TY  - JOUR
AU  - Li, Jian
AU  - Mu, Xin
AU  - Dong, Wenyue
AU  - Chen, Yun
AU  - Kang, Qianjin
AU  - Zhao, Guang
AU  - Hou, Jin
AU  - Gonzalez, Ramon
AU  - Bai, Linquan
AU  - Feng, Yan
AU  - Yang, Chen
AU  - Liu, Tiangang
AU  - Tan, Zaigao
TI  - A non-carboxylative route for the efficient synthesis of central metabolite malonyl-CoA and its derived products
JF  - NATURE CATALYSIS
J2  - NAT CATAL
PY  - 2024
PG  - 25
SN  - 2520-1158
DO  - 10.1038/s41929-023-01103-2
UR  - https://m2.mtmt.hu/api/publication/34583668
ID  - 34583668
AB  - Acetyl coenzyme A (CoA) carboxylation is the natural route for endogenous malonyl-CoA formation; however, this pathway presents slow kinetics, carbon and energy inefficiencies, tight regulations and a complicated architecture. These shortcomings limit flux towards malonyl-CoA and become a bottleneck towards the biosynthesis of malonyl-CoA-derived products (MDPs). Here, we design the non-carboxylative malonyl-CoA pathway as a non-natural route for malonyl-CoA biosynthesis, independent from acetyl-CoA. The designed pathway features enzymes such as beta-alanine-pyruvate transaminase and malonyl-CoA reductase, exhibits fast kinetics and circumvents tight regulations and the architecture associated with the natural pathway. Furthermore, introducing this pathway into microbes enhances the production of MDPs, including short-chain fatty acids and representative phenol, quinone, alkene, aminoglycoside and macrolide polyketide families, such as spinosad. In summary, this malonyl-CoA formation pathway avoids intrinsic inefficiencies of the natural pathway and can serve as a versatile platform for obtaining MDPs that could be used as fuels, fine chemicals and pharmaceuticals.Acetyl-CoA carboxylation is the canonical route for endogenous malonyl-CoA formation in cells. Here, the authors design a non-carboxylative malonyl-CoA pathway independent of acetyl-CoA into multiple microbes for efficient malonyl-CoA-derived natural products biosynthesis.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Boyle, E.
AU  - Wilfling, F.
TI  - Bypassing the nuclear gate: A non-canonical entry pathway for the mitochondrial pyruvate dehydrogenase complex
JF  - MOLECULAR CELL
J2  - MOL CELL
VL  - 82
PY  - 2022
IS  - 5
SP  - 886
EP  - 888
PG  - 3
SN  - 1097-2765
DO  - 10.1016/j.molcel.2022.02.014
UR  - https://m2.mtmt.hu/api/publication/32894110
ID  - 32894110
N1  - Export Date: 20 June 2022            
            CODEN: MOCEF            
            Correspondence Address: Wilfling, F.; Mechanisms of Cellular Quality Control, Germany; email: florian.wilfling@biophys.mpg.de            
            Chemicals/CAS: Pyruvate Dehydrogenase Complex            
            Funding details: Max-Planck-Gesellschaft, MPG            
            Funding text 1: The authors’ research is supported by the Max-Planck-Gesellschaft and the Max Planck Institute of Biophysics .
AB  - Zervopoulos et al. (2022) propose a non-canonical nuclear import pathway for the functional mitochondrial pyruvate dehydrogenase complex (PDC), facilitated by dynamic MFN2-mediated tethering of mitochondria to the nuclear envelope upon exposure to proliferative stimuli. © 2022 Elsevier Inc.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Zervopoulos, S.D.
AU  - Boukouris, A.E.
AU  - Saleme, B.
AU  - Haromy, A.
AU  - Tejay, S.
AU  - Sutendra, G.
AU  - Michelakis, E.D.
TI  - MFN2-driven mitochondria-to-nucleus tethering allows a non-canonical nuclear entry pathway of the mitochondrial pyruvate dehydrogenase complex
JF  - MOLECULAR CELL
J2  - MOL CELL
VL  - 82
PY  - 2022
IS  - 5
SP  - 1066
EP  - 1077.e7
SN  - 1097-2765
DO  - 10.1016/j.molcel.2022.02.003
UR  - https://m2.mtmt.hu/api/publication/32894109
ID  - 32894109
N1  - Cited By :1            
            Export Date: 20 June 2022            
            CODEN: MOCEF            
            Correspondence Address: Sutendra, G.; Department of Medicine, Canada; email: sutendra@ualberta.ca            
            Correspondence Address: Michelakis, E.D.; Department of Medicine, Canada; email: em2@ualberta.ca            
            Chemicals/CAS: lysine, 56-87-1, 6899-06-5, 70-54-2; acetyl coenzyme A, 72-89-9; Acetyl Coenzyme A; Lamins; Pyruvate Dehydrogenase Complex            
            Funding details: Natural Sciences and Engineering Research Council of Canada, NSERC            
            Funding details: Heart and Stroke Foundation of Canada, HSF            
            Funding details: Canada Research Chairs            
            Funding details: Alberta Innovates, AI            
            Funding text 1: B.S. is supported by a graduate scholarship from Alberta Innovates. G.S. is supported by an Alberta Innovates Translational Health Chair in Cardio-Oncology and a National and Alberta New Investigator Award from Heart and Stroke Foundation of Canada . E.D.M. is supported by Canada Research Chair (Tier 1), a CIHR Foundation grant, and Natural Sciences and Engineering Research Council grants.
AB  - The mitochondrial pyruvate dehydrogenase complex (PDC) translocates into the nucleus, facilitating histone acetylation by producing acetyl-CoA. We describe a noncanonical pathway for nuclear PDC (nPDC) import that does not involve nuclear pore complexes (NPCs). Mitochondria cluster around the nucleus in response to proliferative stimuli and tether onto the nuclear envelope (NE) via mitofusin-2 (MFN2)-enriched contact points. A decrease in nuclear MFN2 levels decreases mitochondria tethering and nPDC levels. Mitochondrial PDC crosses the NE and interacts with lamin A, forming a ring below the NE before crossing through the lamin layer into the nucleoplasm, in areas away from NPCs. Effective blockage of NPC trafficking does not decrease nPDC levels. The PDC-lamin interaction is maintained during cell division, when lamin depolymerizes and disassembles before reforming daughter nuclear envelopes, providing another pathway for nPDC entry during mitosis. Our work provides a different angle to understanding mitochondria-to-nucleus communication and nuclear metabolism. © 2022 Elsevier Inc.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Lee, J.
AU  - Oh, S.
AU  - Bhattacharya, S.
AU  - Zhang, Y.
AU  - Florens, L.
AU  - Washburn, M.P.
AU  - Workman, J.L.
