Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
Identifieur interne : 000094 ( Istex/Corpus ); précédent : 000093; suivant : 000095Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
Auteurs : Jörg Ruppert ; John Sidney ; Esteban Celis ; Ralph T. Kubo ; Howard M. Grey ; Alessandro SetteSource :
- Cell [ 0092-8674 ] ; 1993.
English descriptors
- Teeft :
- Affinity, Amino, Amino acid, Amino acid group, Amino acid residues, Amino acid substitutions, Amino acids, Analog, Anchor positions, Anchor residues, Aromatic residues, Assay, Basic residues, Binder, Binding, Binding affinity, Binding assays, Binding capacity, Canonical, Canonical anchor residues, Canonical anchors, Cell responses, Certain residue, Conservative substitutions, Deleterious residues, Detectable binding, Detrimental effects, Extra electron density, Falk, Frequency ratios, Good agreement, Good binding, High affinity, High affinity binders, High affinity binding, Histocompatibility, Immunol, Independent experiments, Inhibitory, Inhibitory concentration, Inhibitory dose, Intermediate affinity, Intermediate binders, Large numbers, Lower affinity, Mage, Main anchor residues, Main anchors, Major histocompatibility, Model peptide, Molecule, More unfavored residues, Negative binders, Negative charges, Negative effects, Nonanchor, Nonanchor positions, Nonanchor residues, Nonbinders, Nonbinding peptides, Parham, Peptide, Peptide antigens, Peptide binding, Peptide binding groove, Peptide ligands, Peptides binding, Peptides peptides, Poor binding, Preferred residues, Protein sequences, Quantitative assay, Residue, Saper, Secondary anchor residues, Secondary anchors, Secondary effects, Secondary pockets, Self peptides, Sette, Side chains, Simple peptides, Standard peptide, Structural requirements, Substitution, Synthetic peptides, Tumor origin, Unfavored, Unfavored residue, Unfavored residues, Viral, Weak binders.
Abstract
Abstract: The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.
Url:
DOI: 10.1016/0092-8674(93)90472-3
Links to Exploration step
ISTEX:783E4B1280F9C0A42088DD16A3A9B2A6B37BA546Le document en format XML
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Grey</name><affiliation><mods:affiliation>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</mods:affiliation></affiliation></author><author><name sortKey="Sette, Alessandro" sort="Sette, Alessandro" uniqKey="Sette A" first="Alessandro" last="Sette">Alessandro Sette</name><affiliation><mods:affiliation>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Cell</title><title level="j" type="abbrev">CELL</title><idno type="ISSN">0092-8674</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993">1993</date><biblScope unit="volume">74</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="929">929</biblScope><biblScope unit="page" to="937">937</biblScope></imprint><idno type="ISSN">0092-8674</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0092-8674</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Affinity</term><term>Amino</term><term>Amino acid</term><term>Amino acid group</term><term>Amino acid residues</term><term>Amino acid substitutions</term><term>Amino acids</term><term>Analog</term><term>Anchor positions</term><term>Anchor residues</term><term>Aromatic residues</term><term>Assay</term><term>Basic residues</term><term>Binder</term><term>Binding</term><term>Binding affinity</term><term>Binding assays</term><term>Binding capacity</term><term>Canonical</term><term>Canonical anchor residues</term><term>Canonical anchors</term><term>Cell responses</term><term>Certain residue</term><term>Conservative substitutions</term><term>Deleterious residues</term><term>Detectable binding</term><term>Detrimental effects</term><term>Extra electron density</term><term>Falk</term><term>Frequency ratios</term><term>Good agreement</term><term>Good binding</term><term>High affinity</term><term>High affinity binders</term><term>High affinity binding</term><term>Histocompatibility</term><term>Immunol</term><term>Independent experiments</term><term>Inhibitory</term><term>Inhibitory concentration</term><term>Inhibitory dose</term><term>Intermediate affinity</term><term>Intermediate binders</term><term>Large numbers</term><term>Lower affinity</term><term>Mage</term><term>Main anchor residues</term><term>Main anchors</term><term>Major histocompatibility</term><term>Model peptide</term><term>Molecule</term><term>More unfavored residues</term><term>Negative binders</term><term>Negative charges</term><term>Negative effects</term><term>Nonanchor</term><term>Nonanchor positions</term><term>Nonanchor residues</term><term>Nonbinders</term><term>Nonbinding peptides</term><term>Parham</term><term>Peptide</term><term>Peptide antigens</term><term>Peptide binding</term><term>Peptide binding groove</term><term>Peptide ligands</term><term>Peptides binding</term><term>Peptides peptides</term><term>Poor binding</term><term>Preferred residues</term><term>Protein sequences</term><term>Quantitative assay</term><term>Residue</term><term>Saper</term><term>Secondary anchor residues</term><term>Secondary anchors</term><term>Secondary effects</term><term>Secondary pockets</term><term>Self peptides</term><term>Sette</term><term>Side chains</term><term>Simple peptides</term><term>Standard peptide</term><term>Structural requirements</term><term>Substitution</term><term>Synthetic peptides</term><term>Tumor origin</term><term>Unfavored</term><term>Unfavored residue</term><term>Unfavored residues</term><term>Viral</term><term>Weak binders</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>peptide</json:string><json:string>binder</json:string><json:string>binding