Changes in Glutathione Redox Potential Are Linked to Aβ42-Induced Neurotoxicity.
Identifieur interne : 000285 ( Main/Exploration ); précédent : 000284; suivant : 000286Changes in Glutathione Redox Potential Are Linked to Aβ42-Induced Neurotoxicity.
Auteurs : Zeenna A. Stapper [Allemagne] ; Thomas R. Jahn [Allemagne]Source :
- Cell reports [ 2211-1247 ] ; 2018.
Descripteurs français
- KwdFr :
- Agrégation pathologique de protéines (anatomopathologie), Agrégation pathologique de protéines (génétique), Agrégation pathologique de protéines (métabolisme), Agrégats de protéines (génétique), Animal génétiquement modifié (MeSH), Animaux (MeSH), Drosophila melanogaster (MeSH), Fragments peptidiques (génétique), Fragments peptidiques (métabolisme), Fragments peptidiques (toxicité), Glutamate-cysteine ligase (génétique), Glutamate-cysteine ligase (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Glutathione peroxidase (génétique), Glutathione peroxidase (métabolisme), Gènes rapporteurs (MeSH), Homéostasie (génétique), Humains (MeSH), Maladie d'Alzheimer (anatomopathologie), Maladie d'Alzheimer (génétique), Maladie d'Alzheimer (métabolisme), Modèles animaux de maladie humaine (MeSH), Neurones (anatomopathologie), Neurones (effets des médicaments et des substances chimiques), Neurones (métabolisme), Névroglie (cytologie), Névroglie (effets des médicaments et des substances chimiques), Névroglie (métabolisme), Oxydoréduction (MeSH), Peptides bêta-amyloïdes (génétique), Peptides bêta-amyloïdes (métabolisme), Peptides bêta-amyloïdes (toxicité), Protéines luminescentes (génétique), Protéines luminescentes (métabolisme), Protéines à fluorescence verte (génétique), Protéines à fluorescence verte (métabolisme), Régulation de l'expression des gènes (effets des médicaments et des substances chimiques), Stress oxydatif (MeSH), Système de signalisation des MAP kinases (MeSH), Évolution de la maladie (MeSH).
- MESH :
- anatomopathologie : Agrégation pathologique de protéines, Maladie d'Alzheimer, Neurones.
- cytologie : Névroglie.
- effets des médicaments et des substances chimiques : Neurones, Névroglie, Régulation de l'expression des gènes.
- génétique : Agrégation pathologique de protéines, Agrégats de protéines, Fragments peptidiques, Glutamate-cysteine ligase, Glutarédoxines, Glutathione peroxidase, Homéostasie, Maladie d'Alzheimer, Peptides bêta-amyloïdes, Protéines luminescentes, Protéines à fluorescence verte.
- métabolisme : Agrégation pathologique de protéines, Fragments peptidiques, Glutamate-cysteine ligase, Glutarédoxines, Glutathion, Glutathione peroxidase, Maladie d'Alzheimer, Neurones, Névroglie, Peptides bêta-amyloïdes, Protéines luminescentes, Protéines à fluorescence verte.
- toxicité : Fragments peptidiques, Peptides bêta-amyloïdes.
- Animal génétiquement modifié, Animaux, Drosophila melanogaster, Gènes rapporteurs, Humains, Modèles animaux de maladie humaine, Oxydoréduction, Stress oxydatif, Système de signalisation des MAP kinases, Évolution de la maladie.
English descriptors
- KwdEn :
- Alzheimer Disease (genetics), Alzheimer Disease (metabolism), Alzheimer Disease (pathology), Amyloid beta-Peptides (genetics), Amyloid beta-Peptides (metabolism), Amyloid beta-Peptides (toxicity), Animals (MeSH), Animals, Genetically Modified (MeSH), Disease Models, Animal (MeSH), Disease Progression (MeSH), Drosophila melanogaster (MeSH), Gene Expression Regulation (drug effects), Genes, Reporter (MeSH), Glutamate-Cysteine Ligase (genetics), Glutamate-Cysteine Ligase (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Peroxidase (genetics), Glutathione Peroxidase (metabolism), Green Fluorescent Proteins (genetics), Green Fluorescent Proteins (metabolism), Homeostasis (genetics), Humans (MeSH), Luminescent Proteins (genetics), Luminescent Proteins (metabolism), MAP Kinase Signaling System (MeSH), Neuroglia (cytology), Neuroglia (drug effects), Neuroglia (metabolism), Neurons (drug effects), Neurons (metabolism), Neurons (pathology), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Peptide Fragments (genetics), Peptide Fragments (metabolism), Peptide Fragments (toxicity), Protein Aggregates (genetics), Protein Aggregation, Pathological (genetics), Protein Aggregation, Pathological (metabolism), Protein Aggregation, Pathological (pathology).
