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Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 12754 - 12763
The biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is a multistage, multicompartment process that is essential for a broad range of cellular... 
4FE-4S CLUSTERS | acyl carrier protein (ACP) | cysteine desulfurase | fatty acid metabolism | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOTHIOL GLUTAREDOXINS FUNCTION | FUNCTIONAL-CHARACTERIZATION | glutaredoxin | mitochondrial disease | frataxin | ACYL CARRIER PROTEIN | ferredoxin | metal biology | chaperone | INTERACTING PROTEIN | ASSEMBLY MACHINERY | AZOTOBACTER-VINELANDII (NIF)ISCA | FE-S PROTEINS | SCAFFOLD PROTEIN | lipoic acid | Mitochondria - enzymology | Adrenodoxin - genetics | Species Specificity | Humans | Protein Multimerization | Adrenodoxin - metabolism | Iron-Sulfur Proteins - genetics | Iron-Binding Proteins - chemistry | Mitochondrial Proteins - genetics | Iron-Sulfur Proteins - chemistry | Iron-Binding Proteins - metabolism | Mitochondrial Proteins - metabolism | Apoenzymes - metabolism | Sulfurtransferases - chemistry | Acyl Carrier Protein - metabolism | Models, Molecular | Sulfurtransferases - genetics | Mitochondria - metabolism | Saccharomyces cerevisiae Proteins - genetics | Protein Folding | Protein Transport | Gene Expression Regulation, Enzymologic | Acyl Carrier Protein - chemistry | Animals | Models, Biological | Acyl Carrier Protein - genetics | Apoenzymes - genetics | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Apoenzymes - chemistry | Adrenodoxin - chemistry | Iron-Binding Proteins - genetics | Protein Conformation | Iron-Sulfur Proteins - metabolism | Sulfurtransferases - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Minireviews
Journal Article
Biochemical Journal, ISSN 0264-6021, 01/2012, Volume 441, Issue 2, pp. 523 - 540
Reactive oxygen and nitrogen species change cellular responses through diverse mechanisms that are now being defined. At low levels, they are signalling... 
Mitochondrion | Oxidative stress | Redox signalling | Neurodegeneration | Autophagy | Nitrative stress | autophagy | CHAPERONE-MEDIATED AUTOPHAGY | ANTIOXIDANT RESPONSIVE ELEMENTS | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIPOFUSCINOSES BATTEN-DISEASE | neurodegeneration | AMYOTROPHIC-LATERAL-SCLEROSIS | mitochondrion | redox signalling | MOTOR-NEURON DEGENERATION | MANGANESE SUPEROXIDE-DISMUTASE | nitrative stress | SMOOTH-MUSCLE-CELLS | PATHOGENIC DJ-1 MUTATIONS | HYPOXIA-INDUCED AUTOPHAGY | oxidative stress | COMPLEX-I DEFICIENCY | Protein Kinases - metabolism | Transcription, Genetic - drug effects | Cardiovascular Diseases - physiopathology | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Reactive Nitrogen Species - metabolism | Humans | Oxidative Stress - physiology | Hydrogen Peroxide - pharmacology | Oncogene Proteins - metabolism | Nitric Oxide - physiology | Autophagy - physiology | Intracellular Signaling Peptides and Proteins - metabolism | Mitochondria - metabolism | Mitochondria - pathology | Parkinson Disease - physiopathology | Lysosomes - physiology | Protein Deglycase DJ-1 | Animals | Signal Transduction - physiology | TOR Serine-Threonine Kinases - physiology | Neoplasms - physiopathology | AMPK, 5′-AMP-activated protein kinase | NBR1, neighbour of BRCA1 (breast cancer early-onset 1) | NGF, nerve growth factor | LC3, light chain 3 | NOX, NADPH oxidase | EM, electron microscopy | TOR, target of rapamycin | ULK, unc (unco-ordinated family member)-51-like kinase | mtDNA, mitochondrial DNA | mTOR, mammalian target of rapamycin | IKKβ, IκB kinase β | LRRK2, leucine-rich repeat kinase 2 | NAC, N-acetyl-L-cysteine | Nrf2, nuclear factor-erythroid 2-related factor 2 | PI3P, phosphatidylinositol 3-phosphate | ECH, enoyl-CoA hydratase | BNIP3L, BNIP3-like | Drp1, dynamin-related protein 1 | tfLC3, tandem fluorescently tagged LC3 | NF-κB, nuclear factor κB | BAG, Bcl-2-associated athanogene | Keap1, Kelch-like ECH-associated protein 1 | PE, phosphatidylethanolamine | 3-MA, 3-methyladenine | UCP, uncoupling protein | IκB, inhibitor of nuclear factor κB | FIP200, focal adhesion kinase family-interacting protein of 200 kDa | PI3K, phosphoinositide 3-kinase | HNE, 4-hydroxynonenal | Review | ALS, amyotrophic lateral sclerosis | ATG, AuTophaGy-related | adenovirus E18 19-kDa-interacting