TI  - The plasticity of the pyruvate dehydrogenase complex confers a labile structure that is associated with its catalytic activity
JF  - PLOS ONE
J2  - PLOS ONE
VL  - 15
PY  - 2021
IS  - 12 December
SN  - 1932-6203
DO  - 10.1371/journal.pone.0243489
UR  - https://m2.mtmt.hu/api/publication/31836491
ID  - 31836491
N1  - Stowers Institute for Medical Research, Kansas City, MO, United States            
            Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, KS, United States            
            Export Date: 29 January 2021            
            CODEN: POLNC            
            Correspondence Address: Workman, J.L.; Stowers Institute for Medical ResearchUnited States; email: jlw@stowers.org            
            Funding details: R35GM118068            
            Funding details: National Institutes of Health, NIH            
            Funding text 1: Stowers Institute for Medical Research (https://www.stowers.org) and National Institutes of General Medical Sciences (https://www.nigms. nih.gov) grant R35GM118068 (J.L.W.). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Stowers Institute for Medical Research, Kansas City, MO, United States            
            Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, KS, United States            
            Export Date: 1 April 2021            
            CODEN: POLNC            
            Correspondence Address: Workman, J.L.; Stowers Institute for Medical ResearchUnited States; email: jlw@stowers.org            
            Chemicals/CAS: sodium chloride, 7647-14-5, 23724-87-0, 49658-21-1; Pyruvate Dehydrogenase Complex; Sodium Chloride            
            Funding details: National Institutes of Health, NIH            
            Funding details: National Institute of General Medical Sciences, NIGMS, R35GM118068            
            Funding text 1: Stowers Institute for Medical Research (https://www.stowers.org) and National Institutes of General Medical Sciences (https://www.nigms. nih.gov) grant R35GM118068 (J.L.W.). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Stowers Institute for Medical Research, Kansas City, MO, United States            
            Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, KS, United States            
            Export Date: 12 August 2021            
            CODEN: POLNC            
            Correspondence Address: Workman, J.L.; Stowers Institute for Medical ResearchUnited States; email: jlw@stowers.org            
            Chemicals/CAS: sodium chloride, 7647-14-5, 23724-87-0, 49658-21-1; Pyruvate Dehydrogenase Complex; Sodium Chloride            
            Funding details: National Institutes of Health, NIH            
            Funding details: National Institute of General Medical Sciences, NIGMS, R35GM118068            
            Funding text 1: Stowers Institute for Medical Research (https://www.stowers.org) and National Institutes of General Medical Sciences (https://www.nigms. nih.gov) grant R35GM118068 (J.L.W.). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
AB  - The pyruvate dehydrogenase complex (PDC) is a multienzyme complex that plays a key role in energy metabolism by converting pyruvate to acetyl-CoA. An increase of nuclear PDC has been shown to be correlated with an increase of histone acetylation that requires acetyl-CoA. PDC has been reported to form a ∼ 10 MDa macromolecular machine that is proficient in performing sequential catalytic reactions via its three components. In this study, we show that the PDC displays size versatility in an ionic strength-dependent manner using size exclusion chromatography of yeast cell extracts. Biochemical analysis in combination with mass spectrometry indicates that yeast PDC (yPDC) is a salt-labile complex that dissociates into sub-megadalton individual components even under physiological ionic strength. Interestingly, we find that each oligomeric component of yPDC displays a larger size than previously believed. In addition, we show that the mammalian PDC also displays this uncommon characteristic of salt-lability, although it has a somewhat different profile compared to yeast. We show that the activity of yPDC is reduced in higher ionic strength. Our results indicate that the structure of PDC may not always maintain its ∼ 10 MDa organization, but is rather variable. We propose that the flexible nature of PDC may allow modulation of its activity. © 2020 Lee et al.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Pavlu-Pereira, H.
AU  - Lousa, D.
AU  - Tomé, C.S.
AU  - Florindo, C.
AU  - Silva, M.J.
AU  - de, Almeida I.T.
AU  - Leandro, P.
AU  - Rivera, I.
AU  - Vicente, J.B.
TI  - Structural and functional impact of clinically relevant E1α variants causing pyruvate dehydrogenase complex deficiency
JF  - BIOCHIMIE
J2  - BIOCHIMIE
VL  - 183
PY  - 2021
SP  - 78
EP  - 88
PG  - 11
SN  - 0300-9084
DO  - 10.1016/j.biochi.2021.02.007
UR  - https://m2.mtmt.hu/api/publication/31936105
ID  - 31936105
N1  - Research Institute for Medicines (iMed.ULisboa) and Department of Biochemistry and Human Biology, Faculty of Pharmacy, Universidade de Lisboa, Lisbon, Portugal            
            Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal            
            Cited By :1            
            Export Date: 29 March 2021            
            CODEN: BICMB            
            Correspondence Address: Vicente, J.B.; Instituto de Tecnologia Química e Biológica António Xavier, Av. da República (EAN), Portugal; email: jvicente@itqb.unl.pt            
            Correspondence Address: Leandro, P.; Research Institute for Medicines, Av. Prof. Gama Pinto, Portugal; email: aleandro@ff.ulisboa.pt            
            Correspondence Address: Rivera, I.; Research Institute for Medicines, Av. Prof. Gama Pinto, Portugal; email: iarivera@ff.ulisboa.pt            
            Funding details: LISBOA-01-0145-FEDER-007344, SFRH/BD/91729/2012, UID/DTP/04138/2019            
            Funding text 1: This work was supported by Funda??o para a Ci?ncia e Tecnologia (strategic project UID/DTP/04138/2019 and grant SFRH/BD/91729/2012). iNOVA4Health Research Unit (LISBOA-01-0145-FEDER-007344), which is cofunded by Funda??o para a Ci?ncia e Tecnologia/Minist?rio da Ci?ncia e do Ensino Superior, through national funds, and by FEDER under the PT2020 Partnership Agreement, is acknowledged. We are thankful to Prof. Cl?udio M. Soares for helpful discussions regarding the parameterization of TPP for MD simulations.            
            Funding text 2: This work was supported by Fundação para a Ciência e Tecnologia (strategic project UID/DTP/04138/2019 and grant SFRH/BD/91729/2012 ). iNOVA4Health Research Unit ( LISBOA-01-0145-FEDER-007344 ), which is cofunded by Fundação para a Ciência e Tecnologia/Ministério da Ciência e do Ensino Superior , through national funds, and by FEDER under the PT2020 Partnership Agreement, is acknowledged. We are thankful to Prof. Cláudio M. Soares for helpful discussions regarding the parameterization of TPP for MD simulations.
Research Institute for Medicines (iMed.ULisboa) and Department of Biochemistry and Human Biology, Faculty of Pharmacy, Universidade de Lisboa, Lisbon, Portugal            
            Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal            
            Cited By :1            
            Export Date: 12 August 2021            
            CODEN: BICMB            
            Correspondence Address: Vicente, J.B.; Instituto de Tecnologia Química e Biológica António Xavier, Av. da República (EAN), Portugal; email: jvicente@itqb.unl.pt            
            Correspondence Address: Leandro, P.; Research Institute for Medicines, Av. Prof. Gama Pinto, Portugal; email: aleandro@ff.ulisboa.pt            
            Correspondence Address: Rivera, I.; Research Institute for Medicines, Av. Prof. Gama Pinto, Portugal; email: iarivera@ff.ulisboa.pt            
            Chemicals/CAS: cocarboxylase, 154-87-0; pyruvate dehydrogenase, 9014-20-4; Pyruvate Dehydrogenase (Lipoamide); pyruvate dehydrogenase E1alpha subunit; Thiamine Pyrophosphate            
            Funding details: LISBOA-01-0145-FEDER-007344, SFRH/BD/91729/2012, UID/DTP/04138/2019            
            Funding text 1: This work was supported by Funda??o para a Ci?ncia e Tecnologia (strategic project UID/DTP/04138/2019 and grant SFRH/BD/91729/2012). iNOVA4Health Research Unit (LISBOA-01-0145-FEDER-007344), which is cofunded by Funda??o para a Ci?ncia e Tecnologia/Minist?rio da Ci?ncia e do Ensino Superior, through national funds, and by FEDER under the PT2020 Partnership Agreement, is acknowledged. We are thankful to Prof. Cl?udio M. Soares for helpful discussions regarding the parameterization of TPP for MD simulations.            
            Funding text 2: This work was supported by Fundação para a Ciência e Tecnologia (strategic project UID/DTP/04138/2019 and grant SFRH/BD/91729/2012 ). iNOVA4Health Research Unit ( LISBOA-01-0145-FEDER-007344 ), which is cofunded by Fundação para a Ciência e Tecnologia/Ministério da Ciência e do Ensino Superior , through national funds, and by FEDER under the PT2020 Partnership Agreement, is acknowledged. We are thankful to Prof. Cláudio M. Soares for helpful discussions regarding the parameterization of TPP for MD simulations.
