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Wyszukujesz frazę ""Electron Transport Complex I"" wg kryterium: Temat


Tytuł :
NMS-873 functions as a dual inhibitor of mitochondrial oxidative phosphorylation.
Autorzy :
Bouwer MF; Calvin University, Department of Chemistry & Biochemistry, 1726 Knollcrest Circle SE, Grand Rapids, MI, 49546, USA.
Hamilton KE; Calvin University, Department of Chemistry & Biochemistry, 1726 Knollcrest Circle SE, Grand Rapids, MI, 49546, USA.
Jonker PB; Calvin University, Department of Chemistry & Biochemistry, 1726 Knollcrest Circle SE, Grand Rapids, MI, 49546, USA.
Kuiper SR; Calvin University, Department of Chemistry & Biochemistry, 1726 Knollcrest Circle SE, Grand Rapids, MI, 49546, USA.
Louters LL; Calvin University, Department of Chemistry & Biochemistry, 1726 Knollcrest Circle SE, Grand Rapids, MI, 49546, USA.
Looyenga BD; Calvin University, Department of Chemistry & Biochemistry, 1726 Knollcrest Circle SE, Grand Rapids, MI, 49546, USA. Electronic address: .
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Źródło :
Biochimie [Biochimie] 2021 Jun; Vol. 185, pp. 33-42. Date of Electronic Publication: 2021 Mar 13.
Typ publikacji :
Journal Article
MeSH Terms :
Acetanilides/*pharmacology
Benzothiazoles/*pharmacology
Electron Transport Complex I/*antagonists & inhibitors
Mitochondria/*metabolism
Oxidative Phosphorylation/*drug effects
Valosin Containing Protein/*antagonists & inhibitors
Allosteric Regulation/drug effects ; Cell Line ; Electron Transport Complex I/metabolism ; Humans ; Valosin Containing Protein/metabolism
Czasopismo naukowe
Tytuł :
Stimulation of cholesterol biosynthesis in mitochondrial complex I-deficiency lowers reductive stress and improves motor function and survival in mice.
Autorzy :
Schirris TJJ; Department of Pharmacology and Toxicology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Rossell S; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Center for Molecular and Biomolecular Informatics, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
de Haas R; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Department of Pediatrics, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Frambach SJCM; Department of Pharmacology and Toxicology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Hoogstraten CA; Department of Pharmacology and Toxicology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Renkema GH; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Department of Pediatrics, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Beyrath JD; Department of Pharmacology and Toxicology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Willems PHGM; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Department of Biochemistry, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Huynen MA; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Center for Molecular and Biomolecular Informatics, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Smeitink JAM; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Department of Pediatrics, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands.
Russel FGM; Department of Pharmacology and Toxicology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands. Electronic address: .
Notebaart RA; Radboud Center for Mitochondrial Medicine, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Center for Molecular and Biomolecular Informatics, Radboud University Medical Center, 6500HB Nijmegen, the Netherlands; Food Microbiology, Wageningen University & Research, 6708WG Wageningen, the Netherlands. Electronic address: .
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Źródło :
Biochimica et biophysica acta. Molecular basis of disease [Biochim Biophys Acta Mol Basis Dis] 2021 Apr 01; Vol. 1867 (4), pp. 166062. Date of Electronic Publication: 2021 Jan 13.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Biosynthetic Pathways/*drug effects
Cholesterol/*metabolism
Electron Transport Complex I/*deficiency
Fibric Acids/*therapeutic use
Mitochondrial Diseases/*metabolism
Animals ; Cholesterol/genetics ; Electron Transport Complex I/drug effects ; Electron Transport Complex I/genetics ; Electron Transport Complex I/metabolism ; Female ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mitochondrial Diseases/genetics ; Mitochondrial Diseases/physiopathology ; Motor Activity/drug effects ; NADP/metabolism ; Oxidation-Reduction/drug effects
SCR Disease Name :
Mitochondrial complex I deficiency
Czasopismo naukowe
Tytuł :
A RanBP2-type zinc finger protein functions in intron splicing in Arabidopsis mitochondria and is involved in the biogenesis of respiratory complex I.
Autorzy :
Bentolila S; Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Gipson AB; Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Kehl AJ; Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Hamm LN; Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Hayes ML; Department of Chemistry and Biochemistry, California State University Los Angeles, Los Angeles, CA 90032, USA.
Mulligan RM; Department of Developmental and Cell Biology, University of California Irvine, Irvine, CA 90032, USA.
Hanson MR; Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
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Źródło :
Nucleic acids research [Nucleic Acids Res] 2021 Apr 06; Vol. 49 (6), pp. 3490-3506.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
RNA Splicing*
Arabidopsis/*genetics
Arabidopsis Proteins/*physiology
Electron Transport Complex I/*genetics
Mitochondria/*genetics
Mitochondrial Proteins/*physiology
Arabidopsis/metabolism ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Electron Transport Complex I/metabolism ; Genes, Lethal ; Introns ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mutation ; Promoter Regions, Genetic ; RNA Splicing Factors/metabolism ; Ribosomal Proteins/genetics ; Ribosomal Proteins/metabolism ; Zinc/metabolism
Czasopismo naukowe
Tytuł :
Role of type I NADH dehydrogenase in Synechocystis sp. PCC 6803 under phycobilisome excited red light.