protein | Tzb, trastuzumab | mETC, mitochondrial electron-transport chain | Rubicon, RUN domain- and cysteine-rich domain-containing beclin-1-interacting protein | VDAC, voltage-dependent anion channel | IP3, inositol 1,4,5-trisphosphate | RFP, red fluorescent protein | ROS, reactive oxygen species | TNFα, tumour necrosis factor α | PINK1, PTEN (phosphatase and tensin homologue deleted on chromosome 10)-induced kinase 1 | GFP, green fluorescent protein | LAMP, lysosome-associated membrane protein | JNK1, c-Jun N-terminal kinase 1 | TAC, transverse aortic constriction | GABARAP, GABAA (γ-aminobutyric acid type A)-receptor-associated protein | HIF-1, hypoxia-inducible factor 1 | NOS, nitric oxide synthase | siRNA, small interfering RNA | SOD, superoxide dismutase | RLS, reactive lipid species | RNS, reactive nitrogen species | ER, endoplasmic reticulum | TIGAR, TP53 (tumour protein 53)-induced glycolysis and apoptosis regulator | Vps34, vacuolar protein sorting 34 | BNIP, Bcl-2
Journal Article
EMBO reports, ISSN 1469-221X, 01/2010, Volume 11, Issue 1, pp. 45 - 51
Autophagy is the cellular homeostatic pathway that delivers large cytosolic materials for degradation in the lysosome. Recent evidence indicates that autophagy... 
mitophagy | Nix | LC3 | GABARAP | selective autophagy | Selective autophagy | Mitophagy | APOPTOSIS | PROTEIN | RETICULOCYTE MATURATION | UBIQUITIN | BNIP3 | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-DEATH | CELL BIOLOGY | STRUCTURAL BASIS | DEGRADATION | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cercopithecus aethiops | Molecular Sequence Data | Substrate Specificity | Autophagy - physiology | Mitochondrial Proteins - genetics | Proto-Oncogene Proteins - chemistry | Mitochondrial Proteins - metabolism | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Membrane Proteins - metabolism | Binding Sites | Proto-Oncogene Proteins - metabolism | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cells, Cultured | Ubiquitin-Protein Ligases - metabolism | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Saccharomyces cerevisiae Proteins - genetics | Blotting, Western | Amino Acid Motifs | Autophagy-Related Protein 8 Family | Animals | Membrane Proteins - chemistry | Reticulocytes - cytology | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Mice | Receptors, GABA-A - metabolism | COS Cells | Proteins | Mitochondria | Cellular biology | Cytoplasm | Scientific Report
Journal Article
The FEBS Journal, ISSN 1742-464X, 02/2018, Volume 285, Issue 3, pp. 416 - 431
Bax and Bak are members of the Bcl‐2 family and core regulators of the intrinsic pathway of apoptosis. Upon apoptotic stimuli, they are activated and... 
BCL‐2 family | mitochondria | apoptosis | BAX | mitochondrial outer membrane permeabilization | BAK | DRP1 | BCL-2 family | OUTER-MEMBRANE | PROAPOPTOTIC BAX | BIOCHEMISTRY & MOLECULAR BIOLOGY | PORE FORMATION | BH3 DOMAINS | CELL-DEATH | PROSURVIVAL BCL-2 PROTEINS | CYTOCHROME-C | CONFORMATIONAL-CHANGES | BH3-ONLY PROTEINS | MEMBRANE PERMEABILIZATION | Mitochondrial Dynamics | Mitochondria - enzymology | bcl-2-Associated X Protein - chemistry | Proto-Oncogene Proteins c-bcl-2 - agonists | Humans | Protein Multimerization | bcl-2-Associated X Protein - agonists | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Mitochondrial Membranes - chemistry | Proto-Oncogene Proteins c-bcl-2 - chemistry | Mitochondrial Membranes - enzymology | Protein Interaction Domains and Motifs | Mitochondria - chemistry | Dimerization | Apoptosis Regulatory Proteins - chemistry | bcl-2-Associated X Protein - metabolism | Mitochondria - metabolism | Lipid Mobilization | Apoptosis Regulatory Proteins - metabolism | Mitochondrial Membranes - metabolism | Animals | Models, Biological | Apoptosis Regulatory Proteins - agonists | Protein Conformation | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Porosity | bcl-2 Homologous Antagonist-Killer Protein - chemistry | Apoptosis | bcl-2 Homologous Antagonist-Killer Protein - agonists | Mitochondria | Regulators | Oligomerization | Bax protein | Bcl-2 protein | Spatial discrimination | Organelles
Journal Article
Science, ISSN 0036-8075, 12/2010, Volume 330, Issue 6009, pp. 1390 - 1393
Although the proteins BAX and BAK are required for initiation of apoptosis at the mitochondria, how BAX and BAK are activated remains unsettled. We provide in... 