- MESH :
- chemical , genetics : Amyloid beta-Peptides, Glutamate-Cysteine Ligase, Glutaredoxins, Glutathione Peroxidase, Green Fluorescent Proteins, Luminescent Proteins, Peptide Fragments, Protein Aggregates.
- cytology : Neuroglia.
- drug effects : Gene Expression Regulation, Neuroglia, Neurons.
- genetics : Alzheimer Disease, Homeostasis, Protein Aggregation, Pathological.
- metabolism : Alzheimer Disease, Amyloid beta-Peptides, Glutamate-Cysteine Ligase, Glutaredoxins, Glutathione, Glutathione Peroxidase, Green Fluorescent Proteins, Luminescent Proteins, Neuroglia, Neurons, Peptide Fragments, Protein Aggregation, Pathological.
- pathology : Alzheimer Disease, Neurons, Protein Aggregation, Pathological.
- chemical , toxicity : Amyloid beta-Peptides, Peptide Fragments.
- Animals, Animals, Genetically Modified, Disease Models, Animal, Disease Progression, Drosophila melanogaster, Genes, Reporter, Humans, MAP Kinase Signaling System, Oxidation-Reduction, Oxidative Stress.
Abstract
Glutathione is the major low-molecular weight thiol of eukaryotic cells. It is central to one of the two major NADPH-dependent reducing systems and is likely to play a role in combating oxidative stress, a process suggested to play a key role in Alzheimer's disease (AD). However, the nature and relevance of redox changes in the onset and progression of AD are still uncertain. Here, we combine genetically encoded redox sensors with our Drosophila models of amyloid-beta (Aβ) aggregation. We find that changes in glutathione redox potential (EGSH) closely correlate with disease onset and progression. We observe this redox imbalance specifically in neurons, but not in glia cells. EGSH changes and Aβ42 deposition are also accompanied by increased JNK stress signaling. Furthermore, pharmacologic and genetic manipulation of glutathione synthesis modulates Aβ42-mediated neurotoxicity, suggesting a causal relationship between disturbed glutathione redox homeostasis and early AD pathology.
DOI: 10.1016/j.celrep.2018.07.052
PubMed: 30110626
Affiliations:
Links toward previous steps (curation, corpus...)
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(toxicity)</term><term>Animals (MeSH)</term><term>Animals, Genetically Modified (MeSH)</term><term>Disease Models, Animal (MeSH)</term><term>Disease Progression (MeSH)</term><term>Drosophila melanogaster (MeSH)</term><term>Gene Expression Regulation (drug effects)</term><term>Genes, Reporter (MeSH)</term><term>Glutamate-Cysteine Ligase (genetics)</term><term>Glutamate-Cysteine Ligase (metabolism)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Glutathione Peroxidase (genetics)</term><term>Glutathione Peroxidase (metabolism)</term><term>Green Fluorescent Proteins (genetics)</term><term>Green Fluorescent Proteins (metabolism)</term><term>Homeostasis (genetics)</term><term>Humans (MeSH)</term><term>Luminescent Proteins (genetics)</term><term>Luminescent Proteins (metabolism)</term><term>MAP Kinase Signaling System (MeSH)</term><term>Neuroglia (cytology)</term><term>Neuroglia (drug effects)</term><term>Neuroglia (metabolism)</term><term>Neurons (drug effects)</term><term>Neurons (metabolism)</term><term>Neurons (pathology)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Peptide Fragments (genetics)</term><term>Peptide Fragments (metabolism)</term><term>Peptide Fragments (toxicity)</term><term>Protein Aggregates (genetics)</term><term>Protein Aggregation, Pathological (genetics)</term><term>Protein Aggregation, Pathological (metabolism)</term><term>Protein Aggregation, Pathological (pathology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agrégation pathologique de protéines (anatomopathologie)</term><term>Agrégation pathologique de protéines (génétique)</term><term>Agrégation pathologique de protéines (métabolisme)</term><term>Agrégats de protéines (génétique)</term><term>Animal génétiquement modifié (MeSH)</term><term>Animaux (MeSH)</term><term>Drosophila melanogaster (MeSH)</term><term>Fragments peptidiques (génétique)</term><term>Fragments peptidiques (métabolisme)</term><term>Fragments peptidiques (toxicité)</term><term>Glutamate-cysteine ligase (génétique)</term><term>Glutamate-cysteine ligase (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Glutathione peroxidase (génétique)</term><term>Glutathione peroxidase (métabolisme)</term><term>Gènes rapporteurs (MeSH)</term><term>Homéostasie (génétique)</term><term>Humains (MeSH)</term><term>Maladie d'Alzheimer (anatomopathologie)</term><term>Maladie d'Alzheimer (génétique)</term><term>Maladie d'Alzheimer (métabolisme)</term><term>Modèles animaux de maladie humaine (MeSH)</term><term>Neurones (anatomopathologie)</term><term>Neurones (effets des médicaments et des substances chimiques)</term><term>Neurones (métabolisme)</term><term>Névroglie (cytologie)</term><term>Névroglie (effets des médicaments et des substances chimiques)</term><term>Névroglie (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Peptides bêta-amyloïdes (génétique)</term><term>Peptides bêta-amyloïdes (métabolisme)</term><term>Peptides bêta-amyloïdes (toxicité)</term><term>Protéines luminescentes (génétique)</term><term>Protéines luminescentes (métabolisme)</term><term>Protéines à fluorescence verte (génétique)</term><term>Protéines à fluorescence verte (métabolisme)</term><term>Régulation