Autorzy :
Toyoshima M; Department of Bioinformatic Engineering, Graduate School of Information Science and Technology, Osaka University, 1-5 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Yamamoto C; Department of Bioinformatic Engineering, Graduate School of Information Science and Technology, Osaka University, 1-5 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Ueno Y; Graduate School of Science, Kobe University, Kobe, Hyogo, 657-8501, Japan.
Toya Y; Department of Bioinformatic Engineering, Graduate School of Information Science and Technology, Osaka University, 1-5 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Akimoto S; Graduate School of Science, Kobe University, Kobe, Hyogo, 657-8501, Japan.
Shimizu H; Department of Bioinformatic Engineering, Graduate School of Information Science and Technology, Osaka University, 1-5 Yamadaoka, Suita, Osaka, 565-0871, Japan. Electronic address: .
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Źródło :
Plant science : an international journal of experimental plant biology [Plant Sci] 2021 Mar; Vol. 304, pp. 110798. Date of Electronic Publication: 2020 Dec 25.
Typ publikacji :
Journal Article
MeSH Terms :
Bacterial Proteins/*physiology
Electron Transport Complex I/*physiology
Phycobilisomes/*pharmacology
Synechocystis/*enzymology
Bacterial Proteins/metabolism ; Electron Transport Complex I/metabolism ; Light ; Oxygen Consumption ; Photosystem I Protein Complex/metabolism ; Photosystem II Protein Complex/metabolism ; Synechocystis/drug effects ; Synechocystis/growth & development ; Synechocystis/radiation effects
Czasopismo naukowe
Tytuł :
Artesunate alleviates schistosomiasis-induced liver fibrosis by downregulation of mitochondrial complex Ⅰ subunit NDUFB8 and complex Ⅲ subunit UQCRC2 in hepatic stellate cells.
Autorzy :
Shen S; Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai, China; Central laboratory, Shanghai Sixth People's Hospital East Campus, Shanghai University of Medicine & Health Sciences, Shanghai, China. Electronic address: .
Luo J; Central laboratory, Shanghai Sixth People's Hospital East Campus, Shanghai University of Medicine & Health Sciences, Shanghai, China; National Demonstration Center for Experimental Fisheries Science Education, Shanghai Ocean University, Shanghai, China; Key Laboratory of Exploration and Utilization of Aquatic Genetic Resources, Ministry of Education, Shanghai Ocean University, Shanghai, China.
Ye J; Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai, China; Central laboratory, Shanghai Sixth People's Hospital East Campus, Shanghai University of Medicine & Health Sciences, Shanghai, China.
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Źródło :
Acta tropica [Acta Trop] 2021 Feb; Vol. 214, pp. 105781. Date of Electronic Publication: 2020 Nov 29.
Typ publikacji :
Journal Article
MeSH Terms :
Artesunate/*therapeutic use
Electron Transport Complex I/*metabolism
Electron Transport Complex III/*metabolism
Hepatic Stellate Cells/*drug effects
Liver Cirrhosis/*drug therapy
Liver Cirrhosis/*etiology
Animals ; Apoptosis/drug effects ; Cell Line ; Down-Regulation/drug effects ; Electron Transport Complex I/genetics ; Electron Transport Complex I/therapeutic use ; Electron Transport Complex III/genetics ; Gene Expression Regulation/drug effects ; Hepatic Stellate Cells/metabolism ; Mice ; Mitochondria/metabolism ; Schistosomiasis/pathology
Czasopismo naukowe
Tytuł :
Structural basis for a complex I mutation that blocks pathological ROS production.
Autorzy :
Yin Z; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.
Burger N; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.
Kula-Alwar D; Department of Medicine, University of Cambridge, Cambridge, UK.
Aksentijević D; William Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, London, UK.; Centre for Inflammation and Therapeutic Innovation, Queen Mary University of London, London, UK.
Bridges HR; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.
Prag HA; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.
Grba DN; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.
Viscomi C; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.; Department of Biomedical Sciences, University of Padova via Ugo Bassi 58/B, Padova, 35131, Italy.
James AM; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.
Mottahedin A; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK.; Department of Medicine, University of Cambridge, Cambridge, UK.; Department of Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Krieg T; Department of Medicine, University of Cambridge, Cambridge, UK.
Murphy MP; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK. .; Department of Medicine, University of Cambridge, Cambridge, UK. .
Hirst J; MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK. .