AB  - Pyruvate dehydrogenase complex (PDC) catalyzes the oxidative decarboxylation of pyruvate to acetyl-coenzyme A, hinging glycolysis and the tricarboxylic acid cycle. PDC deficiency, an inborn error of metabolism, has a broad phenotypic spectrum. Symptoms range from fatal lactic acidosis or progressive neuromuscular impairment in the neonatal period, to chronic neurodegeneration. Most disease-causing mutations in PDC deficiency affect the PDHA1 gene, encoding the α subunit of the PDC-E1 component. Detailed biophysical analysis of pathogenic protein variants is a challenging approach to support the design of therapies based on improving and correcting protein structure and function. Herein, we report the characterization of clinically relevant PDC-E1α variants identified in Portuguese PDC deficient patients. These variants bear amino acid substitutions in different structural regions of PDC-E1α. The structural and functional analyses of recombinant heterotetrameric (αα’ββ’) PDC-E1 variants, combined with molecular dynamics (MD) simulations, show a limited impact of the amino acid changes on the conformational stability, apart from the increased propensity for aggregation of the p.R253G variant as compared to wild-type PDC-E1. However, all variants presented a functional impairment in terms of lower residual PDC-E1 enzymatic activity and ≈3–100 × lower affinity for the thiamine pyrophosphate (TPP) cofactor, in comparison with wild-type PDC-E1. MD simulations neatly showed generally decreased stability (increased flexibility) of all variants with respect to the WT heterotetramer, particularly in the TPP binding region. These results are discussed in light of disease severity of the patients bearing such mutations and highlight the difficulty of developing chaperone-based therapies for PDC deficiency. © 2021 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Bunik, Victoria I.
TI  - Redox-Driven Signaling: 2-Oxo Acid Dehydrogenase Complexes as Sensors and Transmitters of Metabolic Imbalance
JF  - ANTIOXIDANTS & REDOX SIGNALING
J2  - ANTIOXID REDOX SIGNAL
VL  - 30
PY  - 2019
IS  - 16
SP  - 1911
EP  - 1947
PG  - 37
SN  - 1523-0864
DO  - 10.1089/ars.2017.7311
UR  - https://m2.mtmt.hu/api/publication/30672811
ID  - 30672811
N1  - Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :1            
            Export Date: 3 December 2019            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State UniversityRussian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4            
            Funding details: California Department of Fish and Game            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, 18-14-00116            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :1            
            Export Date: 28 January 2020            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State UniversityRussian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4            
            Funding details: California Department of Fish and Game            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, 18-14-00116            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :3            
            Export Date: 27 May 2020            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State UniversityRussian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4            
            Funding details: Deutsche Forschungsgemeinschaft, DFG            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, RSF, 18-14-00116            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :5            
            Export Date: 4 January 2021            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State UniversityRussian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4; iron, 14093-02-8, 53858-86-9, 7439-89-6; mixed function oxidase, 9040-60-2; protein disulfide reductase (glutathione), 9082-53-5; Iron; Keto Acids; Mixed Function Oxygenases; Multienzyme Complexes; Oxygen; Protein Disulfide Reductase (Glutathione); Reactive Nitrogen Species; Reactive Oxygen Species; Thioredoxins; TXN protein, human            
            Funding details: Deutsche Forschungsgemeinschaft, DFG            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, RSF, 18-14-00116            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :5            
            Export Date: 29 January 2021            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Russian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4; iron, 14093-02-8, 53858-86-9, 7439-89-6; mixed function oxidase, 9040-60-2; protein disulfide reductase (glutathione), 9082-53-5; Iron; Keto Acids; Mixed Function Oxygenases; Multienzyme Complexes; Oxygen; Protein Disulfide Reductase (Glutathione); Reactive Nitrogen Species; Reactive Oxygen Species; Thioredoxins; TXN protein, human            
            Funding details: Deutsche Forschungsgemeinschaft, DFG            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, RSF, 18-14-00116            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :7            
            Export Date: 1 April 2021            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Russian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4; iron, 14093-02-8, 53858-86-9, 7439-89-6; mixed function oxidase, 9040-60-2; protein disulfide reductase (glutathione), 9082-53-5; Iron; Keto Acids; Mixed Function Oxygenases; Multienzyme Complexes; Oxygen; Protein Disulfide Reductase (Glutathione); Reactive Nitrogen Species; Reactive Oxygen Species; Thioredoxins; TXN protein, human            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding details: Deutsche Forschungsgemeinschaft, DFG            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, RSF, 18-14-00116            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :9            
            Export Date: 3 May 2021            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Russian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4; iron, 14093-02-8, 53858-86-9, 7439-89-6; mixed function oxidase, 9040-60-2; protein disulfide reductase (glutathione), 9082-53-5; Iron; Keto Acids; Mixed Function Oxygenases; Multienzyme Complexes; Oxygen; Protein Disulfide Reductase (Glutathione); Reactive Nitrogen Species; Reactive Oxygen Species; Thioredoxins; TXN protein, human            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding details: Deutsche Forschungsgemeinschaft, DFG            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, RSF, 18-14-00116            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :9            
            Export Date: 6 May 2021            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Russian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4; iron, 14093-02-8, 53858-86-9, 7439-89-6; mixed function oxidase, 9040-60-2; protein disulfide reductase (glutathione), 9082-53-5; Iron; Keto Acids; Mixed Function Oxygenases; Multienzyme Complexes; Oxygen; Protein Disulfide Reductase (Glutathione); Reactive Nitrogen Species; Reactive Oxygen Species; Thioredoxins; TXN protein, human            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding details: Deutsche Forschungsgemeinschaft, DFG            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, RSF, 18-14-00116            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
Belozersky Institute of Physicochemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russian Federation            
            Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russian Federation            
            Cited By :12            
            Export Date: 12 August 2021            
            CODEN: ARSIF            
            Correspondence Address: Bunik, V.I.; Belozersky Institute of Physicochemical Biology, Russian Federation; email: bunik@belozersky.msu.ru            
            Chemicals/CAS: 2 oxoisovalerate dehydrogenase (lipoamide), 9082-72-8; acyltransferase, 9012-30-0, 9054-54-0; carbon, 7440-44-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glutaredoxin, 157514-02-8; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; oxygen, 7782-44-7; peroxidase, 9003-99-0; pyruvate dehydrogenase, 9014-20-4; superoxide, 11062-77-4; thioredoxin, 52500-60-4; iron, 14093-02-8, 53858-86-9, 7439-89-6; mixed function oxidase, 9040-60-2; protein disulfide reductase (glutathione), 9082-53-5; Iron; Keto Acids; Mixed Function Oxygenases; Multienzyme Complexes; Oxygen; Protein Disulfide Reductase (Glutathione); Reactive Nitrogen Species; Reactive Oxygen Species; Thioredoxins; TXN protein, human            
            Funding details: Alexander von Humboldt-Stiftung            
            Funding details: Deutsche Forschungsgemeinschaft, DFG            
            Funding details: Volkswagen Foundation            
            Funding details: Russian Science Foundation, RSF, 18-14-00116            
            Funding text 1: V.I.B. greatly acknowledges her cooperation with Prof. Dr. Hartmut Follmann (GhK Kassel, Germany) on the thioredoxin interaction with 2-oxo acid dehydrogenase complexes, supported by Volkswagen Foundation and DFG (Germany), and with Dr. Christian Sievers (Tubingen University, Germany) on EPR studies of radical species, supported by Alexander von Humboldt Foundation (Germany). The author thanks Dr. Garik Mkrtchyan (Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark) and Mr. Artem Artiukhov (Lomonosov Moscow State University, Russia) for their qualified technical help in preparation of this article for publication. Research work of V.I.B. is currently supported by the Russian Science Foundation (Grant No. 18-14-00116).