T lymphocytes | Mitochondria | Cytokines | Thymocytes | Neurons | Cell death | REPORTS | Cytochromes | Mice | Potassium | Apoptosis | NEURONAL APOPTOSIS | CYTOCHROME-C | MITOCHONDRIAL APOPTOSIS | MECHANISM | MULTIDISCIPLINARY SCIENCES | BH3 DOMAINS | RELEASE | JNK PATHWAY | PROTEINS | BCL-2 FAMILY-MEMBERS | MEMBRANE PERMEABILIZATION | BH3 Interacting Domain Death Agonist Protein - deficiency | T-Lymphocytes - physiology | bcl-2-Associated X Protein - chemistry | Protein Multimerization | Stress, Physiological | bcl-2 Homologous Antagonist-Killer Protein - genetics | BH3 Interacting Domain Death Agonist Protein - genetics | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Membrane Proteins - deficiency | Caspases - metabolism | Bcl-2-Like Protein 11 | Apoptosis Regulatory Proteins - deficiency | Tumor Suppressor Proteins - deficiency | Tumor Suppressor Proteins - genetics | Neurons - physiology | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | bcl-2-Associated X Protein - genetics | Proto-Oncogene Proteins - metabolism | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Cytochromes c - metabolism | Cells, Cultured | bcl-2-Associated X Protein - metabolism | Proto-Oncogene Proteins - genetics | Mitochondria - metabolism | Permeability | Proto-Oncogene Proteins - deficiency | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Animals | Models, Biological | Cerebellum - cytology | Intracellular Membranes - metabolism | bcl-2 Homologous Antagonist-Killer Protein - chemistry | Protein research | Genetic aspects | Mitochondrial DNA | Biochemical genetics | Research | Properties | Methods
Journal Article
Journal Article
EMBO reports, ISSN 1469-221X, 06/2017, Volume 18, Issue 6, pp. 947 - 961
Journal Article
Science, ISSN 0036-8075, 2/2007, Volume 315, Issue 5813, pp. 856 - 859
A central issue in the regulation of apoptosis by the Bcl-2 family is whether its BH3-only members initiate apoptosis by directly binding to the essential... 
Research fellowships | Protein isoforms | Medical research | Myeloid cells | Antibodies | Cytochromes | Ligands | Reports | Grants | Viability | Apoptosis | RESPONSES | FAMILY-MEMBERS | X-L | MULTIDISCIPLINARY SCIENCES | BIM | HELIX | MITOCHONDRIAL-MEMBRANE | PUMA | DOMAINS | BH3-ONLY PROTEINS | CELL-DEATH | bcl-2-Associated X Protein - chemistry | Humans | BH3 Interacting Domain Death Agonist Protein - genetics | Proto-Oncogene Proteins - chemistry | Neoplasm Proteins - metabolism | bcl-2 Homologous Antagonist-Killer Protein - metabolism | Proto-Oncogene Proteins c-bcl-2 - metabolism | Bcl-2-Like Protein 11 | Tumor Suppressor Proteins - genetics | BH3 Interacting Domain Death Agonist Protein - chemistry | Apoptosis Regulatory Proteins - genetics | bcl-Associated Death Protein - metabolism | Membrane Proteins - metabolism | BH3 Interacting Domain Death Agonist Protein - metabolism | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Cell Line | Tumor Suppressor Proteins - metabolism | Membrane Proteins - genetics | Apoptosis Regulatory Proteins - chemistry | Cells, Cultured | bcl-2-Associated X Protein - metabolism | Proto-Oncogene Proteins - genetics | Apoptosis Regulatory Proteins - metabolism | Mice, Knockout | Animals | Proteins - metabolism | Membrane Proteins - chemistry | Models, Biological | Myeloid Cell Leukemia Sequence 1 Protein | Mice | Mutation | bcl-X Protein - metabolism | Research | Peptides | Analysis
Journal Article
Conference Proceeding