N-Terminomics/TAILS Profiling of Macrophages after Chemical Inhibition of Legumain.
Identifieur interne : 000064 ( Main/Exploration ); précédent : 000063; suivant : 000065N-Terminomics/TAILS Profiling of Macrophages after Chemical Inhibition of Legumain.
Auteurs : Bethany M. Anderson [Australie] ; Luiz G N. De Almeida [Canada] ; Henna Sekhon [Canada] ; Daniel Young [Canada] ; Antoine Dufour [Canada] ; Laura E. Edgington-Mitchell [Australie, États-Unis]Source :
- Biochemistry [ 1520-4995 ] ; 2020.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Asparagine (composition chimique), Asparagine (génétique), Cellules RAW 264.7 (MeSH), Cysteine endopeptidases (composition chimique), Cysteine endopeptidases (génétique), Cysteine endopeptidases (métabolisme), Fer (métabolisme), Humains (MeSH), Macrophages (composition chimique), Macrophages (métabolisme), Marquage isotopique (MeSH), Mitochondries (génétique), Mitochondries (métabolisme), Peptides (composition chimique), Peptides (génétique), Protéomique (MeSH), Régulation de l'expression des gènes (génétique), Souris (MeSH).
- MESH :
- composition chimique : Asparagine, Cysteine endopeptidases, Macrophages, Peptides.
- génétique : Asparagine, Cysteine endopeptidases, Mitochondries, Peptides, Régulation de l'expression des gènes.
- métabolisme : Cysteine endopeptidases, Fer, Macrophages, Mitochondries.
- Animaux, Cellules RAW 264.7, Humains, Marquage isotopique, Protéomique, Souris.
English descriptors
- KwdEn :
- Animals (MeSH), Asparagine (chemistry), Asparagine (genetics), Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Gene Expression Regulation (genetics), Humans (MeSH), Iron (metabolism), Isotope Labeling (MeSH), Macrophages (chemistry), Macrophages (metabolism), Mice (MeSH), Mitochondria (genetics), Mitochondria (metabolism), Peptides (chemistry), Peptides (genetics), Proteomics (MeSH), RAW 264.7 Cells (MeSH).
- MESH :
- chemical , chemistry : Asparagine, Cysteine Endopeptidases, Peptides.
- chemical , genetics : Asparagine, Cysteine Endopeptidases, Peptides.
- chemical , metabolism : Cysteine Endopeptidases, Iron.
- chemistry : Macrophages.
- genetics : Gene Expression Regulation, Mitochondria.
- metabolism : Macrophages, Mitochondria.
- Animals, Humans, Isotope Labeling, Mice, Proteomics, RAW 264.7 Cells.
Abstract
Legumain (asparaginyl endopeptidase) is the only protease with a preference for cleavage after asparagine residues. Increased legumain activity is a hallmark of inflammation, neurodegenerative diseases, and cancer, and legumain inhibitors have exhibited therapeutic effects in mouse models of these pathologies. Improved knowledge of its substrates and cellular functions is a requisite to further validation of legumain as a drug target. We, therefore, aimed to investigate the effects of legumain inhibition in macrophages using an unbiased and systematic approach. By shotgun proteomics, we identified 16 094 unique peptides in RAW264.7 cells. Among these, 326 unique peptides were upregulated in response to legumain inhibition, while 241 were downregulated. Many of these proteins were associated with mitochondria and metabolism, especially iron metabolism, indicating that legumain may have a previously unknown impact on related processes. Furthermore, we used N-terminomics/TAILS (terminal amine isotopic labeling of substrates) to identify potential substrates of legumain. We identified three new proteins that are cleaved after asparagine residues, which may reflect legumain-dependent cleavage. We confirmed that frataxin, a mitochondrial protein associated with the formation of iron-sulfur clusters, can be cleaved by legumain. This further asserts a potential contribution of legumain to mitochondrial function and iron metabolism. Lastly, we also identified a potential new cleavage site within legumain itself that may give rise to a 25 kDa form of legumain that has previously been observed in multiple cell and tissue types. Collectively, these data shed new light on the potential functions of legumain and will be critical for understanding its contribution to disease.
