forms, Biochem. Biophys. Reports<\/em>, 2:50-56 (2015)<\/li>\n
  25. Ambrus A<\/u>, Nemeria NS, Torocsik B, Tretter L, Nilsson M, Jordan F, Adam-Vizi V, Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components, Free Radic. Biol. Med.<\/em> 89: 642-650 (2015)<\/li>\n
  26. Harami-Papp H, Pongor SL, Munk\u00e1csy G, Horvath G, Nagy MA, Ambrus A<\/u>, Hauser P, Szabo A, Tretter L, Gyorffy B, TP53 mutation hits energy metabolism and increases glycolysis in breast cancer, Oncotarget<\/em>, 7:67183-67195 (2016)<\/li>\n
  27. Ambrus A<\/u>#<\/sup>, Wang J#<\/sup>, Mizsei R#<\/sup>, Zambo Z, Torocsik B, Jordan F, Adam-Vizi V, 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, Biochim. Biophys. Acta (Molecular Basis of Disease) <\/span><\/em>1862: 2098-2109 (2016) (#=contributed equally) (invited paper to Ambrus A)<\/li>\n
  28. Szabo E, Ambrus A<\/span>, Molecular pathomechanism of the human dihydrolipoamide dehydrogenase deficiency, Biok\u00e9mia<\/em> (Hungarian), 41(2): 44-63 (2017)\u00a0<\/li>\n
  29. Ambrus A<\/span>, Adam-Vizi V, Human dihydrolipoamide dehydrogenase (E3) deficiency:novel insights into the structural basis and molecular pathomechanism (review), Neurochem. Int.<\/em>, 117: 5-14 (2018)<\/li>\n
  30. Kiss E, Mirzahosseini A, Hubert A, Ambrus A<\/span>, Orfi L, Horvath P, DNA binding of Sunitinib: spectroscopic evidence via<\/em> circular dichroism and nuclear magnetic resonance, J. Pharm. Biomed. Anal.<\/em> 150: 355-361 (2018)<\/li>\n
  31. Mikulas K, Hermann P, Gera I, Koml\u00f3di T, Horv\u00e1th G, Ambrus A<\/span>, Tretter L, Triethylene glycol dimethacrylate impairs bioenergetic functions and induces oxidative stress in mitochondria via<\/em> inhibiting respiratory Complex I, Dent. Mater.<\/em> 34(7):e166-e181 (2018)<\/li>\n
  32. Komlodi T, <\/span>Geibl FF, <\/span>Sassani M, <\/span>Ambrus A<\/span>, Tretter L, <\/span>Membrane potential and delta pH dependency of reverse electron transport-associated hydrogen peroxide production in brain and heart mitochondria, J. Bioenerg. Biomembr. <\/em>50: 355-365 (2018)<\/span><\/li>\n
  33. Szabo E, Mizsei R, Wilk P, Zambo Z, Torocsik B, Weiss MS, Adam-Vizi V, Ambrus A<\/span>, Crystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenase,\u00a0Free Radic. Biol. Med<\/span>.<\/em> 124: 214-220 (2018)<\/span>\u00a0<\/li>\n
  34. Zhou J, Yang L, Ozohanics O, Zhang X, Wang J, Ambrus A<\/span>, Arjunan P, Brukh R, Nemeria NS, Furey W, Jordan F, Unique Protein-Protein Interactions in the Human 2-Oxoglutarate Dehydrogenase Multienzyme Complex as Revealed by Multifaceted Approaches, J. Biol. Chem. <\/em>293: 19213-19227 (2018)<\/li>\n
  35. Ambrus A<\/u>, An updated view on the molecular pathomechanisms of human dihydrolipoamide dehydrogenase deficiency in light of novel crystallographic evidence, Neurochem. Res.<\/em> 44: 2307-2313 (2019)<\/li>\n
