Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Zsofia Zambo"'
1
Structural and Biochemical Investigation of Selected Pathogenic Mutants of the Human Dihydrolipoamide Dehydrogenase
Autor: Ambrus, Eszter Szabo, Eva Nemes-Nikodem, Krisztina Rubina Vass, Zsofia Zambo, Eszter Zrupko, Beata Torocsik, Oliver Ozohanics, Balint Nagy, Attila
Publikováno v: International Journal of Molecular Sciences; Volume 24; Issue 13; Pages: 10826
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 molec
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=multidiscipl::0c2438e4fc13d8309fb382a44da8543a
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2
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
Autor: Zsofia Zambo, Bálint Nagy, Jiří Nováček, Martin Polak, Eszter Szabó, Attila Ambrus, Frank Jordan, Agnes Hubert, Vera Adam-Vizi, Oliver Ozohanics
Publikováno v: Biochimica et biophysica acta. General subjects. 1865(6)
Background 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 neurodeg
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b4ae6f6e285bf472868695abf1f00b9
https://pubmed.ncbi.nlm.nih.gov/33684457
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3
Crystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenase
Autor: Manfred S. Weiss, Vera Adam-Vizi, Réka Mizsei, Eszter Szabó, Attila Ambrus, Zsofia Zambo, Beáta Töröcsik, Piotr Wilk
Publikováno v: Free Radical Biology and Medicine. 124:214-220
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 A resolution, respectively. The wild type structure is a unique uncomplexed, unl
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e72cb16ee7aaa1e395cb87cafce5d580
https://doi.org/10.1016/j.freeradbiomed.2018.06.008
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5
Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants
Autor: Frank Jordan, Palaniappa Arjunan, Andrzej Weichsel, William Furey, Weiss, Bálint Nagy, William R. Montfort, Zsofia Zambo, Vera Adam-Vizi, David Bui, Attila Ambrus, Agnes Hubert, Piotr Wilk, Eszter Szabó, Beáta Töröcsik
Publikováno v: Hum Mol Genet
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 unpr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::765636458b582a0fffa477ce9b4f4161
https://europepmc.org/articles/PMC7275779/
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6
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)
Autor: L. Kursinszki, Eszter Lajkó, Zsofia Zambo, Éva Szőke, Péter Bányai, László Kőhidai
Publikováno v: Cancer Cell International
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
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::baaf8f267ca046b28fb6fb26e740324d
https://doi.org/10.1186/s12935-015-0271-4
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