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1كتاب إلكتروني
المؤلفون: Feiler, UteAff10, Hauska, GünterAff11
المساهمون: Govindjee, editorAff1, Amesz, Jan, editorAff2, Barber, James, editorAff3, Blankenship, Robert E., editorAff4, Aff7, Murata, Norio, editorAff5, Ort, Donald R., editorAff6, Madigan, Michael T., editorAff8, Bauer, Carl E., editorAff9
المصدر: Anoxygenic Photosynthetic Bacteria. 2:665-685
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المؤلفون: Wei Song, Judy Hirst, Maxie M. Roessler, Mikhail A. Hameedi, Daniel N. Grba, Katherine H. Richardson, John J. Wright, Andrew J. Y. Jones
المصدر: The Journal of Biological Chemistry
مصطلحات موضوعية: cryo‐electron microscopy, 0301 basic medicine, Iron-Sulfur Proteins, Yarrowia lipolytica, Biochemistry & Molecular Biology, Arginine, EPR, electron paramagnetic resonance, Stereochemistry, Protein subunit, Iron–sulfur cluster, Yarrowia, cryo-electron microscopy, Oxidative phosphorylation, DSF, differential scanning fluorimetry, Biochemistry, Cofactor, NDH2, type II NADH:ubiquinone oxidoreductase, Fungal Proteins, Mitochondrial Proteins, 03 medical and health sciences, chemistry.chemical_compound, NADH:ubiquinone oxidoreductase, ROS, reactive oxygen species, Oxidoreductase, Molecular Biology, 11 Medical and Health Sciences, chemistry.chemical_classification, Electron Transport Complex I, dimethyl-arginine, 030102 biochemistry & molecular biology, biology, ATP synthase, Protein Stability, complex I, NDUFS2, BN-PAGE, blue native polyacrylamide gel electrophoresis, iron–sulfur cluster, Cell Biology, 06 Biological Sciences, electron paramagnetic resonance (EPR), 030104 developmental biology, chemistry, complex I, NADH:ubiquinone oxidoreductase, cryo-EM, electron cryomicroscopy, biology.protein, iron‐sulfur cluster, 03 Chemical Sciences, Research Article, FeS, iron–sulfur
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75611df039fac8bfd38c2d255fa14341
https://pubmed.ncbi.nlm.nih.gov/33640456 -
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المصدر: Redox Biology
Redox Biology, Vol 20, Iss, Pp 130-145 (2019)مصطلحات موضوعية: Antioxidant, medicine.medical_treatment, MetE, methionine synthase, Review Article, Mal, malate, protein-SSB, BSH protein mixed disulfide, DHAP, dihydroxyacetone phosphate, Biochemistry, LMW, low molecular weight, 0302 clinical medicine, Met, methionine, GSH, glutathione, GlxA/B, glyoxalases A and B, lcsh:QH301-705.5, HTA, hemithioacetal, roGFP2, redox-sensitive green fluorescent protein, RSS, reactive sulfur species, GlcN, glucoseamine, pKa, negative base-10 logarithm of the acid dissociation constant, GapDH, glycolytic glyceraldehyde 3-phosphate dehydrogenase, MSH, mycothiol, OHP, organic hydroperoxide, MRSA, methicillin-resistant Staphylococcus aureus, OhrR, organic hydroperoxide repressor, GuaB, inosine-5-monophosphate dehydrogenases, FeS, iron-sulfur, Protein S-thiolation, Gram-positive bacteria, 3. Good health, Grx, glutaredoxin, FA, formaldehyde, Mca, mycothiol-S-conjugate amidase, lcsh:Medicine (General), MSONH2, MSH sulfinamide, CoASSH, CoASH persulfide, MgsA, methylglyoxal synthase, 03 medical and health sciences, Structure-Activity Relationship, NADH, nicotinamide adenine dinucleotide, CHP, cumene hydroperoxide, HED, hydroxyethyl disulfide, Humans, INH, isoniazid, LC-MS/MS, liquid