AB  - Significance: This article develops a holistic view on production of reactive oxygen species (ROS) by 2-oxo acid dehydrogenase complexes.Recent Advances: Catalytic and structural properties of the complexes and their components evolved to minimize damaging effects of side reactions, including ROS generation, simultaneously exploiting the reactions for homeostatic signaling.Critical Issues: Side reactions of the complexes, characterized in vitro, are analyzed in view of protein interactions and conditions in vivo. Quantitative data support prevalence of the forward 2-oxo acid oxidation over the backward NADH oxidation in feeding physiologically significant ROS production by the complexes. Special focus on interactions between the active sites within 2-oxo acid dehydrogenase complexes highlights the central relevance of the complex-bound thiyl radicals in regulation of and signaling by complex-generated ROS. The thiyl radicals arise when dihydrolipoyl residues of the complexes regenerate FADH(2) from the flavin semiquinone coproduced with superoxide anion radical in 1e(-) oxidation of FADH(2) by molecular oxygen.Future Directions: Interaction of 2-oxo acid dehydrogenase complexes with thioredoxins (TRXs), peroxiredoxins, and glutaredoxins mediates scavenging of the thiyl radicals and ROS generated by the complexes, underlying signaling of disproportional availability of 2-oxo acids, CoA, and NAD(+) in key metabolic branch points through thiol/disulfide exchange and medically important hypoxia-inducible factor, mammalian target of rapamycin (mTOR), poly (ADP-ribose) polymerase, and sirtuins. High reactivity of the coproduced ROS and thiyl radicals to iron/sulfur clusters and nitric oxide, peroxynitrite reductase activity of peroxiredoxins and transnitrosylating function of thioredoxin, implicate the side reactions of 2-oxo acid dehydrogenase complexes in nitric oxide-dependent signaling and damage.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Han, Chendong
AU  - Goodwine, James
AU  - Romero, Nicholas
AU  - Steck, Kyle S.
AU  - Sauer, Karin
AU  - Doiron, Amber
TI  - Enzyme-encapsulating polymeric nanoparticles: A potential adjunctive therapy in Pseudomonas aeruginosa biofilm-associated infection treatment
JF  - COLLOIDS AND SURFACES B: BIOINTERFACES
J2  - COLLOID SURFACE B
VL  - 184
PY  - 2019
PG  - 9
SN  - 0927-7765
DO  - 10.1016/j.colsurfb.2019.110512
UR  - https://m2.mtmt.hu/api/publication/31566924
ID  - 31566924
N1  - Department of Biomedical Engineering, Binghamton University, Binghamton, NY 13902, United States            
            Department of Biological Science, Binghamton University, Binghamton, NY 13902, United States            
            Binghamton Biofilm Research Center, Binghamton University, Binghamton, NY 13902, United States            
            Department of Electrical and Biomedical Engineering, University of Vermont, Burlington, VT 05405, United States            
            Cited By :5            
            Export Date: 1 April 2021            
            CODEN: CSBBE            
            Correspondence Address: Doiron, A.; Department of Electrical and Biomedical Engineering, United States; email: amber.doiron@uvm.edu            
            Chemicals/CAS: polyglactin, 26780-50-7, 34346-01-5; pyruvate dehydrogenase, 9014-20-4; Anti-Bacterial Agents; Biocompatible Materials; Polylactic Acid-Polyglycolic Acid Copolymer; Pyruvate Dehydrogenase Complex            
            Funding details: National Institutes of Health, NIH            
            Funding details: National Institute of Allergy and Infectious Diseases, NIAID, R56AI127815            
            Funding details: Binghamton University            
            Funding text 1: Funding for this work was provided by the NIH (1R56AI127815-01A1), Binghamton University Transdisciplinary Areas of Excellence and Interdisciplinary Collaboration Grants awards, and the Binghamton University Analytics and Diagnostics Laboratory.
Department of Biomedical Engineering, Binghamton University, Binghamton, NY 13902, United States            
            Department of Biological Science, Binghamton University, Binghamton, NY 13902, United States            
            Binghamton Biofilm Research Center, Binghamton University, Binghamton, NY 13902, United States            
            Department of Electrical and Biomedical Engineering, University of Vermont, Burlington, VT 05405, United States            
            Cited By :8            
            Export Date: 12 August 2021            
            CODEN: CSBBE            
            Correspondence Address: Doiron, A.; Department of Electrical and Biomedical Engineering, United States; email: amber.doiron@uvm.edu            
            Chemicals/CAS: polyglactin, 26780-50-7, 34346-01-5; pyruvate dehydrogenase, 9014-20-4; Anti-Bacterial Agents; Biocompatible Materials; Polylactic Acid-Polyglycolic Acid Copolymer; Pyruvate Dehydrogenase Complex            
            Funding details: National Institutes of Health, NIH            
            Funding details: National Institute of Allergy and Infectious Diseases, NIAID, R56AI127815            
            Funding details: Binghamton University            
            Funding text 1: Funding for this work was provided by the NIH (1R56AI127815-01A1), Binghamton University Transdisciplinary Areas of Excellence and Interdisciplinary Collaboration Grants awards, and the Binghamton University Analytics and Diagnostics Laboratory.
AB  - Pseudomonas aeruginosa is a pathogen known to be associated with a variety of diseases and conditions such as cystic fibrosis, chronic wound infections, and burn wound infections. A novel approach was developed to combat the problem of biofilm antibiotic tolerance by reverting biofilm bacteria back to the planktonic mode of growth. This reversion was achieved through the enzymatic depletion of available pyruvate using pyruvate dehydrogenase, which induced biofilm bacteria to disperse from the surface-associated mode of growth into the surrounding environment. However, direct use of the enzyme in clinical settings is not practical as the enzyme is susceptible to denaturation under various storage conditions. We hypothesize that by encapsulating pyruvate dehydrogenase into degradable, biocompatible poly(lactic-co-glycolic) acid nanoparticles, the activity of the enzyme can be extended to deplete available pyruvate and induce dispersion of mature Pseudomonas aeruginosa biofilms. Several particle formulations were attempted in order to permit the use of the smallest dose of nanoparticles while maintaining pyruvate dehydrogenase activity for an extended time length. The nanoparticles synthesized using the optimal formulation showed an average size of 266.7 +/- 1.8 nm. The encapsulation efficiency of pyruvate dehydrogenase was measured at 17.9 +/- 1.4%. Most importantly, the optimal formulation dispersed biofilms and exhibited enzymatic activity after being stored at 37 degrees C for 6 days.
LA  - English
DB  - MTMT
ER  - 

TY  - BOOK
AU  - Artiukhov, A
AU  - Bunik, V
TI  - Vitamin-dependent multienzyme complexes of 2-oxo acid dehydrogenases: Structure, function, regulation and medical implications
T3  - Biochemistry Research Trends
PB  - Nova Science Publishers
CY  - New York, New York
PY  - 2017
SP  - 203
SN  - 9781536121667
UR  - https://m2.mtmt.hu/api/publication/27132991
ID  - 27132991
N1  - Cited By :12            
            Export Date: 12 August 2021
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Ng, F
AU  - Tang, BL
TI  - Pyruvate dehydrogenase complex (PDC) export from the mitochondrial matrix
JF  - MOLECULAR MEMBRANE BIOLOGY
J2  - MOL MEMBR BIOL
VL  - 31
PY  - 2014
IS  - 7-8
SP  - 207
EP  - 210
PG  - 4
SN  - 0968-7688
DO  - 10.3109/09687688.2014.987183
UR  - https://m2.mtmt.hu/api/publication/24453783
ID  - 24453783
N1  - Cited By :5            
            Export Date: 8 August 2019            
            CODEN: MMEBE            
            Correspondence Address: Tang, B.L.; NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, 8 Medical Drive, Singapore            
            Chemicals/CAS: parkin, 356136-82-8; Pyruvate Dehydrogenase Complex            
            Funding text 1: This work was supported by the NUS Graduate School for Integrative Sciences and Engineering.