de l'expression des gènes (effets des médicaments et des substances chimiques)</term><term>Stress oxydatif (MeSH)</term><term>Système de signalisation des MAP kinases (MeSH)</term><term>Évolution de la maladie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amyloid beta-Peptides</term><term>Glutamate-Cysteine Ligase</term><term>Glutaredoxins</term><term>Glutathione Peroxidase</term><term>Green Fluorescent Proteins</term><term>Luminescent Proteins</term><term>Peptide Fragments</term><term>Protein Aggregates</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Agrégation pathologique de protéines</term><term>Maladie d'Alzheimer</term><term>Neurones</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Névroglie</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Neuroglia</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Gene Expression Regulation</term><term>Neuroglia</term><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Neurones</term><term>Névroglie</term><term>Régulation de l'expression des gènes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Alzheimer Disease</term><term>Homeostasis</term><term>Protein Aggregation, Pathological</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Agrégation pathologique de protéines</term><term>Agrégats de protéines</term><term>Fragments peptidiques</term><term>Glutamate-cysteine ligase</term><term>Glutarédoxines</term><term>Glutathione peroxidase</term><term>Homéostasie</term><term>Maladie d'Alzheimer</term><term>Peptides bêta-amyloïdes</term><term>Protéines luminescentes</term><term>Protéines à fluorescence verte</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Alzheimer Disease</term><term>Amyloid beta-Peptides</term><term>Glutamate-Cysteine Ligase</term><term>Glutaredoxins</term><term>Glutathione</term><term>Glutathione Peroxidase</term><term>Green Fluorescent Proteins</term><term>Luminescent Proteins</term><term>Neuroglia</term><term>Neurons</term><term>Peptide Fragments</term><term>Protein Aggregation, Pathological</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Agrégation pathologique de protéines</term><term>Fragments peptidiques</term><term>Glutamate-cysteine ligase</term><term>Glutarédoxines</term><term>Glutathion</term><term>Glutathione peroxidase</term><term>Maladie d'Alzheimer</term><term>Neurones</term><term>Névroglie</term><term>Peptides bêta-amyloïdes</term><term>Protéines luminescentes</term><term>Protéines à fluorescence verte</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Alzheimer Disease</term><term>Neurons</term><term>Protein Aggregation, Pathological</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Amyloid beta-Peptides</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Fragments peptidiques</term><term>Peptides bêta-amyloïdes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Animals, Genetically Modified</term><term>Disease Models, Animal</term><term>Disease Progression</term><term>Drosophila melanogaster</term><term>Genes, Reporter</term><term>Humans</term><term>MAP Kinase Signaling System</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animal génétiquement modifié</term><term>Animaux</term><term>Drosophila melanogaster</term><term>Gènes rapporteurs</term><term>Humains</term><term>Modèles animaux de maladie humaine</term><term>Oxydoréduction</term><term>Stress oxydatif</term><term>Système de signalisation des MAP kinases</term><term>Évolution de la maladie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione is the major low-molecular weight thiol of eukaryotic cells. It is central to one of the two major NADPH-dependent reducing systems and is likely to play a role in combating oxidative stress, a process suggested to play a key role in Alzheimer's disease (AD). However, the nature and relevance of redox changes in the onset and progression of AD are still uncertain. Here, we combine genetically encoded redox sensors with our Drosophila models of amyloid-beta (Aβ) aggregation. We find that changes in glutathione redox potential (E<sub>GSH</sub>) closely correlate with disease onset and progression. We observe this redox imbalance specifically in neurons, but not in glia cells. E<sub>GSH</sub> changes and Aβ<sub>42</sub> deposition are also accompanied by increased JNK stress signaling. Furthermore, pharmacologic and genetic manipulation of glutathione synthesis modulates Aβ<sub>42</sub>-mediated neurotoxicity, suggesting a causal relationship between disturbed glutathione redox homeostasis and early AD pathology.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30110626</PMID><DateCompleted><Year>2019</Year><Month>11</Month><Day>25</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">2211-1247</ISSN><JournalIssue CitedMedium="Internet"><Volume>24</Volume><Issue>7</Issue><PubDate><Year>2018</Year><Month>08</Month><Day>14</Day></PubDate></JournalIssue><Title>Cell reports</Title><ISOAbbreviation>Cell Rep</ISOAbbreviation></Journal><ArticleTitle>Changes in Glutathione Redox Potential Are Linked to Aβ<sub>42</sub>-Induced Neurotoxicity.