The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.
Identifieur interne : 000976 ( PubMed/Curation ); précédent : 000975; suivant : 000977The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.
Auteurs : Blagojce Jovcevski [Australie] ; J. Andrew Aquilina [Australie] ; Justin L P. Benesch [Royaume-Uni] ; Heath Ecroyd [Australie]Source :
- Cell stress & chaperones [ 1466-1268 ] ; 2018.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : alpha-Crystallin B Chain.
- chemical , genetics : alpha-Crystallin B Chain.
- chemical , metabolism : alpha-Crystallin B Chain.
- Humans, Mutation, Protein Domains, Protein Multimerization, Protein Structure, Secondary.
Abstract
αB-Crystallin (HSPB5) is a small heat-shock protein that is composed of dimers that then assemble into a polydisperse ensemble of oligomers. Oligomerisation is mediated by heterologous interactions between the C-terminal tail of one dimer and the core "α-crystallin" domain of another and stabilised by interactions made by the N-terminal region. Comparatively little is known about the latter contribution, but previous studies have suggested that residues in the region 54-60 form contacts that stabilise the assembly. We have generated mutations in this region (P58A, S59A, S59K, R56S/S59R and an inversion of residues 54-60) to examine their impact on oligomerisation and chaperone activity in vitro. By using native mass spectrometry, we found that all the αB-crystallin mutants were assembly competent, populating similar oligomeric distributions to wild-type, ranging from 16-mers to 30-mers. However, circular dichroism spectroscopy, intrinsic tryptophan and bis-ANS fluorescence studies demonstrated that the secondary structure differs to wild type, the 54-60 inversion mutation having the greatest impact. All the mutants exhibited a dramatic decrease in exposed hydrophobicity. We also found that the mutants in general were equally active as the wild-type protein in inhibiting the amorphous aggregation of insulin and seeded amyloid fibrillation of α-synuclein in vitro, except for the 54-60 inversion mutant, which was significantly less effective at inhibiting insulin aggregation. Our data indicate that alterations in the part of the N-terminal region proximal to the core domain do not drastically affect the oligomerisation of αB-crystallin, reinforcing the robustness of αB-crystallin in functioning as a molecular chaperone.
DOI: 10.1007/s12192-018-0889-y
PubMed: 29520626
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Oligomerisation is mediated by heterologous interactions between the C-terminal tail of one dimer and the core "α-crystallin" domain of another and stabilised by interactions made by the N-terminal region. Comparatively little is known about the latter contribution, but previous studies have suggested that residues in the region 54-60 form contacts that stabilise the assembly. We have generated mutations in this region (P58A, S59A, S59K, R56S/S59R and an inversion of residues 54-60) to examine their impact on oligomerisation and chaperone activity in vitro. By using native mass spectrometry, we found that all the αB-crystallin mutants were assembly competent, populating similar oligomeric distributions to wild-type, ranging from 16-mers to 30-mers. However, circular dichroism spectroscopy, intrinsic tryptophan and bis-ANS fluorescence studies demonstrated that the secondary structure differs to wild type, the 54-60 inversion mutation having the greatest impact. All the mutants exhibited a dramatic decrease in exposed hydrophobicity. We also found that the mutants in general were equally active as the wild-type protein in inhibiting the amorphous aggregation of insulin and seeded amyloid fibrillation of α-synuclein in vitro, except for the 54-60 inversion mutant, which was significantly less effective at inhibiting insulin aggregation. Our data indicate that alterations in the part of the N-terminal region proximal to the core domain do not drastically affect the oligomerisation of αB-crystallin, reinforcing the robustness of αB-crystallin in functioning as a molecular chaperone.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29520626</PMID><DateCompleted><Year>2019</Year><Month>05</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1466-1268</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>5</Issue><PubDate><Year>2018</Year><Month>09</Month></PubDate></JournalIssue><Title>Cell stress & chaperones</Title><ISOAbbreviation>Cell Stress Chaperones</ISOAbbreviation></Journal><ArticleTitle>The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.</ArticleTitle><Pagination><MedlinePgn>827-836</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12192-018-0889-y</ELocationID><Abstract><AbstractText>αB-Crystallin (HSPB5) is a small heat-shock protein that is composed of dimers that then assemble into a polydisperse ensemble of oligomers. Oligomerisation is mediated by heterologous interactions between the C-terminal tail of one dimer and the core "α-crystallin" domain of another and stabilised by interactions made by the N-terminal region. Comparatively little is known about the latter contribution, but previous studies have suggested that residues in the region 54-60 form contacts that stabilise the assembly. We have generated mutations in this region (P58A, S59A, S59K, R56S/S59R and an inversion of residues 54-60) to examine their impact on oligomerisation and chaperone activity in vitro. By using native mass spectrometry, we found that all the αB-crystallin mutants were assembly competent, populating similar oligomeric distributions to wild-type, ranging from 16-mers to 30-mers. However, circular dichroism spectroscopy, intrinsic tryptophan and bis-ANS fluorescence studies demonstrated that the secondary structure differs to wild type, the 54-60 inversion mutation having the greatest impact. All the mutants exhibited a dramatic decrease in exposed hydrophobicity. We also found that the mutants in general were equally active as the wild-type protein in inhibiting the amorphous aggregation of insulin and seeded amyloid fibrillation of α-synuclein in vitro, except for the 54-60 inversion mutant, which was significantly less effective at inhibiting insulin aggregation. Our data indicate that alterations in the part of the N-terminal region proximal to the core domain do not drastically affect the oligomerisation of αB-crystallin, reinforcing the robustness of αB-crystallin in functioning as a molecular chaperone.