Cited By :7            
            Export Date: 29 January 2021            
            CODEN: MMEBE            
            Correspondence Address: Tang, B.L.; NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, 8 Medical Drive, Singapore            
            Chemicals/CAS: parkin, 356136-82-8; Pyruvate Dehydrogenase Complex            
            Funding text 1: This work was supported by the NUS Graduate School for Integrative Sciences and Engineering.
Cited By :7            
            Export Date: 1 April 2021            
            CODEN: MMEBE            
            Correspondence Address: Tang, B.L.; NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, 8 Medical Drive, Singapore            
            Chemicals/CAS: parkin, 356136-82-8; Pyruvate Dehydrogenase Complex            
            Funding text 1: This work was supported by the NUS Graduate School for Integrative Sciences and Engineering.
Cited By :9            
            Export Date: 12 August 2021            
            CODEN: MMEBE            
            Correspondence Address: Tang, B.L.; NUS Graduate School for Integrative Sciences and Engineering, National University of Singapore, 8 Medical Drive, Singapore            
            Chemicals/CAS: parkin, 356136-82-8; Pyruvate Dehydrogenase Complex            
            Funding text 1: This work was supported by the NUS Graduate School for Integrative Sciences and Engineering.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Sutendra, G
AU  - Kinnaird, A
AU  - Dromparis, P
AU  - Paulin, R
AU  - Stenson, TH
AU  - Haromy, A
AU  - Hashimoto, K
AU  - Zhang, N
AU  - Flaim, E
AU  - Michelakis, ED
TI  - A nuclear pyruvate dehydrogenase complex is important for the generation of Acetyl-CoA and histone acetylation
JF  - CELL
J2  - CELL
VL  - 158
PY  - 2014
IS  - 1
SP  - 84
EP  - 97
PG  - 14
SN  - 0092-8674
DO  - 10.1016/j.cell.2014.04.046
UR  - https://m2.mtmt.hu/api/publication/24131865
ID  - 24131865
N1  - Department of Medicine, University of Alberta, Edmonton, AB T6G 2B7, Canada            
            NanoFAB Fabrication and Characterization Facility, University of Alberta, Edmonton, AB T6G 2B7, Canada            
            Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom            
            Cited By :174            
            Export Date: 8 August 2019            
            CODEN: CELLB            
            Correspondence Address: Sutendra, G.; Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom; email: gopinath.sutendra@ludwig.ox.ac.uk            
            Chemicals/CAS: acetyl coenzyme A, 72-89-9; epidermal growth factor, 62229-50-9; lysine, 56-87-1, 6899-06-5, 70-54-2            
            Funding details: Canadian Institutes of Health Research            
            Funding details: Alberta Innovates - Health Solutions            
            Funding text 1: We would like to thank Dr. Ryan McKay of the Canadian National High Field NMR Centre (NANUC) and Chenomx for the NMR acquisition and data analysis, Dr. Nasser Tahbaz (University of Alberta) for the immunogold labeling and electron microscopy, and Dr. Gregg Semenza (Johns Hopkins University) for the adenoviruses encoding LacZ and CA5. This study was funded by the Canadian Institutes for Health Research, the Alberta Innovation for Health Solutions, and the Hecht Foundation (Vancouver, Canada) to E.D.M.
Department of Medicine, University of Alberta, Edmonton, AB T6G 2B7, Canada            
            NanoFAB Fabrication and Characterization Facility, University of Alberta, Edmonton, AB T6G 2B7, Canada            
            Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom            
            Cited By :249            
            Export Date: 29 January 2021            
            CODEN: CELLB            
            Correspondence Address: Sutendra, G.; Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom; email: gopinath.sutendra@ludwig.ox.ac.uk            
            Chemicals/CAS: acetyl coenzyme A, 72-89-9; epidermal growth factor, 62229-50-9; lysine, 56-87-1, 6899-06-5, 70-54-2            
            Funding details: Canadian Institutes of Health Research, CIHR            
            Funding details: Alberta Innovates - Health Solutions, AIHS            
            Funding details: Lotte and John Hecht Memorial Foundation            
            Funding text 1: We would like to thank Dr. Ryan McKay of the Canadian National High Field NMR Centre (NANUC) and Chenomx for the NMR acquisition and data analysis, Dr. Nasser Tahbaz (University of Alberta) for the immunogold labeling and electron microscopy, and Dr. Gregg Semenza (Johns Hopkins University) for the adenoviruses encoding LacZ and CA5. This study was funded by the Canadian Institutes for Health Research, the Alberta Innovation for Health Solutions, and the Hecht Foundation (Vancouver, Canada) to E.D.M.
Department of Medicine, University of Alberta, Edmonton, AB T6G 2B7, Canada            
            NanoFAB Fabrication and Characterization Facility, University of Alberta, Edmonton, AB T6G 2B7, Canada            
            Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom            
            Cited By :255            
            Export Date: 1 April 2021            
            CODEN: CELLB            
            Correspondence Address: Sutendra, G.; Ludwig Institute for Cancer Research, , Oxford OX3 7DQ, United Kingdom; email: gopinath.sutendra@ludwig.ox.ac.uk            
            Chemicals/CAS: acetyl coenzyme A, 72-89-9; epidermal growth factor, 59459-45-9, 62229-50-9; lysine, 56-87-1, 6899-06-5, 70-54-2            
            Funding details: Canadian Institutes of Health Research, CIHR            
            Funding text 1: We would like to thank Dr. Ryan McKay of the Canadian National High Field NMR Centre (NANUC) and Chenomx for the NMR acquisition and data analysis, Dr. Nasser Tahbaz (University of Alberta) for the immunogold labeling and electron microscopy, and Dr. Gregg Semenza (Johns Hopkins University) for the adenoviruses encoding LacZ and CA5. This study was funded by the Canadian Institutes for Health Research, the Alberta Innovation for Health Solutions, and the Hecht Foundation (Vancouver, Canada) to E.D.M.