  36. Szabo E, Wilk P, Nagy B, Zambo Z, Bui D, Weichsel A, Arjunan P, Torocsik B, Hubert A, Furey W, Montfort WR, Jordan F, Weiss MS, Adam-Vizi V, Ambrus A<\/u>, Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants, Hum. Mol. Genet. <\/em>28: 3339-3354 (2019)<\/li>\n
  37. Svab G, Doczy J, Gerencser A, Ambrus A<\/span>, Gallyas F, Sumegi B, \u00a0Tretter L, The mitochondrial targets of neuroprotective drug vinpocetine on primary neuron cultures, brain capillary endothelial cells, synaptosomes, and brain mitochondria, Neurochem. Res.<\/em> 44: 2435-2447 (2019)<\/li>\n
  38. Dobolyi A, Bago A, Palkovits M, Nemeria NS, Jordan F, Doczi J, Ambrus A,<\/u> Adam-Vizi V, Chinopoulos C, Exclusive neuronal detection of KGDHC-specific subunits in the adult human brain cortex despite pancellular protein lysine succinylation, Brain Struct. Funct. <\/em>225: 639-667 (2020)<\/li>\n
  39. Zhang X, Nemeria NS, Leandro J, Houten S, Lazarus MB, Gerfen GJ, Ozohanics O, Ambrus A<\/span>, Nagy B, Brukh R, Jordan F, Structure-function analyses of the G729R 2-oxoadipate dehydrogenase genetic variant associated with L-lysine metabolism disorder, J. Biol. Chem.<\/em>, 295(23): 8078-8095 (2020)<\/li>\n
  40. Mikulas K, Komlodi T, F\u00f6ldes A, Svab G, Horvath G, Nagy AM, Ambrus A<\/u>, Gyulai-Gaal S, Gera I, Hermann P, Varga G, Tretter L, Bioenergetic impairment of triethylene glycol dimethacrylate- (TEGDMA-) treated dental pulp stem cells (DPSCs) and isolated brain mitochondria are amended by redox compound methylene blue, Materials (Basel)<\/em> 13(16): 3472 (2020)<\/li>\n
  41. Ozohanics O, Ambrus A<\/u>, Hydrogen-Deuterium Exchange Mass Spectrometry: A novel structural biology approach to structure, dynamics and interactions of proteins and their complexes, Life (Basel)<\/em> 10(11): E286 (2020)<\/li>\n
  42. Nagy B, Polak M, Ozohanics O, Zambo Z, Szabo E, Hubert A, Jordan F, Nova\u010dek J, Adam-Vizi V, Ambrus A<\/u>, 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, BBA \u2013 Gen. Subj. <\/em>1865(6):129889 (2021)<\/li>\n
  43. Svab G, Kokas M, Sipos I, Ambrus A<\/u>, Tretter L, Methylene blue bridges the inhibition and produces unusual respiratory changes in complex III inhibited mitochondria. Studies on rats, mice and guinea pigs. Antioxidants <\/em>10(2):305 (2021)\u00a0<\/li>\n
  44. Szabo E, Ambrus A,<\/u> Editorial for the Special Issue \u201cCurrent Approaches in Molecular Enzymology\u201d (Guest Editor: Attila Ambrus), Life (Basel) <\/em>12(3):336 (2022)<\/li>\n
  45. Nemeria NS, Nagy B, Sanchez R, Zhang X, Leandro J, Ambrus A<\/u>, Houten S, Jordan F, Insight into the transformation of 2-oxopimelate by the human 2-oxoadipate dehydrogenase complex in the L-lysine degradation pathway and its chemoenzymatic applications. Int. J. Mol. Sci. <\/em>23(15):8213 (2022)<\/li>\n
  46. Horv\u00e1th G, Svab G, Koml\u00f3di T, Ravasz D, Kacs\u00f3 G, Doczi J, Chinopoulos C, Ambrus A<\/u>, Tretter L, Reduced mitochondrial ROS production in \u03b1-ketoglutarate dehydrogenase (\u03b1-KGDH) subunit (E2 and\/or E3) heterozygote knock out animals. Reverse electron flow-induced H2<\/sub>O2<\/sub> formation is also modified in the heterozygote KO animals. Antioxidants <\/em>11(8):1487 (2022)<\/li>\n