</ArticleTitle><Pagination><MedlinePgn>1696-1703</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S2211-1247(18)31155-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.celrep.2018.07.052</ELocationID><Abstract><AbstractText>Glutathione is the major low-molecular weight thiol of eukaryotic cells. It is central to one of the two major NADPH-dependent reducing systems and is likely to play a role in combating oxidative stress, a process suggested to play a key role in Alzheimer's disease (AD). However, the nature and relevance of redox changes in the onset and progression of AD are still uncertain. Here, we combine genetically encoded redox sensors with our Drosophila models of amyloid-beta (Aβ) aggregation. We find that changes in glutathione redox potential (E<sub>GSH</sub>) closely correlate with disease onset and progression. We observe this redox imbalance specifically in neurons, but not in glia cells. E<sub>GSH</sub> changes and Aβ<sub>42</sub> deposition are also accompanied by increased JNK stress signaling. Furthermore, pharmacologic and genetic manipulation of glutathione synthesis modulates Aβ<sub>42</sub>-mediated neurotoxicity, suggesting a causal relationship between disturbed glutathione redox homeostasis and early AD pathology.</AbstractText><CopyrightInformation>Copyright © 2018 The Author(s). Published by Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stapper</LastName><ForeName>Zeenna A</ForeName><Initials>ZA</Initials><AffiliationInfo><Affiliation>Schaller Research Group Proteostasis in Neurodegenerative Disease, University of Heidelberg and the DKFZ, INF 581, 69120 Heidelberg, Germany; Faculty of Biosciences, Heidelberg University, INF 234, 69120 Heidelberg, Germany; German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Center of Molecular Biology of Heidelberg University (ZMBH), INF 280 and 282, 69120 Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jahn</LastName><ForeName>Thomas R</ForeName><Initials>TR</Initials><AffiliationInfo><Affiliation>Schaller Research Group Proteostasis in Neurodegenerative Disease, University of Heidelberg and the DKFZ, INF 581, 69120 Heidelberg, Germany. Electronic address: thomas.r.jahn@abbvie.com.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell Rep</MedlineTA><NlmUniqueID>101573691</NlmUniqueID></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016229">Amyloid beta-Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008164">Luminescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D066329">Protein Aggregates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C075222">amyloid beta-protein (1-42)</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C413663">fluorescent protein 583</NameOfSubstance></Chemical><Chemical><RegistryNumber>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.3.2.2</RegistryNumber><NameOfSubstance UI="D005721">Glutamate-Cysteine Ligase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000544" MajorTopicYN="N">Alzheimer Disease</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016229" MajorTopicYN="N">Amyloid beta-Peptides</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D030801" MajorTopicYN="N">Animals, Genetically Modified</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018450" MajorTopicYN="N">Disease Progression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004331" MajorTopicYN="N">Drosophila melanogaster</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017930" MajorTopicYN="N">Genes, Reporter</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005721" MajorTopicYN="N">Glutamate-Cysteine Ligase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" 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MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008164" MajorTopicYN="N">Luminescent Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020935" MajorTopicYN="N">MAP Kinase Signaling System</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009457" MajorTopicYN="N">Neuroglia</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D066329" MajorTopicYN="N">Protein Aggregates</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D066263" MajorTopicYN="N">Protein Aggregation, Pathological</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Alzheimer’s disease</Keyword><Keyword MajorTopicYN="Y">Drosophila models</Keyword><Keyword MajorTopicYN="Y">amyloid-beta</Keyword><Keyword MajorTopicYN="Y">glutathione redox balance</Keyword><Keyword MajorTopicYN="Y">redox sensors</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>10</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>05</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>07</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>8</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>8</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>11</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30110626</ArticleId><ArticleId IdType="pii">S2211-1247(18)31155-0</ArticleId><ArticleId IdType="doi">10.1016/j.celrep.2018.07.052</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bade-Wurtemberg</li><li>District de Karlsruhe</li></region><settlement><li>Heidelberg</li></settlement></list><tree><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Stapper, Zeenna A" sort="Stapper, Zeenna A" uniqKey="Stapper Z" first="Zeenna A" last="Stapper">Zeenna A. Stapper</name></region><name sortKey="Jahn, Thomas R" sort="Jahn, Thomas R" uniqKey="Jahn T" first="Thomas R" last="Jahn">Thomas R. Jahn</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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