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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Antigenic role of single residues within the main immunogenic region of the nicotinic acetylcholine receptor.</title><author><name sortKey="Papadouli, I" sort="Papadouli, I" uniqKey="Papadouli I" first="I" last="Papadouli">I. Papadouli</name></author><author><name sortKey="Potamianos, S" sort="Potamianos, S" uniqKey="Potamianos S" first="S" last="Potamianos">S. Potamianos</name></author><author><name sortKey="Hadjidakis, I" sort="Hadjidakis, I" uniqKey="Hadjidakis I" first="I" last="Hadjidakis">I. Hadjidakis</name></author><author><name sortKey="Bairaktari, E" sort="Bairaktari, E" uniqKey="Bairaktari E" first="E" last="Bairaktari">E. Bairaktari</name></author><author><name sortKey="Tsikaris, V" sort="Tsikaris, V" uniqKey="Tsikaris V" first="V" last="Tsikaris">V. Tsikaris</name></author><author><name sortKey="Sakarellos, C" sort="Sakarellos, C" uniqKey="Sakarellos C" first="C" last="Sakarellos">C. Sakarellos</name></author><author><name sortKey="Cung, M T" sort="Cung, M T" uniqKey="Cung M" first="M T" last="Cung">M T Cung</name></author><author><name sortKey="Marraud, M" sort="Marraud, M" uniqKey="Marraud M" first="M" last="Marraud">M. Marraud</name></author><author><name sortKey="Tzartos, S J" sort="Tzartos, S J" uniqKey="Tzartos S" first="S J" last="Tzartos">S J Tzartos</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">1695844</idno><idno type="pmc">1131559</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1131559</idno><idno type="RBID">PMC:1131559</idno><date when="1990">1990</date><idno type="wicri:Area/Pmc/Corpus">000048</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000048</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Antigenic role of single residues within the main immunogenic region of the nicotinic acetylcholine receptor.</title><author><name sortKey="Papadouli, I" sort="Papadouli, I" uniqKey="Papadouli I" first="I" last="Papadouli">I. Papadouli</name></author><author><name sortKey="Potamianos, S" sort="Potamianos, S" uniqKey="Potamianos S" first="S" last="Potamianos">S. Potamianos</name></author><author><name sortKey="Hadjidakis, I" sort="Hadjidakis, I" uniqKey="Hadjidakis I" first="I" last="Hadjidakis">I. Hadjidakis</name></author><author><name sortKey="Bairaktari, E" sort="Bairaktari, E" uniqKey="Bairaktari E" first="E" last="Bairaktari">E. Bairaktari</name></author><author><name sortKey="Tsikaris, V" sort="Tsikaris, V" uniqKey="Tsikaris V" first="V" last="Tsikaris">V. Tsikaris</name></author><author><name sortKey="Sakarellos, C" sort="Sakarellos, C" uniqKey="Sakarellos C" first="C" last="Sakarellos">C. Sakarellos</name></author><author><name sortKey="Cung, M T" sort="Cung, M T" uniqKey="Cung M" first="M T" last="Cung">M T Cung</name></author><author><name sortKey="Marraud, M" sort="Marraud, M" uniqKey="Marraud M" first="M" last="Marraud">M. Marraud</name></author><author><name sortKey="Tzartos, S J" sort="Tzartos, S J" uniqKey="Tzartos S" first="S J" last="Tzartos">S J Tzartos</name></author></analytic><series><title level="j">Biochemical Journal</title><idno type="ISSN">0264-6021</idno><idno type="eISSN">1470-8728</idno><imprint><date when="1990">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The target of most of the autoantibodies against the acetylcholine receptor (AChR) in myasthenic sera is the main immunogenic region (MIR) on the extracellular side of the AChR alpha-subunit. Binding of anti-MIR monoclonal antibodies (mAbs) has been recently localized between residues alpha 67 and alpha 76 of Torpedo californica electric organ (WNPADYGGIK) and human muscle (WNPDDYGGVK) AChR. In order to evaluate the contribution of each residue to the antigenicity of the MIR, we synthesized peptides corresponding to residues alpha 67-76 from Torpedo and human AChRs, together with 13 peptide analogues. Nine of these analogues had one residue of the Torpedo decapeptide replaced by L-alanine, three had a