  47. Szabo E, Ambrus A<\/u>, Lipoamide dehydrogenase (LADH) deficiency: medical perspectives of the structural and functional characterization of LADH and its pathogenic variants, Biol. Futur. <\/em>74:109\u2013118 (2023)<\/li>\n
  48. Piroli GG, Manuel AM, McCain RS, Smith HH, Ozohanics O, Mellid S, Cox JH, Cotham WE, Walla MD, Casc\u00f3n A, Ambrus A<\/u>, Frizzell N, Defective function of \u03b1-ketoglutarate dehydrogenase exacerbates mitochondrial ATP deficits during complex I deficiency, Redox Biol.<\/em> 67: 102932 (2023)<\/li>\n
  49. Ozohanics O, Zhang X, Nemeria NS, Ambrus A#<\/sup><\/u>, Jordan F#<\/sup>, Probing the E1o\/E1a-E2o Interactions in Binary Sub-complexes of the Human 2-Oxoglutarate\/2-Oxoadipate Dehydrogenase Complexes by Chemical Cross-Linking Mass Spectrometry and Molecular Dynamics Simulations Analyses, Int. J. Mol. Sci.<\/em> 24, 4555 (2023)\u00a0(#<\/sup>=shared co-last authors)<\/li>\n
  50. Wittinger S, Szabo E, Ambrus A<\/u>, Function, structure and regulation of mitochondrial \u03b1-keto acid dehydrogenase enzyme complexes, Biok\u00e9mia<\/em> (Hungarian), 47(1): 19-31 (2023)<\/li>\n
  51. Szabo E, Nemes-Nikodem E, Vass KR, Zambo Z, Zrupko E, Torocsik B, Weiss MS, Adam-Vizi V, Ambrus A<\/u>, Structural and biochemical investigation of selected pathogenic mutants of the human dihydrolipoamide dehydrogenase, Int. J. Mol. Sci., <\/em>24(13):10826 (2023)<\/li>\n
  52. Szabo E, Nagy B, Czajlik A, Komlodi T, Ozohanics O, Tretter L, Ambrus A<\/u>, Mitochondrial alpha-keto acid dehydrogenase complexes: recent developments on structure and function in health and disease, Subcell. Biochem.<\/em> (Macromolecular Protein Complexes V, Springer Nature e-book), 104: 295-381 (2024)<\/li>\n
  53. Kokas M, Budai A, K\u00e1d\u00e1r A, Mozaffaritabar S, Zhou L, T\u00e9gl\u00e1s T, Orova RS, G\u00e1sp\u00e1r D, N\u00e9meth K, Toth DM, Sayour NV, Kov\u00e1csh\u00e1zi C, Xue A, Szatm\u00e1ri RZ, T\u00f6r\u0151csik B, M\u00e1th\u00e9 D, Kov\u00e1cs N, Szigeti K, Nagy P, Szatm\u00e1ri I, Fekete C, Ar\u00e1nyi T, Varga ZV, Ferdinandy P, Rad\u00e1k Z, Kozlov AV, Tretter L, Koml\u00f3di T#<\/sup>, Ambrus A#<\/sup><\/u>, Microgliosis, neuronal death, minor behavioral abnormalities and reduced endurance performance in alpha-ketoglutarate dehydrogenase complex deficient mice, Redox Biol<\/em>., 85: 103743, 2025\u00a0(#<\/sup>=shared co-last authors)<\/li>\n
  54. Kokas M, Ambrus A<\/u>, Tretter L, Koml\u00f3di T, Interplay between neuronal metabolism and signaling upon alpha-ketoglutarate dehydrogenase complex impairment, Biochemistry (Moscow)<\/em>, 2026, under review<\/li>\n<\/ol>\n

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    MTMT2: https:\/\/m2.mtmt.hu\/gui2\/?type=authors&mode=browse&sel=10000177<\/a><\/p>\n

    ORCID: http:\/\/orcid.org\/0000-0001-6014-3175<\/a><\/p>\n

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