Výsledky vyhledávání - "Natalia S. Nemeria"

Akademický článek

Toward an Understanding of the Structural and Mechanistic Aspects of Protein-Protein Interactions in 2-Oxoacid Dehydrogenase Complexes

Autor: Natalia S. Nemeria, Xu Zhang, Joao Leandro, Jieyu Zhou, Luying Yang, Sander M. Houten, Frank Jordan

Publikováno v: Life, Vol 11, Iss 5, p 407 (2021)

The 2-oxoglutarate dehydrogenase complex (OGDHc) is a key enzyme in the tricarboxylic acid (TCA) cycle and represents one of the major regulators of mitochondrial metabolism through NADH and reactive oxygen species levels. The OGDHc impacts cell meta

Externí odkaz: https://doaj.org/article/287852682b644e1d865912d3f42da563

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Functional Versatility of the Human 2-Oxoadipate Dehydrogenase in the L-Lysine Degradation Pathway toward Its Non-Cognate Substrate 2-Oxopimelic Acid

Autor: Natalia S. Nemeria, Balint Nagy, Roberto Sanchez, Xu Zhang, João Leandro, Attila Ambrus, Sander M. Houten, Frank Jordan

Publikováno v: International Journal of Molecular Sciences; Volume 23; Issue 15; Pages: 8213

The human 2-oxoadipate dehydrogenase complex (OADHc) in L-lysine catabolism is involved in the oxidative decarboxylation of 2-oxoadipate (OA) to glutaryl-CoA and NADH (+H+). Genetic findings have linked the DHTKD1 encoding 2-oxoadipate dehydrogenase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0778be8807a3d5b3d08c3435137afdb
https://pubmed.ncbi.nlm.nih.gov/35897808

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Structure–function analyses of the G729R 2-oxoadipate dehydrogenase genetic variant associated with a disorder of l-lysine metabolism

Autor: Gary J. Gerfen, Frank Jordan, Bálint Nagy, Natalia S. Nemeria, Attila Ambrus, Michael B. Lazarus, Xu Zhang, Sander M. Houten, Roman Brukh, Oliver Ozohanics, João Leandro

Publikováno v: J Biol Chem

2-Oxoadipate dehydrogenase (E1a, also known as DHTKD1, dehydrogenase E1, and transketolase domain-containing protein 1) is a thiamin diphosphate-dependent enzyme and part of the 2-oxoadipate dehydrogenase complex (OADHc) in l-lysine catabolism. Genet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::635e7b8f7a6f3d9df3614469e73b289d
https://doi.org/10.1074/jbc.ra120.012761

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DHTKD1 and OGDH display substrate overlap in cultured cells and form a hybrid 2-oxo acid dehydrogenase complex in vivo

Autor: Natalia S. Nemeria, Frank Jordan, Chunli Yu, Xu Zhang, Sander M. Houten, Robert J. DeVita, Ronald C. Hendrickson, João Leandro, Jan Aten, Tetyana Dodatko, Roberto Sanchez

Publikováno v: Leandro, J, Dodatko, T, Aten, J, Nemeria, N S, Zhang, X, Jordan, F, Hendrickson, R C, Sanchez, R, Yu, C, DeVita, R J & Houten, S M 2020, ' DHTKD1 and OGDH display substrate overlap in cultured cells and form a hybrid 2-oxo acid dehydrogenase complex in vivo ', Human Molecular Genetics, vol. 29, no. 7, pp. 1168-1179 . https://doi.org/10.1093/HMG/DDAA037
Human molecular genetics, 29(7), 1168-1179. Oxford University Press
Hum Mol Genet
Human Molecular Genetics, 29(7), 1168-1179. Oxford University Press

Glutaric aciduria type 1 (GA1) is an inborn error of lysine degradation characterized by a specific encephalopathy that is caused by toxic accumulation of lysine degradation intermediates. Substrate reduction through inhibition of DHTKD1, an enzyme u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4b211cbfed828d5e97d2e00a37a3975
https://doi.org/10.1093/hmg/ddaa037

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Exclusive neuronal detection of KGDHC-specific subunits in the adult human brain cortex despite pancellular protein lysine succinylation

Autor: Frank Jordan, Attila Ambrus, Christos Chinopoulos, Attila G. Bagó, Natalia S. Nemeria, Árpád Dobolyi, Miklós Palkovits, Judit Doczi, Vera Adam-Vizi

Publikováno v: Brain Structure & Function

The ketoglutarate dehydrogenase complex (KGDHC) consists of three different subunits encoded by OGDH (or OGDHL), DLST, and DLD, combined in different stoichiometries. DLD subunit is shared between KGDHC and pyruvate dehydrogenase complex, branched-ch

