Dora Ravasz
Overview
Explore the profile of Dora Ravasz including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
10
Citations
148
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Ravasz D, Bui D, Nazarian S, Pallag G, Karnok N, Roberts J, et al.
Sci Rep
. 2024 Jan;
14(1):1729.
PMID: 38242919
Anoxia halts oxidative phosphorylation (OXPHOS) causing an accumulation of reduced compounds in the mitochondrial matrix which impedes dehydrogenases. By simultaneously measuring oxygen concentration, NADH autofluorescence, mitochondrial membrane potential and ubiquinone...
2.
Horvath G, Svab G, Komlodi T, Ravasz D, Kacso G, Doczi J, et al.
Antioxidants (Basel)
. 2022 Aug;
11(8).
PMID: 36009207
α-ketoglutarate dehydrogenase complex (KGDHc), or 2-oxoglutarate dehydrogenase complex (OGDHc) is a rate-limiting enzyme in the tricarboxylic acid cycle, that has been identified in neurodegenerative diseases such as in Alzheimer's disease....
3.
Pallag G, Nazarian S, Ravasz D, Bui D, Komlodi T, Doerrier C, et al.
Int J Mol Sci
. 2022 May;
23(9).
PMID: 35563503
The oxidation of proline to pyrroline-5-carboxylate (P5C) leads to the transfer of electrons to ubiquinone in mitochondria that express proline dehydrogenase (ProDH). This electron transfer supports Complexes CIII and CIV,...
4.
Bui D, Ravasz D, Chinopoulos C
Neurochem Res
. 2019 Feb;
44(10):2301-2306.
PMID: 30810978
The reaction catalyzed by succinate-CoA ligase in the mitochondrial matrix yields a high-energy phosphate when operating towards hydrolysis of the thioester bond of succinyl-CoA, known as mitochondrial substrate-level phosphorylation (mSLP)....
5.
Ravasz D, Kacso G, Fodor V, Horvath K, Adam-Vizi V, Chinopoulos C
Biochim Biophys Acta Bioenerg
. 2018 May;
1859(9):909-924.
PMID: 29746824
Provision of NAD for oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA by the ketoglutarate dehydrogenase complex (KGDHC) is critical for maintained operation of succinyl-CoA ligase yielding high-energy phosphates, a process known...
6.
Chen E, Kiebish M, McDaniel J, Niedzwiecka K, Kucharczyk R, Ravasz D, et al.
Sci Rep
. 2018 Apr;
8(1):5915.
PMID: 29651047
Heterologous expression is a landmark technique for studying a protein itself or its effect on the expression host, in which membrane-embedded proteins are a common choice. Yet, the impact of...
7.
Ravasz D, Kacso G, Fodor V, Horvath K, Adam-Vizi V, Chinopoulos C
Neurochem Int
. 2017 Mar;
109:41-53.
PMID: 28300620
GABA is catabolized in the mitochondrial matrix through the GABA shunt, encompassing transamination to succinic semialdehyde followed by oxidation to succinate by the concerted actions of GABA transaminase (GABA-T) and...
8.
Chen E, Kiebish M, McDaniel J, Gao F, Narain N, Sarangarajan R, et al.
Biochim Biophys Acta
. 2016 Aug;
1861(11):1727-1735.
PMID: 27542539
Encysted embryos (cysts) of the crustacean Artemia franciscana exhibit enormous tolerance to adverse conditions encompassing high doses of radiation, years of anoxia, desiccation and extreme salinity. So far, several mechanisms...
9.
Kacso G, Ravasz D, Doczi J, Nemeth B, Madgar O, Saada A, et al.
Biochem J
. 2016 Aug;
473(20):3463-3485.
PMID: 27496549
Succinate-CoA ligase (SUCL) is a heterodimer enzyme composed of Suclg1 α-subunit and a substrate-specific Sucla2 or Suclg2 β-subunit yielding ATP or GTP, respectively. In humans, the deficiency of this enzyme...
10.
Nemeth B, Doczi J, Csete D, Kacso G, Ravasz D, Adams D, et al.
FASEB J
. 2015 Sep;
30(1):286-300.
PMID: 26358042
Itaconate is a nonamino organic acid exhibiting antimicrobial effects. It has been recently identified in cells of macrophage lineage as a product of an enzyme encoded by immunoresponsive gene 1...