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Źródło :
Nature communications [Nat Commun] 2021 Jan 29; Vol. 12 (1), pp. 707. Date of Electronic Publication: 2021 Jan 29.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I/*ultrastructure
Mitochondria/*pathology
Myocardial Reperfusion Injury/*pathology
NADH Dehydrogenase/*genetics
Reactive Oxygen Species/*metabolism
Amino Acid Substitution ; Animals ; Cryoelectron Microscopy ; DNA, Mitochondrial/genetics ; Disease Models, Animal ; Disease Resistance/genetics ; Electron Transport/genetics ; Electron Transport Complex I/genetics ; Electron Transport Complex I/metabolism ; Humans ; Isolated Heart Preparation ; Leucine/genetics ; Male ; Mice ; Mice, Transgenic ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondrial Membranes/pathology ; Myocardial Reperfusion Injury/genetics ; NAD/metabolism ; NADH Dehydrogenase/metabolism ; NADH Dehydrogenase/ultrastructure ; Oxidation-Reduction ; Point Mutation ; Proline/genetics
Czasopismo naukowe
Tytuł :
Assembly of The Mitochondrial ComplexI Assembly Complex Suggests a Regulatory Role for Deflavination.
Autorzy :
Giachin G; Structural Biology Group, European Synchrotron Radiation Facility (ESRF), 71 avenue des Martyrs, 38043, Grenoble, France.
Jessop M; Institut de Biologie Structurale (IBS), CNRS, CEA, Université Grenoble Alpes, 71 avenue des Martyrs, 38044, Grenoble, France.
Bouverot R; Structural Biology Group, European Synchrotron Radiation Facility (ESRF), 71 avenue des Martyrs, 38043, Grenoble, France.
Acajjaoui S; Structural Biology Group, European Synchrotron Radiation Facility (ESRF), 71 avenue des Martyrs, 38043, Grenoble, France.
Saïdi M; Structural Biology Group, European Synchrotron Radiation Facility (ESRF), 71 avenue des Martyrs, 38043, Grenoble, France.
Chretien A; Structural Biology Group, European Synchrotron Radiation Facility (ESRF), 71 avenue des Martyrs, 38043, Grenoble, France.
Bacia-Verloop M; Institut de Biologie Structurale (IBS), CNRS, CEA, Université Grenoble Alpes, 71 avenue des Martyrs, 38044, Grenoble, France.
Signor L; Institut de Biologie Structurale (IBS), CNRS, CEA, Université Grenoble Alpes, 71 avenue des Martyrs, 38044, Grenoble, France.
Mas PJ; Integrated Structural Biology Grenoble (ISBG) CNRS, CEA, Université Grenoble Alpes, 71 avenue des Martyrs, 38042, Grenoble, France.
Favier A; Institut de Biologie Structurale (IBS), CNRS, CEA, Université Grenoble Alpes, 71 avenue des Martyrs, 38044, Grenoble, France.
Borel Meneroud E; Grenoble Institut des Neurosciences (GIN), Centre Inserm U1216, Equipe Neuropathologies et Dysfonctions Synaptiques, Université Grenoble Alpes, 31 Chemin Fortuné Ferrini, 38700, La Tronche, France.
Hons M; European Molecular Biology Laboratory (EMBL), Grenoble Outstation, 71 avenue des Martyrs, 38042, Grenoble, France.
Hart DJ; Institut de Biologie Structurale (IBS), CNRS, CEA, Université Grenoble Alpes, 71 avenue des Martyrs, 38044, Grenoble, France.
Kandiah E; Structural Biology Group, European Synchrotron Radiation Facility (ESRF), 71 avenue des Martyrs, 38043, Grenoble, France.
Boeri Erba E; Institut de Biologie Structurale (IBS), CNRS, CEA, Université Grenoble Alpes, 71 avenue des Martyrs, 38044, Grenoble, France.
Buisson A; Grenoble Institut des Neurosciences (GIN), Centre Inserm U1216, Equipe Neuropathologies et Dysfonctions Synaptiques, Université Grenoble Alpes, 31 Chemin Fortuné Ferrini, 38700, La Tronche, France.
Leonard G; Structural Biology Group, European Synchrotron Radiation Facility (ESRF), 71 avenue des Martyrs, 38043, Grenoble, France.
Gutsche I; Institut de Biologie Structurale (IBS), CNRS, CEA, Université Grenoble Alpes, 71 avenue des Martyrs, 38044, Grenoble, France.
Soler-Lopez M; Structural Biology Group, European Synchrotron Radiation Facility (ESRF), 71 avenue des Martyrs, 38043, Grenoble, France.
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Źródło :
Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2021 Feb 23; Vol. 60 (9), pp. 4689-4697. Date of Electronic Publication: 2021 Jan 12.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I/*chemistry
Flavin-Adenine Dinucleotide/*metabolism
Mitochondria/*metabolism
Acyl-CoA Dehydrogenases/genetics ; Acyl-CoA Dehydrogenases/metabolism ; Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/metabolism ; Cryoelectron Microscopy ; Electron Transport Complex I/metabolism ; Energy Metabolism ; Flavin-Adenine Dinucleotide/chemistry ; Humans ; Oxidative Phosphorylation ; Protein Interaction Domains and Motifs ; Protein Structure, Tertiary ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification
Czasopismo naukowe
Tytuł :
Combinatorial Therapeutic Effect of Inhibitors of Aldehyde Dehydrogenase and Mitochondrial Complex I, and the Chemotherapeutic Drug, Temozolomide against Glioblastoma Tumorspheres.