structure which was intermediate between those of the Torpedo and human alpha 67-76 decapeptides, and one had D-alanine in position 73. Binding studies employing six anti-MIR mAbs and all 15 peptides revealed that some residues (Asn68 and Asp71) are indispensable for binding by all mAbs tested, whereas others are important only for binding by some mAbs. Antibody binding was mainly restricted to residues alpha 68-74, the most critical sequence being alpha 68-71. Fish electric organ and human MIR form two distinct groups of strongly overlapping epitopes. Some peptide analogues enhanced mAb binding compared with Torpedo and human peptides, suggesting that the construction of a very antigenic MIR is feasible.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Biochem J</journal-id><journal-title>Biochemical Journal</journal-title><issn pub-type="ppub">0264-6021</issn><issn pub-type="epub">1470-8728</issn></journal-meta><article-meta><article-id pub-id-type="pmid">1695844</article-id><article-id pub-id-type="pmc">1131559</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group></article-categories><title-group><article-title>Antigenic role of single residues within the main immunogenic region of the nicotinic acetylcholine receptor.</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Papadouli</surname><given-names>I</given-names></name></contrib><contrib contrib-type="author"><name><surname>Potamianos</surname><given-names>S</given-names></name></contrib><contrib contrib-type="author"><name><surname>Hadjidakis</surname><given-names>I</given-names></name></contrib><contrib contrib-type="author"><name><surname>Bairaktari</surname><given-names>E</given-names></name></contrib><contrib contrib-type="author"><name><surname>Tsikaris</surname><given-names>V</given-names></name></contrib><contrib contrib-type="author"><name><surname>Sakarellos</surname><given-names>C</given-names></name></contrib><contrib contrib-type="author"><name><surname>Cung</surname><given-names>M T</given-names></name></contrib><contrib contrib-type="author"><name><surname>Marraud</surname><given-names>M</given-names></name></contrib><contrib contrib-type="author"><name><surname>Tzartos</surname><given-names>S J</given-names></name></contrib></contrib-group><aff>Hellenic Pasteur Institute, Athens, Greece.</aff><pub-date pub-type="ppub"><day>1</day><month>7</month><year>1990</year></pub-date><volume>269</volume><issue>1</issue><fpage>239</fpage><lpage>245</lpage><abstract><p>The target of most of the autoantibodies against the acetylcholine receptor (AChR) in myasthenic sera is the main immunogenic region (MIR) on the extracellular side of the AChR alpha-subunit. Binding of anti-MIR monoclonal antibodies (mAbs) has been recently localized between residues alpha 67 and alpha 76 of Torpedo californica electric organ (WNPADYGGIK) and human muscle (WNPDDYGGVK) AChR. In order to evaluate the contribution of each residue to the antigenicity of the MIR, we synthesized peptides corresponding to residues alpha 67-76 from Torpedo and human AChRs, together with 13 peptide analogues. Nine of these analogues had one residue of the Torpedo decapeptide replaced by L-alanine, three had a structure which was intermediate between those of the Torpedo and human alpha 67-76 decapeptides, and one had D-alanine in position 73. Binding studies employing six anti-MIR mAbs and all 15 peptides revealed that some residues (Asn68 and Asp71) are indispensable for binding by all mAbs tested, whereas others are important only for binding by some mAbs. Antibody binding was mainly restricted to residues alpha 68-74, the most critical sequence being alpha 68-71. Fish electric organ and human MIR form two distinct groups of strongly overlapping epitopes. Some peptide analogues enhanced mAb binding compared with Torpedo and human peptides, suggesting that the construction of a very antigenic MIR is feasible.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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