DOI: 10.1021/acs.biochem.9b00821
PubMed: 31774660
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Anderson</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3052 , Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3052 </wicri:regionArea><wicri:noRegion>Victoria 3052 </wicri:noRegion></affiliation></author><author><name sortKey="De Almeida, Luiz G N" sort="De Almeida, Luiz G N" uniqKey="De Almeida L" first="Luiz G N" last="De Almeida">Luiz G N. De Almeida</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 </wicri:regionArea><wicri:noRegion>Alberta T2N 4N1 </wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 </wicri:regionArea><wicri:noRegion>Alberta T2N 4N1 </wicri:noRegion></affiliation></author><author><name sortKey="Sekhon, Henna" sort="Sekhon, Henna" uniqKey="Sekhon H" first="Henna" last="Sekhon">Henna Sekhon</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 </wicri:regionArea><wicri:noRegion>Alberta T2N 4N1 </wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 </wicri:regionArea><wicri:noRegion>Alberta T2N 4N1 </wicri:noRegion></affiliation></author><author><name sortKey="Young, Daniel" sort="Young, Daniel" uniqKey="Young D" first="Daniel" last="Young">Daniel Young</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 </wicri:regionArea><wicri:noRegion>Alberta T2N 4N1 </wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 </wicri:regionArea><wicri:noRegion>Alberta T2N 4N1 </wicri:noRegion></affiliation></author><author><name sortKey="Dufour, Antoine" sort="Dufour, Antoine" uniqKey="Dufour A" first="Antoine" last="Dufour">Antoine Dufour</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 </wicri:regionArea><wicri:noRegion>Alberta T2N 4N1 </wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 </wicri:regionArea><wicri:noRegion>Alberta T2N 4N1 </wicri:noRegion></affiliation></author><author><name sortKey="Edgington Mitchell, Laura E" sort="Edgington Mitchell, Laura E" uniqKey="Edgington Mitchell L" first="Laura E" last="Edgington-Mitchell">Laura E. Edgington-Mitchell</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3052 , Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3052 </wicri:regionArea><wicri:noRegion>Victoria 3052 </wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences , Monash University , Parkville , Victoria 3052 , Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences , Monash University , Parkville , Victoria 3052 </wicri:regionArea><wicri:noRegion>Victoria 3052 </wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Oral and Maxillofacial Surgery , New York University College of Dentistry, Bluestone Center for Clinical Research , New York , New York 10010 , United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Oral and Maxillofacial Surgery , New York University College of Dentistry, Bluestone Center for Clinical Research , New York , New York 10010 </wicri:regionArea><wicri:noRegion>New York 10010 </wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Asparagine (chemistry)</term><term>Asparagine (genetics)</term><term>Cysteine Endopeptidases (chemistry)</term><term>Cysteine Endopeptidases (genetics)</term><term>Cysteine Endopeptidases (metabolism)</term><term>Gene Expression Regulation (genetics)</term><term>Humans (MeSH)</term><term>Iron (metabolism)</term><term>Isotope Labeling (MeSH)</term><term>Macrophages (chemistry)</term><term>Macrophages (metabolism)</term><term>Mice (MeSH)</term><term>Mitochondria (genetics)</term><term>Mitochondria (metabolism)</term><term>Peptides (chemistry)</term><term>Peptides (genetics)</term><term>Proteomics (MeSH)</term><term>RAW 264.7 Cells (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Asparagine (composition chimique)</term><term>Asparagine (génétique)</term><term>Cellules RAW 264.7 (MeSH)</term><term>Cysteine endopeptidases (composition chimique)</term><term>Cysteine endopeptidases (génétique)</term><term>Cysteine endopeptidases (métabolisme)</term><term>Fer (métabolisme)</term><term>Humains (MeSH)</term><term>Macrophages (composition chimique)</term><term>Macrophages (métabolisme)</term><term>Marquage isotopique (MeSH)</term><term>Mitochondries (génétique)</term><term>Mitochondries (métabolisme)</term><term>Peptides (composition chimique)</term><term>Peptides (génétique)</term><term>Protéomique (MeSH)</term><term>Régulation de l'expression des gènes (génétique)</term><term>Souris (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Asparagine</term><term>Cysteine Endopeptidases</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Asparagine</term><term>Cysteine Endopeptidases</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Iron</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Macrophages</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Asparagine</term><term>Cysteine