Autorzy :
Park HH; Department of Neurosurgery, Gangnam Severance Hospital, Yonsei University College of Medicine, Seoul 06273, Korea.
Park J; Department of Neurosurgery, Brain Tumor Center, Severance Hospital, Yonsei University College of Medicine, Seoul 03722, Korea.; Precision Medicine Research Center, College of Medicine, The Catholic University of Korea, Seoul 06591, Korea.
Cho HJ; Department of Neurosurgery, Brain Tumor Center, Severance Hospital, Yonsei University College of Medicine, Seoul 03722, Korea.
Shim JK; Department of Neurosurgery, Brain Tumor Center, Severance Hospital, Yonsei University College of Medicine, Seoul 03722, Korea.
Moon JH; Department of Neurosurgery, Brain Tumor Center, Severance Hospital, Yonsei University College of Medicine, Seoul 03722, Korea.
Kim EH; Department of Neurosurgery, Brain Tumor Center, Severance Hospital, Yonsei University College of Medicine, Seoul 03722, Korea.
Chang JH; Department of Neurosurgery, Brain Tumor Center, Severance Hospital, Yonsei University College of Medicine, Seoul 03722, Korea.
Kim SY; Division of Cancer Biology, Research Institute, National Cancer Center, Goyang 10408, Korea.
Kang SG; Department of Neurosurgery, Brain Tumor Center, Severance Hospital, Yonsei University College of Medicine, Seoul 03722, Korea.; Department of Medical Science, Yonsei University Graduate School, Seoul 03722, Korea.
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Źródło :
Molecules (Basel, Switzerland) [Molecules] 2021 Jan 08; Vol. 26 (2). Date of Electronic Publication: 2021 Jan 08.
Typ publikacji :
Journal Article
MeSH Terms :
Brain Neoplasms*/drug therapy
Brain Neoplasms*/enzymology
Glioblastoma*/drug therapy
Glioblastoma*/enzymology
Aldehyde Dehydrogenase/*antagonists & inhibitors
Antineoplastic Combined Chemotherapy Protocols/*pharmacology
Electron Transport Complex I/*antagonists & inhibitors
Neoplasm Proteins/*antagonists & inhibitors
Spheroids, Cellular/*enzymology
Aldehyde Dehydrogenase/metabolism ; Electron Transport Complex I/metabolism ; Enzyme Inhibitors/pharmacology ; Humans ; Neoplasm Proteins/metabolism ; Temozolomide/pharmacology
Czasopismo naukowe
Tytuł :
Respiratory complex I: Bottleneck at the entrance of quinone site requires conformational change for its opening.
Autorzy :
Wang P; Department of Chemistry, University of California at Davis, One Shields Avenue, Davis, CA 95616, United States of America.
Dhananjayan N; Department of Chemistry, University of California at Davis, One Shields Avenue, Davis, CA 95616, United States of America.
Hagras MA; Department of Chemistry, University of California at Davis, One Shields Avenue, Davis, CA 95616, United States of America.
Stuchebrukhov AA; Department of Chemistry, University of California at Davis, One Shields Avenue, Davis, CA 95616, United States of America. Electronic address: .
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Źródło :
Biochimica et biophysica acta. Bioenergetics [Biochim Biophys Acta Bioenerg] 2021 Jan 01; Vol. 1862 (1), pp. 148326. Date of Electronic Publication: 2020 Oct 09.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Bacterial Proteins/*chemistry
Benzoquinones/*chemistry
Electron Transport Complex I/*chemistry
Fungal Proteins/*chemistry
Thermus thermophilus/*enzymology
Yarrowia/*enzymology
Animals ; Bacterial Proteins/metabolism ; Benzoquinones/metabolism ; Electron Transport Complex I/metabolism ; Fungal Proteins/metabolism ; Humans ; Mice ; Models, Molecular ; Protein Domains ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Sheep
Czasopismo naukowe
Tytuł :
Functional Water Wires Catalyze Long-Range Proton Pumping in the Mammalian Respiratory Complex I.
Autorzy :
Röpke M; Center for Integrated Protein Science Munich at the Department of Chemistry, Technical University of Munich, Lichtenbergstrasse 4, D85748 Garching, Germany.
Saura P; Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Riepl D; Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Pöverlein MC; Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Kaila VRI; Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.; Center for Integrated Protein Science Munich at the Department of Chemistry, Technical University of Munich, Lichtenbergstrasse 4, D85748 Garching, Germany.
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Źródło :
Journal of the American Chemical Society [J Am Chem Soc] 2020 Dec 30; Vol. 142 (52), pp. 21758-21766. Date of Electronic Publication: 2020 Dec 16.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Biocatalysis*
Molecular Dynamics Simulation*
Electron Transport Complex I/*metabolism
Water/*metabolism
Electron Transport ; Electron Transport Complex I/chemistry ; Quantum Theory ; Static Electricity ; Thermodynamics
Czasopismo naukowe
Tytuł :
Metformin protects high glucose‑cultured cardiomyocytes from oxidative stress by promoting NDUFA13 expression and mitochondrial biogenesis via the AMPK signaling pathway.