capacity</json:string><json:string>nonbinders</json:string><json:string>anchor residues</json:string><json:string>canonical</json:string><json:string>nonanchor</json:string><json:string>unfavored</json:string><json:string>amino</json:string><json:string>saper</json:string><json:string>mage</json:string><json:string>analog</json:string><json:string>histocompatibility</json:string><json:string>falk</json:string><json:string>sette</json:string><json:string>immunol</json:string><json:string>viral</json:string><json:string>parham</json:string><json:string>nonanchor positions</json:string><json:string>amino acids</json:string><json:string>residue</json:string><json:string>anchor positions</json:string><json:string>high affinity binding</json:string><json:string>main anchors</json:string><json:string>poor binding</json:string><json:string>good agreement</json:string><json:string>intermediate binders</json:string><json:string>assay</json:string><json:string>substitution</json:string><json:string>inhibitory concentration</json:string><json:string>major histocompatibility</json:string><json:string>model peptide</json:string><json:string>peptide binding</json:string><json:string>canonical anchors</json:string><json:string>aromatic residues</json:string><json:string>peptide ligands</json:string><json:string>structural requirements</json:string><json:string>binding affinity</json:string><json:string>tumor origin</json:string><json:string>main anchor residues</json:string><json:string>protein sequences</json:string><json:string>amino acid residues</json:string><json:string>secondary anchors</json:string><json:string>unfavored residues</json:string><json:string>binding assays</json:string><json:string>conservative substitutions</json:string><json:string>secondary anchor residues</json:string><json:string>negative effects</json:string><json:string>high affinity binders</json:string><json:string>weak binders</json:string><json:string>detectable binding</json:string><json:string>peptide antigens</json:string><json:string>good binding</json:string><json:string>deleterious residues</json:string><json:string>inhibitory dose</json:string><json:string>affinity</json:string><json:string>molecule</json:string><json:string>binding</json:string><json:string>amino acid</json:string><json:string>quantitative assay</json:string><json:string>nonbinding peptides</json:string><json:string>amino acid group</json:string><json:string>frequency ratios</json:string><json:string>detrimental effects</json:string><json:string>standard peptide</json:string><json:string>secondary pockets</json:string><json:string>amino acid substitutions</json:string><json:string>certain residue</json:string><json:string>peptides peptides</json:string><json:string>preferred residues</json:string><json:string>self peptides</json:string><json:string>synthetic peptides</json:string><json:string>basic residues</json:string><json:string>independent experiments</json:string><json:string>peptide binding groove</json:string><json:string>negative charges</json:string><json:string>simple peptides</json:string><json:string>nonanchor residues</json:string><json:string>unfavored residue</json:string><json:string>canonical anchor residues</json:string><json:string>high affinity</json:string><json:string>more unfavored residues</json:string><json:string>negative binders</json:string><json:string>intermediate affinity</json:string><json:string>lower affinity</json:string><json:string>large numbers</json:string><json:string>cell responses</json:string><json:string>side chains</json:string><json:string>secondary effects</json:string><json:string>peptides binding</json:string><json:string>extra electron density</json:string><json:string>inhibitory</json:string></teeft></keywords><author><json:item><name>Jörg Ruppert</name><affiliations><json:string>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</json:string></affiliations></json:item><json:item><name>John Sidney</name><affiliations><json:string>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</json:string></affiliations></json:item><json:item><name>Esteban Celis</name><affiliations><json:string>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</json:string></affiliations></json:item><json:item><name>Ralph T. Kubo</name><affiliations><json:string>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</json:string></affiliations></json:item><json:item><name>Howard M. Grey</name><affiliations><json:string>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</json:string></affiliations></json:item><json:item><name>Alessandro Sette</name><affiliations><json:string>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</json:string></affiliations></json:item></author><arkIstex>ark:/67375/6H6-1K9SH7B6-V</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.