Department of Medicine, University of Alberta, Edmonton, AB T6G 2B7, Canada            
            NanoFAB Fabrication and Characterization Facility, University of Alberta, Edmonton, AB T6G 2B7, Canada            
            Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, United Kingdom            
            Cited By :282            
            Export Date: 12 August 2021            
            CODEN: CELLB            
            Correspondence Address: Sutendra, G.; Ludwig Institute for Cancer Research, , Oxford OX3 7DQ, United Kingdom; email: gopinath.sutendra@ludwig.ox.ac.uk            
            Chemicals/CAS: acetyl coenzyme A, 72-89-9; epidermal growth factor, 59459-45-9, 62229-50-9; lysine, 56-87-1, 6899-06-5, 70-54-2            
            Funding details: Canadian Institutes of Health Research, CIHR            
            Funding text 1: We would like to thank Dr. Ryan McKay of the Canadian National High Field NMR Centre (NANUC) and Chenomx for the NMR acquisition and data analysis, Dr. Nasser Tahbaz (University of Alberta) for the immunogold labeling and electron microscopy, and Dr. Gregg Semenza (Johns Hopkins University) for the adenoviruses encoding LacZ and CA5. This study was funded by the Canadian Institutes for Health Research, the Alberta Innovation for Health Solutions, and the Hecht Foundation (Vancouver, Canada) to E.D.M.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Kim, SY Kim J
TI  - Roles of dihydrolipoamide dehydrogenase Lpd1 in Candida albicans filamentation
JF  - FUNGAL GENETICS AND BIOLOGY
J2  - FUNGAL GENET BIOL
VL  - 47
PY  - 2010
IS  - 9
SP  - 782
EP  - 789
PG  - 8
SN  - 1087-1845
DO  - 10.1016/j.fgb.2010.06.005
UR  - https://m2.mtmt.hu/api/publication/21254142
ID  - 21254142
N1  - Cited By :11            
            Export Date: 8 August 2019            
            CODEN: FGBIF            
            Correspondence Address: Kim, J.; Department of Microbiology and Molecular Biology, College of Biosciences and Biotechnology, Chungnam National University, Yuseong-Gu, Gung-Dong 220, Daejeon 305-764, South Korea; email: jmkim@cnu.ac.kr            
            Chemicals/CAS: acetic acid, 127-08-2, 127-09-3, 64-19-7, 71-50-1; alcohol, 64-17-5; carbon, 7440-44-0; citric acid, 126-44-3, 5949-29-1, 77-92-9, 8002-14-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glucose, 50-99-7, 84778-64-3; glycerol, 56-81-5; hydrogen peroxide, 7722-84-1; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; Dihydrolipoamide Dehydrogenase, 1.8.1.4; Fungal Proteins; Dihydrolipoamide Dehydrogenase; Fungal Proteins            
            Funding details: Ministry of Education, Government of the People's Republic of Bangladesh            
            Funding details: RO1-2006-000-10841-0            
            Funding text 1: This work was supported by a grant from the Korean Science and Engineering Foundation (RO1-2006-000-10841-0) to J. Kim. S.-Y. Kim was supported by the BK21 program administered by the Ministry of Education, Republic of Korea.
Cited By :12            
            Export Date: 29 January 2021            
            CODEN: FGBIF            
            Correspondence Address: Kim, J.; Department of Microbiology and Molecular Biology, Yuseong-Gu, Gung-Dong 220, Daejeon 305-764, South Korea; email: jmkim@cnu.ac.kr            
            Chemicals/CAS: acetic acid, 127-08-2, 127-09-3, 64-19-7, 71-50-1; alcohol, 64-17-5; carbon, 7440-44-0; citric acid, 126-44-3, 5949-29-1, 77-92-9, 8002-14-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glucose, 50-99-7, 84778-64-3; glycerol, 56-81-5; hydrogen peroxide, 7722-84-1; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; Dihydrolipoamide Dehydrogenase, 1.8.1.4; Fungal Proteins; Dihydrolipoamide Dehydrogenase; Fungal Proteins            
            Funding details: RO1-2006-000-10841-0            
            Funding text 1: This work was supported by a grant from the Korean Science and Engineering Foundation (RO1-2006-000-10841-0) to J. Kim. S.-Y. Kim was supported by the BK21 program administered by the Ministry of Education, Republic of Korea.
Cited By :12            
            Export Date: 1 April 2021            
            CODEN: FGBIF            
            Correspondence Address: Kim, J.; Department of Microbiology and Molecular Biology, Yuseong-Gu, Gung-Dong 220, Daejeon 305-764, South Korea; email: jmkim@cnu.ac.kr            
            Chemicals/CAS: acetic acid, 127-08-2, 127-09-3, 64-19-7, 71-50-1; alcohol, 64-17-5; carbon, 7440-44-0; citric acid, 126-44-3, 5949-29-1, 77-92-9, 8002-14-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glucose, 50-99-7, 84778-64-3; glycerol, 56-81-5; hydrogen peroxide, 7722-84-1; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; Dihydrolipoamide Dehydrogenase, 1.8.1.4; Fungal Proteins; Dihydrolipoamide Dehydrogenase; Fungal Proteins            
            Funding details: Ministry of Education, MOE            
            Funding details: Korea Science and Engineering Foundation, KOSEF, RO1-2006-000-10841-0            
            Funding text 1: This work was supported by a grant from the Korean Science and Engineering Foundation (RO1-2006-000-10841-0) to J. Kim. S.-Y. Kim was supported by the BK21 program administered by the Ministry of Education, Republic of Korea.
Cited By :12            
            Export Date: 12 August 2021            
            CODEN: FGBIF            
            Correspondence Address: Kim, J.; Department of Microbiology and Molecular Biology, Yuseong-Gu, Gung-Dong 220, Daejeon 305-764, South Korea; email: jmkim@cnu.ac.kr            
            Chemicals/CAS: acetic acid, 127-08-2, 127-09-3, 64-19-7, 71-50-1; alcohol, 64-17-5; carbon, 7440-44-0; citric acid, 126-44-3, 5949-29-1, 77-92-9, 8002-14-0; dihydrolipoamide dehydrogenase, 37340-89-9, 9001-18-7; glucose, 50-99-7, 84778-64-3; glycerol, 56-81-5; hydrogen peroxide, 7722-84-1; Dihydrolipoamide Dehydrogenase; Fungal Proteins            
            Funding details: Ministry of Education, MOE            
            Funding details: Korea Science and Engineering Foundation, KOSEF, RO1-2006-000-10841-0            
            Funding text 1: This work was supported by a grant from the Korean Science and Engineering Foundation (RO1-2006-000-10841-0) to J. Kim. S.-Y. Kim was supported by the BK21 program administered by the Ministry of Education, Republic of Korea.
LA  - English
DB  - MTMT
ER  - 

TY  - CHAP
AU  - Balish, MF
AU  - Krause, DC
ED  - Razin, S
ED  - Herrmann, R
TI  - Cytadherence and the Cytoskeleton
T2  - Molecular Biology and Pathogenicity of Mycoplasmas 2002
PY  - 2002
SP  - 491
EP  - 518
PG  - 28
UR  - https://m2.mtmt.hu/api/publication/10038476
ID  - 10038476
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Melegh, Béla
AU  - Skuta, G
AU  - Pajor, László
AU  - Hegedus, G
AU  - Sümegi, Balázs
TI  - Autoantibodies against subunits of pyruvate dehydrogenase and citrate synthase in a case of paediatric biliary cirrhosis
JF  - GUT
J2  - GUT
VL  - 42
PY  - 1998
SP  - 753
EP  - 756
PG  - 4
SN  - 0017-5749
DO  - 10.1136/gut.42.5.753
UR  - https://m2.mtmt.hu/api/publication/1003011
ID  - 1003011
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Krungkrai, J
TI  - PURIFICATION, CHARACTERIZATION AND LOCALIZATION OF MITOCHONDRIAL DIHYDROOROTATE DEHYDROGENASE IN PLASMODIUM-FALCIPARUM, HUMAN MALARIA PARASITE
JF  - BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
J2  - BBA-GEN SUBJECTS
VL  - 1243
PY  - 1995
SP  - 351
EP  - 360
PG  - 10
SN  - 0304-4165
DO  - 10.1016/0304-4165(94)00158-T
UR  - https://m2.mtmt.hu/api/publication/20173391
ID  - 20173391
N1  - Cited By :87            
            Export Date: 8 August 2019            
            CODEN: BBGSB            
            Correspondence Address: Krungkrai, J.; Department of Biochemistry, Faculty of Medicine, Chulalongkorn Uniuersity, Rama IV Rd, Bangkok, 10330, Thailand; email: fmedjkk@chulkn.chula.ac.th            
            Chemicals/CAS: Benzoquinones; Cytochrome-c Oxidase, EC 1.9.3.1; dihydroorotate dehydrogenase, EC 1.3.99.11; Gold, 7440-57-5; NADH Dehydrogenase, EC 1.6.99.3; Naphthoquinones; Orotic Acid, 65-86-1; Oxidoreductases, EC 1.; Ubiquinone, 1339-63-5            
            Funding text 1: We thank S.R. Krungkrai, A. Bhumiratana, P. Learn-garamkul, R. Kanjanarithisak, S. Vetchagarun for their technical assistance with parasite cultivation, enzyme purification and EM techniques. This work was supported by the UNDP/World Bank/WHO Special Programme for Research and Training in Tropical Diseases, and also by the Research Affairs Division of Chulalongkorn University.