Autorzy :
Liu XD; Department of Cardiology, Tongji Hospital, School of Medicine, Tongji University, Shanghai 200065, P.R. China.
Li YG; Department of Cardiology, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, P.R. China.
Wang GY; Department of Cardiology, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, P.R. China.
Bi YG; Department of Cardiology, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, P.R. China.
Zhao Y; Department of Cardiology, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, P.R. China.
Yan ML; Department of Cardiology, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, P.R. China.
Liu X; Department of Cardiology, Tongji Hospital, School of Medicine, Tongji University, Shanghai 200065, P.R. China.
Wei M; Department of Cardiology, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, P.R. China.
Wan LL; Division of Pharmacy, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200233, P.R. China.
Zhang QY; Department of Cardiology, Shanghai Ninth People's Hospital, Shanghai Jiaotong University School of Medicine, Shanghai 200011, P.R. China.
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Źródło :
Molecular medicine reports [Mol Med Rep] 2020 Dec; Vol. 22 (6), pp. 5262-5270. Date of Electronic Publication: 2020 Oct 14.
Typ publikacji :
Journal Article
MeSH Terms :
Electron Transport Complex I/*metabolism
Metformin/*pharmacology
Molecular Chaperones/*metabolism
Myocytes, Cardiac/*metabolism
AMP-Activated Protein Kinases/metabolism ; Animals ; Cell Line ; Cell Survival/drug effects ; China ; Electron Transport Complex I/drug effects ; Glucose/metabolism ; Hyperglycemia/metabolism ; Metformin/metabolism ; Mitochondria/drug effects ; Mitochondria/metabolism ; Mitochondrial Proteins/metabolism ; Molecular Chaperones/drug effects ; Myocytes, Cardiac/drug effects ; Organelle Biogenesis ; Oxidative Stress/drug effects ; Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha/metabolism ; Protein-Serine-Threonine Kinases ; Rats ; Reactive Oxygen Species/metabolism ; Signal Transduction/drug effects ; Superoxide Dismutase/metabolism ; Transcription Factors/genetics
Czasopismo naukowe
Tytuł :
Structure of inhibitor-bound mammalian complex I.
Autorzy :
Bridges HR; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Fedor JG; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Blaza JN; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.; Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.
Di Luca A; Center for Integrated Protein Science Munich (CIPSM) at Department of Chemistry, Technische Universität München, 85748, Garching, Germany.; Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, 106 91, Stockholm, Sweden.
Jussupow A; Center for Integrated Protein Science Munich (CIPSM) at Department of Chemistry, Technische Universität München, 85748, Garching, Germany.
Jarman OD; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Wright JJ; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus, London, W12 0BZ, UK.
Agip AA; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK.
Gamiz-Hernandez AP; Center for Integrated Protein Science Munich (CIPSM) at Department of Chemistry, Technische Universität München, 85748, Garching, Germany.; Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, 106 91, Stockholm, Sweden.
Roessler MM; Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, White City Campus, London, W12 0BZ, UK.
Kaila VRI; Center for Integrated Protein Science Munich (CIPSM) at Department of Chemistry, Technische Universität München, 85748, Garching, Germany. .; Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, 106 91, Stockholm, Sweden. .
Hirst J; The Medical Research Council Mitochondrial Biology Unit, University of Cambridge, The Keith Peters Building, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY, UK. .
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Źródło :
Nature communications [Nat Commun] 2020 Oct 16; Vol. 11 (1), pp. 5261. Date of Electronic Publication: 2020 Oct 16.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I/*chemistry
Electron Transport Complex I/*metabolism
Enzyme Inhibitors/*metabolism
Mammals/*metabolism
Animals ; Binding Sites ; Cryoelectron Microscopy ; Electron Transport Complex I/antagonists & inhibitors ; Electron Transport Complex I/genetics ; Enzyme Inhibitors/chemistry ; Female ; Mammals/genetics ; Mice ; Mice, Inbred C57BL ; Mitochondria, Heart/genetics ; Mitochondria, Heart/metabolism ; Molecular Dynamics Simulation ; Oxidative Phosphorylation ; Pyridines/chemistry ; Pyridines/metabolism
Czasopismo naukowe
Tytuł :
Essential role of accessory subunit LYRM6 in the mechanism of mitochondrial complex I.
Autorzy :
Galemou Yoga E; Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.; Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Parey K; Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.; Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.; Department of Structural Biology, Max Planck Institute of Biophysics, Max von Laue Str. 3, 60438, Frankfurt am Main, Germany.; Department of Structural Biology, University of Osnabrück, Barbarastraße 13, 49076, Osnabrück, Germany.
Djurabekova A; Department of Physics, P.O. Box 64, University of Helsinki, FI-00014, Helsinki, Finland.