</abstract><qualityIndicators><score>8.824</score><pdfWordCount>6087</pdfWordCount><pdfCharCount>37626</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>9</pdfPageCount><pdfPageSize>598 x 792 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>152</abstractWordCount><abstractCharCount>1103</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules</title><pmid><json:string>8104103</json:string></pmid><pii><json:string>0092-8674(93)90472-3</json:string></pii><genre><json:string>research-article</json:string></genre><serie><title>Proc. Natl. Acad. Sci. USA</title><language><json:string>unknown</json:string></language><volume>86</volume><pages><first>4649</first><last>4653</last></pages></serie><host><title>Cell</title><language><json:string>unknown</json:string></language><publicationDate>1993</publicationDate><issn><json:string>0092-8674</json:string></issn><pii><json:string>S0092-8674(00)X0378-9</json:string></pii><volume>74</volume><issue>5</issue><pages><first>929</first><last>937</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1993</json:string><json:string>9 or 2/10</json:string></date><geogName></geogName><orgName><json:string>Chiron Corporation</json:string><json:string>Cytel Corporation</json:string><json:string>Bachem</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>Esteban Celis</json:string><json:string>V. H. Engelhard</json:string><json:string>Joyce Joseph</json:string><json:string>In</json:string><json:string>Scott Southwood</json:string><json:string>Ralph T. Kubo</json:string><json:string>Howard M. Grey</json:string></persName><placeName><json:string>Capacity</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Parham, 1992</json:string><json:string>Sette et al., 1993</json:string><json:string>Latron et al., 1992</json:string><json:string>Chen and Parham, 1989</json:string><json:string>Guo et al., 1992</json:string><json:string>Boehncke et al. (1993)</json:string><json:string>Corr et al., 1992</json:string><json:string>Bjorkman and Parham, 1990</json:string><json:string>Rdtzschke and Falk, 1991</json:string><json:string>Hunt et al., 1992</json:string><json:string>Buus et al., 1987</json:string><json:string>Garret et al., 1989</json:string><json:string>Parker et al., 1992</json:string><json:string>Jardetzky et al., 1991</json:string><json:string>Matsumura et al., 1992</json:string><json:string>Saper et al., 1991</json:string><json:string>Townsend and Bodmer, 1989</json:string><json:string>Schumacher et al., 1991</json:string><json:string>Travers and Thorpe, 1992</json:string><json:string>Schaeffer et al.</json:string><json:string>Falk et al., 1991</json:string><json:string>Fremont et al., 1992</json:string><json:string>Jameson and Bevan, 1992</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-1K9SH7B6-V</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - 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The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.</p></abstract></profileDesc><revisionDesc><change when="1993-06-22">Modified</change><change when="1993">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-1K9SH7B6-V/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>CELL</jid><aid>93904723</aid><ce:pii>0092-8674(93)90472-3</ce:pii><ce:doi>10.1016/0092-8674(93)90472-3</ce:doi><ce:copyright type="unknown" year="1993"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Article</ce:textfn></ce:dochead><ce:title>Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules</ce:title><ce:author-group><ce:author><ce:given-name>Jörg</ce:given-name><ce:surname>Ruppert</ce:surname></ce:author><ce:author><ce:given-name>John</ce:given-name><ce:surname>Sidney</ce:surname></ce:author><ce:author><ce:given-name>Esteban</ce:given-name><ce:surname>Celis</ce:surname></ce:author><ce:author><ce:given-name>Ralph T.</ce:given-name><ce:surname>Kubo</ce:surname></ce:author><ce:author><ce:given-name>Howard M.</ce:given-name><ce:surname>Grey</ce:surname></ce:author><ce:author><ce:given-name>Alessandro</ce:given-name><ce:surname>Sette</ce:surname></ce:author><ce:affiliation><ce:textfn>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="26" month="5" year="1993"></ce:date-received><ce:date-revised day="22" month="6" year="1993"></ce:date-revised><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules</title></titleInfo><name type="personal"><namePart type="given">Jörg</namePart><namePart type="family">Ruppert</namePart><affiliation>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">John</namePart><namePart type="family">Sidney</namePart><affiliation>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Esteban</namePart><namePart type="family">Celis</namePart><affiliation>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ralph T.</namePart><namePart type="family">Kubo</namePart><affiliation>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Howard M.</namePart><namePart type="family">Grey</namePart><affiliation>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Alessandro</namePart><namePart type="family">Sette</namePart><affiliation>Cytel Corporation 3525 John Hopkins Court San Diego, California 92121 USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1993</dateIssued><dateModified encoding="w3cdtf">1993-06-22</dateModified><copyrightDate encoding="w3cdtf">1993</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs.</abstract><note type="content">Section title: Article</note><relatedItem type="host"><titleInfo><title>Cell</title></titleInfo><titleInfo type="abbreviated"><title>CELL</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1993</dateIssued></originInfo><identifier type="ISSN">0092-8674</identifier><identifier type="PII">S0092-8674(00)X0378-9</identifier><part><date>1993</date><detail type="volume"><number>74</number><caption>vol.</caption></detail><detail type="issue"><number>5</number><caption>no.</caption></detail><extent unit="issue-pages"><start>769</start><end>946</end></extent><extent unit="pages"><start>929</start><end>937</end></extent></part></relatedItem><identifier type="istex">783E4B1280F9C0A42088DD16A3A9B2A6B37BA546</identifier><identifier type="ark">ark:/67375/6H6-1K9SH7B6-V</identifier><identifier type="DOI">10.1016/0092-8674(93)90472-3</identifier><identifier type="PII">0092-8674(93)90472-3</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-1K9SH7B6-V/record.json</uri></json:item></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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