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jovcevski</LastName><ForeName>Blagojce</ForeName><Initials>B</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-7999-1385</Identifier><AffiliationInfo><Affiliation>Illawarra Health and Medical Research Institute and School of Biological Sciences, University of Wollongong, Northfields Ave, Wollongong, NSW, 2522, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Andrew Aquilina</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Illawarra Health and Medical Research Institute and School of Biological Sciences, University of Wollongong, Northfields Ave, Wollongong, NSW, 2522, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Benesch</LastName><ForeName>Justin L P</ForeName><Initials>JLP</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ecroyd</LastName><ForeName>Heath</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Illawarra Health and Medical Research Institute and School of Biological Sciences, University of Wollongong, Northfields Ave, Wollongong, NSW, 2522, Australia. heathe@uow.edu.au.</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>2018</Year><Month>03</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Cell Stress Chaperones</MedlineTA><NlmUniqueID>9610925</NlmUniqueID><ISSNLinking>1355-8145</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C059215">CRYAB protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D038203">alpha-Crystallin B Chain</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein Domains</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D038203" MajorTopicYN="N">alpha-Crystallin B Chain</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Amyloid fibrils</Keyword><Keyword MajorTopicYN="Y">HSPB5</Keyword><Keyword MajorTopicYN="Y">Molecular chaperone</Keyword><Keyword MajorTopicYN="Y">Native mass spectrometry</Keyword><Keyword MajorTopicYN="Y">Protein aggregation</Keyword><Keyword MajorTopicYN="Y">Proteostasis</Keyword><Keyword MajorTopicYN="Y">Small heat-shock protein</Keyword><Keyword MajorTopicYN="Y">αB-crystallin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>01</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>02</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>02</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>5</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29520626</ArticleId><ArticleId IdType="doi">10.1007/s12192-018-0889-y</ArticleId><ArticleId IdType="pii">10.1007/s12192-018-0889-y</ArticleId><ArticleId IdType="pmc">PMC6111084</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Methods Enzymol. 1998;290:365-83</Citation><ArticleIdList><ArticleId IdType="pubmed">9534176</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochim Biophys Acta. 2016 Jan;1860(1 Pt B):149-66</Citation><ArticleIdList><ArticleId IdType="pubmed">26116912</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2004 Feb 27;315(1):113-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15013433</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2017 Oct 13;429(20):3018-3030</Citation><ArticleIdList><ArticleId IdType="pubmed">28918091</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Philos Trans R Soc Lond B Biol Sci. 2013 Mar 25;368(1617):20110405</Citation><ArticleIdList><ArticleId IdType="pubmed">23530258</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Cell Mol Life Sci. 2009 Jan;66(1):62-81</Citation><ArticleIdList><ArticleId IdType="pubmed">18810322</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nat Struct Mol Biol. 2010 Sep;17(9):1037-42</Citation><ArticleIdList><ArticleId IdType="pubmed">20802487</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2011 Oct 21;413(2):297-309</Citation><ArticleIdList><ArticleId IdType="pubmed">21839090</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nat Struct Biol. 2001 Dec;8(12):1025-30</Citation><ArticleIdList><ArticleId IdType="pubmed">11702068</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Struct Biol. 2011 Apr;174(1):92-9</Citation><ArticleIdList><ArticleId IdType="pubmed">21195185</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Neurochem. 2016 May;137(4):489-505</Citation><ArticleIdList><ArticleId IdType="pubmed">26872075</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Structure. 2011 Dec 7;19(12):1855-63</Citation><ArticleIdList><ArticleId IdType="pubmed">22153508</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Cell Stress Chaperones. 2013 Jan;18(1):75-85</Citation><ArticleIdList><ArticleId IdType="pubmed">22851138</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem J. 2012 Dec 15;448(3):343-52</Citation><ArticleIdList><ArticleId IdType="pubmed">23005341</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2012 Jun 26;51(25):5105-12</Citation><ArticleIdList><ArticleId IdType="pubmed">22670769</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>PLoS One. 2014 Aug 26;9(8):e105892</Citation><ArticleIdList><ArticleId IdType="pubmed">25157403</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nature. 