Haapanen O; Department of Physics, P.O. Box 64, University of Helsinki, FI-00014, Helsinki, Finland.
Siegmund K; Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.; Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Zwicker K; Medical School, Institute of Biochemistry I, Goethe University, Theodor-Stern-Kai 7, 60590, Frankfurt am Main, Germany.
Sharma V; Department of Physics, P.O. Box 64, University of Helsinki, FI-00014, Helsinki, Finland. .; HiLIFE Institute of Biotechnology, P.O. Box 56, University of Helsinki, FI-00014, Helsinki, Finland. .
Zickermann V; Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.; Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Angerer H; Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany. .; Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany. .
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Źródło :
Nature communications [Nat Commun] 2020 Nov 26; Vol. 11 (1), pp. 6008. Date of Electronic Publication: 2020 Nov 26.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I/*metabolism
Fungal Proteins/*metabolism
Protein Subunits/*metabolism
Electron Transport Complex I/genetics ; Electron Transport Complex I/ultrastructure ; Fungal Proteins/genetics ; Fungal Proteins/ultrastructure ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Protein Subunits/genetics ; Protons ; Ubiquinone/metabolism ; Yarrowia/genetics ; Yarrowia/metabolism
Czasopismo naukowe
Tytuł :
Uniparental isodisomy as a cause of mitochondrial complex I respiratory chain disorder due to a novel splicing NDUFS4 mutation.
Autorzy :
González-Quintana A; Mitochondrial Diseases Laboratory, Hospital Universitario '12 de Octubre', Madrid, Spain; Center for Biomedical Network Research on Rare Diseases (CIBERER), Madrid, Spain.
Trujillo-Tiebas MJ; Center for Biomedical Network Research on Rare Diseases (CIBERER), Madrid, Spain; Department of Genetics, IIS-Fundación Jiménez Díaz University Hospital (IIS-FJD, UAM), Madrid, Spain.
Fernández-Perrone AL; Pediatric Neurology Department, Hospital Quirónsalud, Madrid, Spain.
Blázquez A; Mitochondrial Diseases Laboratory, Hospital Universitario '12 de Octubre', Madrid, Spain; Center for Biomedical Network Research on Rare Diseases (CIBERER), Madrid, Spain; Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), Madrid, Spain.
Lucia A; Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), Madrid, Spain; Faculty of Sport Sciences, Universidad Europea de Madrid, Madrid, Spain; Center for Biomedical Research Network on Frailty and Healthy Aging (CIBERFES), Madrid, Spain.
Morán M; Mitochondrial Diseases Laboratory, Hospital Universitario '12 de Octubre', Madrid, Spain; Center for Biomedical Network Research on Rare Diseases (CIBERER), Madrid, Spain; Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), Madrid, Spain.
Ugalde C; Mitochondrial Diseases Laboratory, Hospital Universitario '12 de Octubre', Madrid, Spain; Center for Biomedical Network Research on Rare Diseases (CIBERER), Madrid, Spain; Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), Madrid, Spain.
Arenas J; Mitochondrial Diseases Laboratory, Hospital Universitario '12 de Octubre', Madrid, Spain; Center for Biomedical Network Research on Rare Diseases (CIBERER), Madrid, Spain; Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), Madrid, Spain.
Ayuso C; Center for Biomedical Network Research on Rare Diseases (CIBERER), Madrid, Spain; Department of Genetics, IIS-Fundación Jiménez Díaz University Hospital (IIS-FJD, UAM), Madrid, Spain.
Martín MA; Mitochondrial Diseases Laboratory, Hospital Universitario '12 de Octubre', Madrid, Spain; Center for Biomedical Network Research on Rare Diseases (CIBERER), Madrid, Spain; Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), Madrid, Spain. Electronic address: .
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Źródło :
Molecular genetics and metabolism [Mol Genet Metab] 2020 Nov; Vol. 131 (3), pp. 341-348. Date of Electronic Publication: 2020 Oct 16.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I/*deficiency
Electron Transport Complex I/*genetics
Mitochondrial Diseases/*genetics
Uniparental Disomy/*genetics
Electron Transport Complex I/metabolism ; Female ; Genetic Predisposition to Disease ; Homozygote ; Humans ; Infant ; Mitochondrial Diseases/metabolism ; Mitochondrial Diseases/pathology ; Mutation/genetics ; RNA Splicing/genetics ; Uniparental Disomy/pathology
SCR Disease Name :
Mitochondrial complex I deficiency
Czasopismo naukowe
Tytuł :
Inhibition of mitochondria NADH-Ubiquinone oxidoreductase (complex I) sensitizes the radioresistant glioma U87MG cells to radiation.
Autorzy :
Gao X; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Yang Y; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China; Department of Radiotherapy, the Second Affiliated Hospital, Dalian Medical University, Dalian 116044, China.
Wang J; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Zhang L; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Sun C; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Wang Y; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Zhang J; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Dong H; Eight-year Clinical Medicine Education Program, Dalian Medical University, Dalian 116044, China.