endopeptidases</term><term>Macrophages</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Gene Expression Regulation</term><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Asparagine</term><term>Cysteine endopeptidases</term><term>Mitochondries</term><term>Peptides</term><term>Régulation de l'expression des gènes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Macrophages</term><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Fer</term><term>Macrophages</term><term>Mitochondries</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Isotope Labeling</term><term>Mice</term><term>Proteomics</term><term>RAW 264.7 Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules RAW 264.7</term><term>Humains</term><term>Marquage isotopique</term><term>Protéomique</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Legumain (asparaginyl endopeptidase) is the only protease with a preference for cleavage after asparagine residues. Increased legumain activity is a hallmark of inflammation, neurodegenerative diseases, and cancer, and legumain inhibitors have exhibited therapeutic effects in mouse models of these pathologies. Improved knowledge of its substrates and cellular functions is a requisite to further validation of legumain as a drug target. We, therefore, aimed to investigate the effects of legumain inhibition in macrophages using an unbiased and systematic approach. By shotgun proteomics, we identified 16 094 unique peptides in RAW264.7 cells. Among these, 326 unique peptides were upregulated in response to legumain inhibition, while 241 were downregulated. Many of these proteins were associated with mitochondria and metabolism, especially iron metabolism, indicating that legumain may have a previously unknown impact on related processes. Furthermore, we used N-terminomics/TAILS (terminal amine isotopic labeling of substrates) to identify potential substrates of legumain. We identified three new proteins that are cleaved after asparagine residues, which may reflect legumain-dependent cleavage. We confirmed that frataxin, a mitochondrial protein associated with the formation of iron-sulfur clusters, can be cleaved by legumain. This further asserts a potential contribution of legumain to mitochondrial function and iron metabolism. Lastly, we also identified a potential new cleavage site within legumain itself that may give rise to a 25 kDa form of legumain that has previously been observed in multiple cell and tissue types. Collectively, these data shed new light on the potential functions of legumain and will be critical for understanding its contribution to disease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31774660</PMID><DateCompleted><Year>2020</Year><Month>07</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>59</Volume><Issue>3</Issue><PubDate><Year>2020</Year><Month>01</Month><Day>28</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>N-Terminomics/TAILS Profiling of Macrophages after Chemical Inhibition of Legumain.</ArticleTitle><Pagination><MedlinePgn>329-340</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.9b00821</ELocationID><Abstract><AbstractText>Legumain (asparaginyl endopeptidase) is the only protease with a preference for cleavage after asparagine residues. Increased legumain activity is a hallmark of inflammation, neurodegenerative diseases, and cancer, and legumain inhibitors have exhibited therapeutic effects in mouse models of these pathologies. Improved knowledge of its substrates and cellular functions is a requisite to further validation of legumain as a drug target. We, therefore, aimed to investigate the effects of legumain inhibition in macrophages using an unbiased and systematic approach. By shotgun proteomics, we identified 16 094 unique peptides in RAW264.7 cells. Among these, 326 unique peptides were upregulated in response to legumain inhibition, while 241 were downregulated. Many of these proteins were associated with mitochondria and metabolism, especially iron metabolism, indicating that legumain may have a previously unknown impact on related processes. Furthermore, we used N-terminomics/TAILS (terminal amine isotopic labeling of substrates) to identify potential substrates of legumain. We identified three new proteins that are cleaved after asparagine residues, which may reflect legumain-dependent cleavage. We confirmed that frataxin, a mitochondrial protein associated with the formation of iron-sulfur clusters, can be cleaved by legumain. This further asserts a potential contribution of legumain to mitochondrial function and iron metabolism. Lastly, we also identified a potential new cleavage site within legumain itself that may give rise to a 25 kDa form of legumain that has previously been observed in multiple cell and tissue types. Collectively, these data shed new light on the potential functions of legumain and will be critical for understanding its contribution to disease.