Cited By :91            
            Export Date: 29 January 2021            
            CODEN: BBGSB            
            Correspondence Address: Krungkrai, J.; Department of Biochemistry, Faculty of Medicine, Chulalongkorn Uniuersity, Rama IV Rd, Bangkok, 10330, Thailand; email: fmedjkk@chulkn.chula.ac.th            
            Chemicals/CAS: Benzoquinones; Cytochrome-c Oxidase, EC 1.9.3.1; dihydroorotate dehydrogenase, EC 1.3.99.11; Gold, 7440-57-5; NADH Dehydrogenase, EC 1.6.99.3; Naphthoquinones; Orotic Acid, 65-86-1; Oxidoreductases, EC 1.; Ubiquinone, 1339-63-5            
            Funding details: Chulalongkorn University, CU            
            Funding text 1: We thank S.R. Krungkrai, A. Bhumiratana, P. Learn-garamkul, R. Kanjanarithisak, S. Vetchagarun for their technical assistance with parasite cultivation, enzyme purification and EM techniques. This work was supported by the UNDP/World Bank/WHO Special Programme for Research and Training in Tropical Diseases, and also by the Research Affairs Division of Chulalongkorn University.
Cited By :91            
            Export Date: 1 April 2021            
            CODEN: BBGSB            
            Correspondence Address: Krungkrai, J.; Department of Biochemistry, Faculty of Medicine, Chulalongkorn Uniuersity, Rama IV Rd, Bangkok, 10330, Thailand; email: fmedjkk@chulkn.chula.ac.th            
            Chemicals/CAS: Benzoquinones; Cytochrome-c Oxidase, EC 1.9.3.1; dihydroorotate dehydrogenase, EC 1.3.99.11; Gold, 7440-57-5; NADH Dehydrogenase, EC 1.6.99.3; Naphthoquinones; Orotic Acid, 65-86-1; Oxidoreductases, EC 1.; Ubiquinone, 1339-63-5            
            Funding details: Chulalongkorn University, CU            
            Funding details: World Health Organization, WHO            
            Funding details: World Bank Group, WBG            
            Funding details: United Nations Development Programme, UNDP            
            Funding text 1: We thank S.R. Krungkrai, A. Bhumiratana, P. Learn-garamkul, R. Kanjanarithisak, S. Vetchagarun for their technical assistance with parasite cultivation, enzyme purification and EM techniques. This work was supported by the UNDP/World Bank/WHO Special Programme for Research and Training in Tropical Diseases, and also by the Research Affairs Division of Chulalongkorn University.
Cited By :91            
            Export Date: 12 August 2021            
            CODEN: BBGSB            
            Correspondence Address: Krungkrai, J.; Department of Biochemistry, Faculty of Medicine, Chulalongkorn Uniuersity, Rama IV Rd, Bangkok, 10330, Thailand; email: fmedjkk@chulkn.chula.ac.th            
            Chemicals/CAS: Benzoquinones; Cytochrome-c Oxidase, EC 1.9.3.1; dihydroorotate dehydrogenase, EC 1.3.99.11; Gold, 7440-57-5; NADH Dehydrogenase, EC 1.6.99.3; Naphthoquinones; Orotic Acid, 65-86-1; Oxidoreductases, EC 1.; Ubiquinone, 1339-63-5            
            Funding details: Chulalongkorn University, CU            
            Funding text 1: We thank S.R. Krungkrai, A. Bhumiratana, P. Learn-garamkul, R. Kanjanarithisak, S. Vetchagarun for their technical assistance with parasite cultivation, enzyme purification and EM techniques. This work was supported by the UNDP/World Bank/WHO Special Programme for Research and Training in Tropical Diseases, and also by the Research Affairs Division of Chulalongkorn University.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Sonia, Beeckmans
AU  - Edilbert, Van Driessche
AU  - Louis, Kanarek
TI  - Immobilized enzymes as tools for the demonstration of metabolon formation. A short overview
JF  - JOURNAL OF MOLECULAR RECOGNITION
J2  - J MOL RECOGNIT
VL  - 6
PY  - 1993
IS  - 4
SP  - 195
EP  - 204
PG  - 10
SN  - 0952-3499
DO  - 10.1002/jmr.300060408
UR  - https://m2.mtmt.hu/api/publication/22861805
ID  - 22861805
N1  - Cited By :17            
            Export Date: 8 August 2019            
            Correspondence Address: Beeckmans, S.; Laboratorium Voor Chemie Der Proteïnen, Vrije Universiteit Brussel, Paardenstraat 65, Sint-Genesium-Rode, B-1640, Belgium            
            Chemicals/CAS: glyoxylic acid, 298-12-4; Enzymes, Immobilized; Glyoxylates; glyoxylic acid, 298-12-4
Cited By :18            
            Export Date: 29 January 2021            
            Correspondence Address: Beeckmans, S.; Laboratorium Voor Chemie Der Proteïnen, Paardenstraat 65, Sint-Genesium-Rode, B-1640, Belgium            
            Chemicals/CAS: glyoxylic acid, 298-12-4; Enzymes, Immobilized; Glyoxylates; glyoxylic acid, 298-12-4
Cited By :18            
            Export Date: 1 April 2021            
            Correspondence Address: Beeckmans, S.; Laboratorium Voor Chemie Der Proteïnen, Paardenstraat 65, Sint-Genesium-Rode, B-1640, Belgium            
            Chemicals/CAS: glyoxylic acid, 298-12-4; Enzymes, Immobilized; Glyoxylates; glyoxylic acid, 298-12-4
Cited By :19            
            Export Date: 12 August 2021            
            Correspondence Address: Beeckmans, S.; Laboratorium Voor Chemie Der Proteïnen, Paardenstraat 65, Sint-Genesium-Rode, B-1640, Belgium            
            Chemicals/CAS: glyoxylic acid, 298-12-4; Enzymes, Immobilized; Glyoxylates; glyoxylic acid, 298-12-4
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Hemila, H
AU  - Palva, A
AU  - Paulin, L
AU  - Adler, L
AU  - Arvidson, S
AU  - Palva, I
TI  - THE SECRETORY S-COMPLEX IN BACILLUS-SUBTILIS IS IDENTIFIED AS PYRUVATE-DEHYDROGENASE
JF  - RESEARCH IN MICROBIOLOGY
J2  - RES MICROBIOL
VL  - 142
PY  - 1991
SP  - 779
EP  - 785
PG  - 7
SN  - 0923-2508
DO  - 10.1016/0923-2508(91)90055-F
UR  - https://m2.mtmt.hu/api/publication/20173070
ID  - 20173070
N1  - Institute of Biotechnology, Valimotie 7, 00380 Helsinki, Finland            
            Department of Bacteriology, Karolinska Institute, S-104 01 Stockholm, Sweden            
            Cited By :4            
            Export Date: 8 August 2019            
            CODEN: RMCRE            
            Correspondence Address: Hemilä, H.; Institute of Biotechnology, Valimotie 7, 00380 Helsinki, Finland            
            Chemicals/CAS: pyruvate dehydrogenase, 9014-20-4; Bacterial Proteins; DNA, Bacterial; Pyruvate Dehydrogenase Complex
Institute of Biotechnology, Valimotie 7, 00380 Helsinki, Finland            
            Department of Bacteriology, Karolinska Institute, S-104 01 Stockholm, Sweden            
            Cited By :4            
            Export Date: 29 January 2021            
            CODEN: RMCRE            