Zhang H; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Gao C; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Zhang B; Department of Radiotherapy, the First Affiliated Hospital, Dalian Medical University, Dalian 116044, China.
Feng B; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China.
Mao W; College of Basic Medical Sciences, Dalian Medical University, Dalian 116044, China. Electronic address: .
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Źródło :
Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie [Biomed Pharmacother] 2020 Sep; Vol. 129, pp. 110460. Date of Electronic Publication: 2020 Jul 01.
Typ publikacji :
Journal Article
MeSH Terms :
Brain Neoplasms/*radiotherapy
Electron Transport Complex I/*antagonists & inhibitors
Enzyme Inhibitors/*pharmacology
Glioma/*radiotherapy
Metformin/*pharmacology
Mitochondria/*drug effects
Radiation Tolerance/*drug effects
Radiation-Sensitizing Agents/*pharmacology
Rotenone/*pharmacology
Brain Neoplasms/enzymology ; Brain Neoplasms/genetics ; Brain Neoplasms/pathology ; Cell Line, Tumor ; Electron Transport Complex I/genetics ; Electron Transport Complex I/metabolism ; Glioma/enzymology ; Glioma/genetics ; Glioma/pathology ; Humans ; Mitochondria/enzymology ; Mitochondria/genetics ; Mitochondria/pathology
Czasopismo naukowe
Tytuł :
Leigh Syndrome Due to NDUFV1 Mutations Initially Presenting as LBSL.
Autorzy :
Borna NN; Diagnostics and Therapeutics of Intractable Diseases, Intractable Disease Research Center, Graduate School of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113-8421, Japan.
Kishita Y; Diagnostics and Therapeutics of Intractable Diseases, Intractable Disease Research Center, Graduate School of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113-8421, Japan.
Sakai N; Child Healthcare and Genetic Science Laboratory, Division of Health Sciences, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
Hamada Y; Department of Pediatrics, Toyonaka Municipal Hospital, Toyonaka, Osaka 560-8565, Japan.
Kamagata K; Department of Radiology, Graduate School of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113-8421, Japan.
Kohda M; Diagnostics and Therapeutics of Intractable Diseases, Intractable Disease Research Center, Graduate School of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113-8421, Japan.
Ohtake A; Department of Pediatrics & Clinical Genomics, Faculty of Medicine, Saitama Medical University, Moroyama, Saitama 350-0495, Japan.; Center for Intractable Diseases, Saitama Medical University Hospital, Moroyama, Saitama 350-0495, Japan.
Murayama K; Department of Metabolism, Chiba Children's Hospital, Midori-ku, Chiba 266-0007, Japan.
Okazaki Y; Diagnostics and Therapeutics of Intractable Diseases, Intractable Disease Research Center, Graduate School of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113-8421, Japan.; Laboratory for Comprehensive Genomic Analysis, RIKEN Center for Integrative Medical Sciences, Yokohama, Kanagawa 230-0045, Japan.
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Źródło :
Genes [Genes (Basel)] 2020 Nov 09; Vol. 11 (11). Date of Electronic Publication: 2020 Nov 09.
Typ publikacji :
Case Reports; Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I/*genetics
Leigh Disease/*diagnosis
Leigh Disease/*genetics
Adolescent ; Aspartate-tRNA Ligase/deficiency ; Aspartate-tRNA Ligase/genetics ; Brain/diagnostic imaging ; Brain Stem/pathology ; Child, Preschool ; Electron Transport Complex I/metabolism ; Female ; Humans ; Leigh Disease/pathology ; Leukoencephalopathies/diagnosis ; Leukoencephalopathies/genetics ; Leukoencephalopathies/pathology ; Magnetic Resonance Imaging/methods ; Mitochondrial Diseases/diagnosis ; Mitochondrial Diseases/genetics ; Mitochondrial Diseases/pathology ; Mutation ; Phenotype
SCR Disease Name :
Leukoencephalopathy with Brainstem and Spinal Cord Involvement and Lactate Elevation
Czasopismo naukowe
Tytuł :
Induced pluripotent stem cell line UOMi002-A from a patient with Leigh syndrome with compound heterozygous mutations in the NDUFV1 gene.
Autorzy :
Sequiera GL; Institute of Cardiovascular Sciences, St. Boniface Hospital Albrechtsen Research Centre, Regenerative Medicine Program, Department of Physiology and Pathophysiology, Max Rady College of Medicine, Rady Faculty of Health Sciences, University of Manitoba, Canada.
Rockman-Greenberg C; Department of Pediatrics and Child Health, Max Rady College of Medicine, Rady Faculty of Health Sciences, University of Manitoba, Canada.
Dhingra S; Institute of Cardiovascular Sciences, St. Boniface Hospital Albrechtsen Research Centre, Regenerative Medicine Program, Department of Physiology and Pathophysiology, Max Rady College of Medicine, Rady Faculty of Health Sciences, University of Manitoba, Canada. Electronic address: .