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6a6564d534a3a44fcaa8ef2cae2ee8b
https://doi.org/10.1007/s00429-020-02026-5

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Probing the E1o-E2o and E1a-E2o Interactions in Binary Subcomplexes of the Human 2-Oxoglutarate Dehydrogenase and 2-Oxoadipate Dehydrogenase Complexes by Chemical Cross-Linking Mass Spectrometry and Molecular Dynamics Simulation

Autor: Oliver Ozohanics, Xu Zhang, Natalia S. Nemeria, Attila Ambrus, Frank Jordan

Publikováno v: International Journal of Molecular Sciences
Volume 24
Issue 5
Pages: 4555

The human 2-oxoglutarate dehydrogenase complex (hOGDHc) is a key enzyme in the tricarboxylic acid cycle and is one of the main regulators of mitochondrial metabolism through NADH and reactive oxygen species levels. Evidence was obtained for formation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa2ee36e3741ef993f5503f237b8fe7a
https://doi.org/10.3390/ijms24054555

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E. coli and the etiology of human PBC: Antimitochondrial antibodies and spreading determinants

Autor: Patrick S.C. Leung, Pietro Invernizzi, Natalia S. Nemeria, William M. Ridgway, M. Eric Gershwin, Yao Yang, Guo-Xiang Yang, Mark J. Kurth, Frank Jordan, Jinjung Choi, Ross L. Coppel, Ying Chen, Ti-Hong Shao, Weici Zhang, Aftab A. Ansari

Publikováno v: Hepatology (Baltimore, Md.)REFERENCES. 75(2)

Background and Aims: The increased frequency of urinary tract infections in patients with primary biliary cholangitis (PBC) and the cross-reactivity between the lipoyl domains (LD) of human pyruvate dehydrogenase complex (hPDC-E2) and Escherichia col

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a580790e9d6af456c0a3049c23e2d092
https://pubmed.ncbi.nlm.nih.gov/34608663

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Understanding of the 2-oxoglutarate dehydrogenase and 2-oxoadipate dehydrogenase assembly with the E2o core relevant to a hybrid complex formation

Autor: Xu Zhang, Frank Jordan, Natalia S. Nemeria

The 2-oxoglutarate (OG) dehydrogenase complex (OGDHc) is a key enzyme in the tricarboxylic acid cycle (TCA) and comprises multiple copies of three components: 2-oxoglutarate dehydrogenase (hE1o), dihydrolipoamide succinyltransferase (hE2o), and dihyd

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1132667d332b6bec4566330e4823d2eb
https://doi.org/10.1101/2021.02.03.429618

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Inhibition and Crystal Structure of the Human DHTKD1-Thiamin Diphosphate Complex

Autor: Michelle R. Arkin, João Leandro, Christopher G. Wilson, Sander M. Houten, Hui Wang, Michael B. Lazarus, Robert J. DeVita, Frank Jordan, Tetyana Dodatko, Brandon Stauffer, Roberto Sanchez, Natalia S. Nemeria, Chunli Yu, Chalada Suebsuwong, Susmita Khamrui, Moses Moustakim, Wang M, Cody Secor, Khoi Huynh

Publikováno v: ACS chemical biology, vol 15, iss 8
ACS Chem Biol

DHTKD1 is the E1 component of the 2-oxoadipic acid dehydrogenase complex (OADHc), which functions in the L-lysine degradation pathway. Mutations in DHTKD1 have been associated with 2-aminoadipic and 2-oxoadipic aciduria, Charcot-Marie-Tooth disease t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db1ec499ee06b35d557c41e6c15f5e44
https://escholarship.org/uc/item/5dj5p5mg

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An Update on Developments in the Field of Thiamin Diphosphate-Dependent Enzymes

Autor: Da Jeong Shim, Elena L. Guevara, Natalia S. Nemeria, Frank Jordan, Junjie Wang, Xu Zhang, Hetal Patel, Jieyu Zhou, Joydeep Chakraborty, Anand Balakrishnan, Pradeep Nareddy, Luying Yang

The Jordan group's interest center on: E. coli (ec) and human (h) pyruvate dehydrogenase (PDHc), 2-oxoglutarate dehydrogenase (OGDHc) and 2-oxoadipate dehydrogenase (OADHc) complexes; and on 1-deoxy-D-xylulose-5-phosphate synthase (DXPS). The most im

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dc99cf7ec0b8c9c5ed0442a487b4ec76
https://doi.org/10.1016/b978-0-12-409547-2.14833-4

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