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Anderson</LastName><ForeName>Bethany M</ForeName><Initials>BM</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3052 , Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Almeida</LastName><ForeName>Luiz G N</ForeName><Initials>LGN</Initials><AffiliationInfo><Affiliation>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sekhon</LastName><ForeName>Henna</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Young</LastName><ForeName>Daniel</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dufour</LastName><ForeName>Antoine</ForeName><Initials>A</Initials><Identifier Source="ORCID">0000-0002-3429-4188</Identifier><AffiliationInfo><Affiliation>Department of Physiology and Pharmacology , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>McCaig Institute for Bone and Joint Health , University of Calgary , Calgary , Alberta T2N 4N1 , Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Edgington-Mitchell</LastName><ForeName>Laura E</ForeName><Initials>LE</Initials><Identifier Source="ORCID">0000-0002-6810-6149</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute , The University of Melbourne , Parkville , Victoria 3052 , Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences , Monash University , Parkville , Victoria 3052 , Australia.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Oral and Maxillofacial Surgery , New York University College of Dentistry, Bluestone Center for Clinical Research , New York , New York 10010 , United States.</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><ArticleDate DateType="Electronic"><Year>2019</Year><Month>11</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>7006-34-0</RegistryNumber><NameOfSubstance UI="D001216">Asparagine</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.34</RegistryNumber><NameOfSubstance UI="C069586">asparaginylendopeptidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001216" MajorTopicYN="N">Asparagine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007553" MajorTopicYN="N">Isotope Labeling</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008264" MajorTopicYN="N">Macrophages</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="Y">Proteomics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000067996" MajorTopicYN="N">RAW 264.7 Cells</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>7</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31774660</ArticleId><ArticleId IdType="doi">10.1021/acs.biochem.9b00821</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>Canada</li><li>États-Unis</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Anderson, Bethany M" sort="Anderson, Bethany M" uniqKey="Anderson B" first="Bethany M" last="Anderson">Bethany M. Anderson</name></noRegion><name sortKey="Edgington Mitchell, Laura E" sort="Edgington Mitchell, Laura E" uniqKey="Edgington Mitchell L" first="Laura E" last="Edgington-Mitchell">Laura E. Edgington-Mitchell</name><name sortKey="Edgington Mitchell, Laura E" sort="Edgington Mitchell, Laura E" uniqKey="Edgington Mitchell L" first="Laura E" last="Edgington-Mitchell">Laura E. Edgington-Mitchell</name></country><country name="Canada"><noRegion><name sortKey="De Almeida, Luiz G N" sort="De Almeida, Luiz G N" uniqKey="De Almeida L" first="Luiz G N" last="De Almeida">Luiz G N. De Almeida</name></noRegion><name sortKey="De Almeida, Luiz G N" sort="De Almeida, Luiz G N" uniqKey="De Almeida L" first="Luiz G N" last="De Almeida">Luiz G N. De Almeida</name><name sortKey="Dufour, Antoine" sort="Dufour, Antoine" uniqKey="Dufour A" first="Antoine" last="Dufour">Antoine Dufour</name><name sortKey="Dufour, Antoine" sort="Dufour, Antoine" uniqKey="Dufour A" first="Antoine" last="Dufour">Antoine Dufour</name><name sortKey="Sekhon, Henna" sort="Sekhon, Henna" uniqKey="Sekhon H" first="Henna" last="Sekhon">Henna Sekhon</name><name sortKey="Sekhon, Henna" sort="Sekhon, Henna" uniqKey="Sekhon H" first="Henna" last="Sekhon">Henna Sekhon</name><name sortKey="Young, Daniel" sort="Young, Daniel" uniqKey="Young D" first="Daniel" last="Young">Daniel Young</name><name sortKey="Young, Daniel" sort="Young, Daniel" uniqKey="Young D" first="Daniel" last="Young">Daniel Young</name></country><country name="États-Unis"><noRegion><name sortKey="Edgington Mitchell, Laura E" sort="Edgington Mitchell, Laura E" uniqKey="Edgington Mitchell L" first="Laura E" last="Edgington-Mitchell">Laura E. Edgington-Mitchell</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Bois
|area= IronSulferCluV1
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|texte= N-Terminomics/TAILS Profiling of Macrophages after Chemical Inhibition of Legumain.
}}
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