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Źródło :
Stem cell research [Stem Cell Res] 2020 Oct; Vol. 48, pp. 101964. Date of Electronic Publication: 2020 Aug 27.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I*
Induced Pluripotent Stem Cells*
Leigh Disease*/genetics
Child ; Child, Preschool ; DNA, Mitochondrial/genetics ; Female ; Humans ; Mitochondria ; Mutation
Czasopismo naukowe
Tytuł :
Production of superoxide and hydrogen peroxide in the mitochondrial matrix is dominated by site I Q of complex I in diverse cell lines.
Autorzy :
Fang J; Buck Institute for Research on Aging, 8001 Redwood Blvd, Novato, CA, 94945, USA. Electronic address: .
Wong HS; Buck Institute for Research on Aging, 8001 Redwood Blvd, Novato, CA, 94945, USA. Electronic address: .
Brand MD; Buck Institute for Research on Aging, 8001 Redwood Blvd, Novato, CA, 94945, USA. Electronic address: .
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Źródło :
Redox biology [Redox Biol] 2020 Oct; Vol. 37, pp. 101722. Date of Electronic Publication: 2020 Sep 14.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I*/metabolism
Superoxides*/metabolism
Animals ; Cell Line ; Humans ; Hydrogen Peroxide/metabolism ; Mice ; Mitochondria/metabolism ; Rats
Czasopismo naukowe
Tytuł :
Progressive optic atrophy in a retinal ganglion cell-specific mouse model of complex I deficiency.
Autorzy :
Wang L; Department of Ophthalmology, Box 3712 Med Center, Duke University, 2351 Erwin Road, Durham, NC, 27710, USA.
Klingeborn M; Department of Ophthalmology, Box 3712 Med Center, Duke University, 2351 Erwin Road, Durham, NC, 27710, USA.
Travis AM; Department of Ophthalmology and Visual Sciences, University of Michigan, Ann Arbor, MI, 48105, USA.
Hao Y; Department of Ophthalmology, Box 3712 Med Center, Duke University, 2351 Erwin Road, Durham, NC, 27710, USA.
Arshavsky VY; Department of Ophthalmology, Box 3712 Med Center, Duke University, 2351 Erwin Road, Durham, NC, 27710, USA.; Department of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, 27710, USA.
Gospe SM 3rd; Department of Ophthalmology, Box 3712 Med Center, Duke University, 2351 Erwin Road, Durham, NC, 27710, USA. .
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Źródło :
Scientific reports [Sci Rep] 2020 Oct 01; Vol. 10 (1), pp. 16326. Date of Electronic Publication: 2020 Oct 01.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Electron Transport Complex I/*deficiency
Mitochondrial Diseases/*pathology
Optic Nerve Diseases/*pathology
Retinal Ganglion Cells/*pathology
Animals ; Disease Models, Animal ; Electron Transport Complex I/metabolism ; Female ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mitochondrial Diseases/complications ; Optic Nerve Diseases/etiology ; Vesicular Glutamate Transport Protein 2/metabolism
SCR Disease Name :
Mitochondrial complex I deficiency
Czasopismo naukowe
Tytuł :
Key role of quinone in the mechanism of respiratory complex I.
Autorzy :
Gutiérrez-Fernández J; Institute of Science and Technology Austria, Am Campus 1, A-3400, Klosterneuburg, Austria.
Kaszuba K; Institute of Science and Technology Austria, Am Campus 1, A-3400, Klosterneuburg, Austria.
Minhas GS; Medical Research Council Mitochondrial Biology Unit, Keith Peters Building, Hills rd, Cambridge, CB2 0XY, UK.; Sosei Heptares, Steinmetz Building, Granta Park, Cambridge, CB21 6DG, UK.
Baradaran R; Medical Research Council Mitochondrial Biology Unit, Keith Peters Building, Hills rd, Cambridge, CB2 0XY, UK.; Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, 17165, Solna, Sweden.
Tambalo M; Institute of Science and Technology Austria, Am Campus 1, A-3400, Klosterneuburg, Austria.
Gallagher DT; Medical Research Council Mitochondrial Biology Unit, Keith Peters Building, Hills rd, Cambridge, CB2 0XY, UK.
Sazanov LA; Institute of Science and Technology Austria, Am Campus 1, A-3400, Klosterneuburg, Austria. .
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Źródło :
Nature communications [Nat Commun] 2020 Aug 18; Vol. 11 (1), pp. 4135. Date of Electronic Publication: 2020 Aug 18.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Molecular Dynamics Simulation*
Electron Transport Complex I/*chemistry
Quinones/*chemistry
Thermus thermophilus/*enzymology
Allosteric Regulation ; Bacterial Proteins/chemistry ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Electron Transport/genetics ; Electron Transport Complex I/genetics ; Electron Transport Complex I/metabolism ; Electron Transport Complex I/ultrastructure ; Models, Molecular ; NAD/chemistry ; NAD/metabolism ; Neural Networks, Computer ; Protein Conformation ; Protons ; Quinones/metabolism ; Thermus thermophilus/genetics
Czasopismo naukowe

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