chromatography tandem mass spectrometry, Pathogenic bacteria, CA-MRSA, community acquired MRSA, MT, metallothionein, EGT, ergothioneine, Gst, GSH-S-transferases, MsrA/B, methionine sulfoxide reductase A/B, 030104 developmental biology, chemistry, DTT, dithiothreitol, MG, methylglyoxal, MST, mycothiol-S-transferase, 030217 neurology & neurosurgery, 0301 basic medicine, Cys, cysteine, Clinical Biochemistry, Mrx1, mycoredoxin1, Bacillithiol, medicine.disease_cause, Bca, BSH S-conjugate amidase, Corynebacterium glutamicum, chemistry.chemical_compound, Trx, thioredoxin, MetSO, methionine sulfoxide, PpaC, inorganic pyrophosphatase, lcsh:R5-920, Glucosamine, biology, Mycobacterium smegmatis, Glycopeptides, SarZ, redox-sensing virulence regulator, AcCys, acetyl cysteine, Brx, bacilliredoxin, H2O2, hydrogen peroxide, GlcNAc, N-acetyl glucoseamine, BSSB, oxidized bacillithiol disulfide, NFC, nitrofuranylcalanolide, Oxidation-Reduction, Bst, BSH-S-transferases, TrxR, thioredoxin reductase, Mtb, Mycobacterium tuberculosis, PPP, pentose phosphate pathway, Mycothiol, Models, Biological, GSSG, oxidized glutathione disulfide, RNS, reactive nitrogen species, ROS, reactive oxygen species, AhpE, membrane-associated peroxidase, BshB, deacetylase producing GlcN-Mal, PDB, Protein Data Bank, YpdA, NADPH-dependent flavin oxidoreductase, medicine, Ins, myoinositol, CoASH, coenzymeA, Animals, BshC, cysteine ligase for BSH biosynthesis, MSNO, S-nitrosomycothiol, Cysteine, Sulfhydryl Compounds, Ac, acetyl, BshA, glycosyltransferase for GlcNAc-Mal biosynthesis, HOCl, sodium hypochlorite, Organic Chemistry, NADPH, nicotinamide adenine dinucleotide phosphate, STRING, Search Tool for the Retrieval of Interacting Genes/Proteins, biology.organism_classification, AldA, aldehyde dehydrogenase A, BSH, bacillithiol, lcsh:Biology (General), Protein Processing, Post-Translational, Bacteria, RES, reactive electrophilic species, Inositol
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المؤلفون: Judy Hirst, Maxie M. Roessler
المصدر: Biochimica et Biophysica Acta
مصطلحات موضوعية: 0301 basic medicine, Ubiquinol, Semiquinone, EPR, electron paramagnetic resonance, Iron–sulfur cluster, Protein Conformation, Ubiquinone, Biophysics, Flavin mononucleotide, Molecular Dynamics Simulation, Photochemistry, 7. Clean energy, Redox, Biochemistry, Article, Catalysis, Electron Transport, 03 medical and health sciences, chemistry.chemical_compound, Electron transfer, NADH:ubiquinone oxidoreductase, HYSCORE, hyperfine sub-level correlation, Binding Sites, Electron Transport Complex I, 030102 biochemistry & molecular biology, SQ, semiquinone, CW, continuous wave, Superoxide, SMP, submitochondrial particle, Cell Biology, Proton-coupled electron transfer, NAD, Electron transport chain, 3. Good health, Enzyme Activation, 030104 developmental biology, chemistry, Energy Transfer, Models, Chemical, Electron paramagnetic resonance, Reactive Oxygen Species, Oxidation-Reduction, ESEEM, electron spin echo envelope modulation, FeS, iron–sulfur, Protein Binding
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4c1817bb7a1356b08b5de2a1060ef84
http://europepmc.org/articles/PMC4893023 -
5كتاب
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6دورية أكاديمية
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