            Correspondence Address: Hemilä, H.; Institute of Biotechnology, Valimotie 7, 00380 Helsinki, Finland            
            Chemicals/CAS: pyruvate dehydrogenase, 9014-20-4; Bacterial Proteins; DNA, Bacterial; Pyruvate Dehydrogenase Complex
Institute of Biotechnology, Valimotie 7, 00380 Helsinki, Finland            
            Department of Bacteriology, Karolinska Institute, S-104 01 Stockholm, Sweden            
            Cited By :4            
            Export Date: 1 April 2021            
            CODEN: RMCRE            
            Correspondence Address: Hemilä, H.; Institute of Biotechnology, Valimotie 7, 00380 Helsinki, Finland            
            Chemicals/CAS: pyruvate dehydrogenase, 9014-20-4; Bacterial Proteins; DNA, Bacterial; Pyruvate Dehydrogenase Complex
Institute of Biotechnology, Valimotie 7, 00380 Helsinki, Finland            
            Department of Bacteriology, Karolinska Institute, S-104 01 Stockholm, Sweden            
            Cited By :4            
            Export Date: 12 August 2021            
            CODEN: RMCRE            
            Correspondence Address: Hemilä, H.; Institute of Biotechnology, Valimotie 7, 00380 Helsinki, Finland            
            Chemicals/CAS: pyruvate dehydrogenase, 9014-20-4; Bacterial Proteins; DNA, Bacterial; Pyruvate Dehydrogenase Complex
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Maas, E
AU  - Adami, P
AU  - Bisswanger, H
TI  - APPLICATION OF HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY TO THE PURIFICATION, DISINTEGRATION AND MOLECULAR MASS DETERMINATION OF PYRUVATE-DEHYDROGENASE MULTIENZYME COMPLEXES FROM DIFFERENT SOURCES
JF  - JOURNAL OF CHROMATOGRAPHY A
J2  - J CHROMATOGR A
VL  - 521
PY  - 1990
SP  - 169
EP  - 178
PG  - 10
SN  - 0021-9673
DO  - 10.1016/0021-9673(90)85041-S
UR  - https://m2.mtmt.hu/api/publication/20173394
ID  - 20173394
N1  - Cited By :1            
            Export Date: 8 August 2019            
            CODEN: JCRAE            
            Correspondence Address: Maas, E.; Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Strasse 4, D-7400 Tübingen, Germany            
            Chemicals/CAS: Pyruvate Dehydrogenase Complex
Cited By :1            
            Export Date: 29 January 2021            
            CODEN: JCRAE            
            Correspondence Address: Maas, E.; Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Strasse 4, D-7400 Tübingen, Germany            
            Chemicals/CAS: Pyruvate Dehydrogenase Complex
Cited By :1            
            Export Date: 1 April 2021            
            CODEN: JCRAE            
            Correspondence Address: Maas, E.; Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Strasse 4, D-7400 Tübingen, Germany            
            Chemicals/CAS: Pyruvate Dehydrogenase Complex
Cited By :1            
            Export Date: 12 August 2021            
            CODEN: JCRAE            
            Correspondence Address: Maas, E.; Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Strasse 4, D-7400 Tübingen, Germany            
            Chemicals/CAS: Pyruvate Dehydrogenase Complex
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Maas, E
AU  - Bisswanger, H
TI  - LOCALIZATION OF THE ALPHA-OXOACID DEHYDROGENASE MULTIENZYME COMPLEXES WITHIN THE MITOCHONDRION
JF  - FEBS LETTERS
J2  - FEBS LETT
VL  - 277
PY  - 1990
SP  - 189
EP  - 190
PG  - 2
SN  - 0014-5793
DO  - 10.1016/0014-5793(90)80840-F
UR  - https://m2.mtmt.hu/api/publication/20173393
ID  - 20173393
N1  - Cited By :29            
            Export Date: 8 August 2019            
            CODEN: FEBLA            
            Correspondence Address: Bisswanger, H.; Physiologisch-chemisches Institut der Universität Tübingen, D-7400 Tübingen, Germany            
            Chemicals/CAS: Detergents; Ketoglutarate Dehydrogenase Complex, EC 1.2.4.2; Malate Dehydrogenase, EC 1.1.1.37; Multienzyme Complexes; Pyruvate Dehydrogenase Complex
Cited By :30            
            Export Date: 29 January 2021            
            CODEN: FEBLA            
            Correspondence Address: Bisswanger, H.; Physiologisch-chemisches Institut der Universität Tübingen, D-7400 Tübingen, Germany            
            Chemicals/CAS: Detergents; Ketoglutarate Dehydrogenase Complex, EC 1.2.4.2; Malate Dehydrogenase, EC 1.1.1.37; Multienzyme Complexes; Pyruvate Dehydrogenase Complex
Cited By :30            
            Export Date: 1 April 2021            
            CODEN: FEBLA            
            Correspondence Address: Bisswanger, H.; Physiologisch-chemisches Institut der Universität Tübingen, D-7400 Tübingen, Germany            
            Chemicals/CAS: Detergents; Ketoglutarate Dehydrogenase Complex, EC 1.2.4.2; Malate Dehydrogenase, EC 1.1.1.37; Multienzyme Complexes; Pyruvate Dehydrogenase Complex
Cited By :30            
            Export Date: 12 August 2021            
            CODEN: FEBLA            
            Correspondence Address: Bisswanger, H.; Physiologisch-chemisches Institut der Universität Tübingen, D-7400 Tübingen, Germany            
            Chemicals/CAS: Detergents; Ketoglutarate Dehydrogenase Complex, EC 1.2.4.2; Malate Dehydrogenase, EC 1.1.1.37; Multienzyme Complexes; Pyruvate Dehydrogenase Complex
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Sümegi, Balázs
AU  - Melegh, Béla
AU  - Adamovich, Károly
AU  - Trombitás, Károly
TI  - CYTOCHROME-OXIDASE DEFICIENCY AFFECTING THE STRUCTURE OF THE MYOFIBER AND THE SHAPE OF MITOCHONDRIAL-CRISTAE MEMBRANE
JF  - CLINICA CHIMICA ACTA
J2  - CLIN CHIM ACTA
VL  - 192
PY  - 1990
IS  - 1
SP  - 9
EP  - 18
PG  - 10
SN  - 0009-8981
DO  - 10.1016/0009-8981(90)90266-U
UR  - https://m2.mtmt.hu/api/publication/1322375
ID  - 1322375
AB  - Cytochrome oxidase deficiency was detected in the skeletal muscle of a newborn floppy child. There was a significant decrease in the quantity of subunit 5 and 6 of cytochrome oxidase as showed in Western blot with cytochrome oxidase antibody. By contrast, the NADH: cytochrome c oxidoreductase activity was normal. Electron microscopic studies revealed serious distortion in the myofibres with broken Z-bands and disorganized fibers. The relative molecular mass of actin in the myopathic muscle was smaller than in control. The diffuse actin band in Western blot suggested a proteolytic degradation of F-actin in the myopathic muscle. There was also a serious distortion in the mitochondrial structure. Cytochrome oxidase has a direct role in the formation of cristae and mutation in its components may be directly responsible for the abnormal structure.
LA  - English
DB  - MTMT
ER  -