2011 Jul 20;475(7356):324-32</Citation><ArticleIdList><ArticleId IdType="pubmed">21776078</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2017 Jun 16;292(24):9944-9957</Citation><ArticleIdList><ArticleId IdType="pubmed">28487364</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Structure. 2015 Nov 3;23(11):2066-75</Citation><ArticleIdList><ArticleId IdType="pubmed">26439766</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2014 Apr 22;111(16):E1562-70</Citation><ArticleIdList><ArticleId IdType="pubmed">24711386</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Prog Biophys Mol Biol. 2014 Jul;115(1):3-10</Citation><ArticleIdList><ArticleId IdType="pubmed">24576798</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Prog Biophys Mol Biol. 2014 Jul;115(1):11-20</Citation><ArticleIdList><ArticleId IdType="pubmed">24674783</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Chem Biol. 2015 Feb 19;22(2):186-95</Citation><ArticleIdList><ArticleId IdType="pubmed">25699602</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2006 Dec 29;281(52):40420-8</Citation><ArticleIdList><ArticleId IdType="pubmed">17079234</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2009 Feb 6;385(5):1481-97</Citation><ArticleIdList><ArticleId IdType="pubmed">19041879</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Int J Biol Macromol. 1998 May-Jun;22(3-4):211-7</Citation><ArticleIdList><ArticleId IdType="pubmed">9650075</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2004 Jul 2;279(27):28675-80</Citation><ArticleIdList><ArticleId IdType="pubmed">15117944</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2003 Sep 16;100(19):10611-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12947045</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Curr Mol Med. 2009 Sep;9(7):887-92</Citation><ArticleIdList><ArticleId IdType="pubmed">19860667</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2008 Oct 17;283(42):28513-7</Citation><ArticleIdList><ArticleId IdType="pubmed">18713743</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Int J Biochem Cell Biol. 2012 Oct;44(10):1687-97</Citation><ArticleIdList><ArticleId IdType="pubmed">22405853</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Mol Vis. 2006 May 24;12:581-7</Citation><ArticleIdList><ArticleId IdType="pubmed">16760894</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>EMBO J. 2012 Dec 12;31(24):4587-94</Citation><ArticleIdList><ArticleId IdType="pubmed">23188086</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2016 Oct 21;291(43):22618-22629</Citation><ArticleIdList><ArticleId IdType="pubmed">27587396</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2011 Oct 21;413(2):310-20</Citation><ArticleIdList><ArticleId IdType="pubmed">21839749</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2008 Feb 15;319(5865):916-9</Citation><ArticleIdList><ArticleId IdType="pubmed">18276881</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2011 Apr 19;108(16):6409-14</Citation><ArticleIdList><ArticleId IdType="pubmed">21464278</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2012 Feb 14;51(6):1257-68</Citation><ArticleIdList><ArticleId IdType="pubmed">22264079</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nat Struct Mol Biol. 2015 Nov;22(11):898-905</Citation><ArticleIdList><ArticleId IdType="pubmed">26458046</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Cell Mol Life Sci. 2015 Feb;72(3):429-451</Citation><ArticleIdList><ArticleId IdType="pubmed">25352169</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2002 Sep 13;322(2):383-93</Citation><ArticleIdList><ArticleId IdType="pubmed">12217698</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Sci. 2010 May;19(5):1031-43</Citation><ArticleIdList><ArticleId IdType="pubmed">20440841</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20491-6</Citation><ArticleIdList><ArticleId IdType="pubmed">22143763</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS J. 2008 Mar;275(5):935-47</Citation><ArticleIdList><ArticleId IdType="pubmed">18218039</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS Lett. 2013 Apr 17;587(8):1073-80</Citation><ArticleIdList><ArticleId IdType="pubmed">23340341</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2014 May 27;111(21):7671-6</Citation><ArticleIdList><ArticleId IdType="pubmed">24817693</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2013 Oct 1;110(40):E3780-9</Citation><ArticleIdList><ArticleId IdType="pubmed">24043785</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Parkinsons Dis. 2011;1(4):359-71</Citation><ArticleIdList><ArticleId IdType="pubmed">23933657</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2006 Aug 15;45(32):9878-86</Citation><ArticleIdList><ArticleId IdType="pubmed">16893188</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Structure. 2013 Feb 5;21(2):220-8</Citation><ArticleIdList><ArticleId IdType="pubmed">23273429</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2009 May 12;48(18):3828-37</Citation><ArticleIdList><ArticleId IdType="pubmed">19323523</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2009 Sep 15;106(37):15604-9</Citation><ArticleIdList><ArticleId IdType="pubmed">19717454</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Cell Mol Life Sci. 2015 Nov;72(21):4127-37</Citation><ArticleIdList><ArticleId IdType="pubmed">26210153</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2013 May 10;288(19):13602-9</Citation><ArticleIdList><ArticleId IdType="pubmed">23532854</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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