Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody
The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody''s contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design...
| Autores: | , , , , , , , , , , , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2020 |
| País: | España |
| Institución: | Universidad de Zaragoza |
| Repositorio: | Zaguán. Repositorio Digital de la Universidad de Zaragoza |
| OAI Identifier: | oai:zaguan.unizar.es:108329 |
| Acceso en línea: | http://zaguan.unizar.es/record/108329 |
| Access Level: | acceso abierto |
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Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibodyMacías-León, J.Bermejo, I.A.Asín, A.García-García, A.Compañón, I.Jiménez-Moreno, E.Coelho, H.Mangini, V.Albuquerque, I.S.Marcelo, F.Asensio, J.L.Bernardes, G.J.L.Joshi, H.J.Fiammengo, R.Blixt, O.Hurtado-Guerrero, R.Corzana, F.The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody''s contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design of peptide-mimetics for developing efficient anti-cancer vaccines and diagnostic tools.2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttp://zaguan.unizar.es/record/108329reponame:Zaguán. Repositorio Digital de la Universidad de Zaragozainstname:Universidad de ZaragozaInglésinfo:eu-repo/grantAgreement/ES/AEI/BFU2016-75633-Pinfo:eu-repo/grantAgreement/ES/AEI/CTQ2013-44367-C2-2-Pinfo:eu-repo/grantAgreement/ES/AEI/PID2019-105451GB-I00info:eu-repo/grantAgreement/ES/AEI/PID2019-107476GB-I00info:eu-repo/grantAgreement/ES/AEI/RTI-2018-099592-B-C21info:eu-repo/semantics/openAccessoai:zaguan.unizar.es:1083292026-05-29T13:59:51Z |
| dc.title.none.fl_str_mv |
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody |
| title |
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody |
| spellingShingle |
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody Macías-León, J. |
| title_short |
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody |
| title_full |
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody |
| title_fullStr |
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody |
| title_full_unstemmed |
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody |
| title_sort |
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody |
| dc.creator.none.fl_str_mv |
Macías-León, J. Bermejo, I.A. Asín, A. García-García, A. Compañón, I. Jiménez-Moreno, E. Coelho, H. Mangini, V. Albuquerque, I.S. Marcelo, F. Asensio, J.L. Bernardes, G.J.L. Joshi, H.J. Fiammengo, R. Blixt, O. Hurtado-Guerrero, R. Corzana, F. |
| author |
Macías-León, J. |
| author_facet |
Macías-León, J. Bermejo, I.A. Asín, A. García-García, A. Compañón, I. Jiménez-Moreno, E. Coelho, H. Mangini, V. Albuquerque, I.S. Marcelo, F. Asensio, J.L. Bernardes, G.J.L. Joshi, H.J. Fiammengo, R. Blixt, O. Hurtado-Guerrero, R. Corzana, F. |
| author_role |
author |
| author2 |
Bermejo, I.A. Asín, A. García-García, A. Compañón, I. Jiménez-Moreno, E. Coelho, H. Mangini, V. Albuquerque, I.S. Marcelo, F. Asensio, J.L. Bernardes, G.J.L. Joshi, H.J. Fiammengo, R. Blixt, O. Hurtado-Guerrero, R. Corzana, F. |
| author2_role |
author author author author author author author author author author author author author author author author |
| description |
The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody''s contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design of peptide-mimetics for developing efficient anti-cancer vaccines and diagnostic tools. |
| publishDate |
2020 |
| dc.date.none.fl_str_mv |
2020 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/acceptedVersion |
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article |
| status_str |
acceptedVersion |
| dc.identifier.none.fl_str_mv |
http://zaguan.unizar.es/record/108329 |
| url |
http://zaguan.unizar.es/record/108329 |
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Inglés |
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Inglés |
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info:eu-repo/grantAgreement/ES/AEI/BFU2016-75633-P info:eu-repo/grantAgreement/ES/AEI/CTQ2013-44367-C2-2-P info:eu-repo/grantAgreement/ES/AEI/PID2019-105451GB-I00 info:eu-repo/grantAgreement/ES/AEI/PID2019-107476GB-I00 info:eu-repo/grantAgreement/ES/AEI/RTI-2018-099592-B-C21 |
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info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
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application/pdf |
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reponame:Zaguán. Repositorio Digital de la Universidad de Zaragoza instname:Universidad de Zaragoza |
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Universidad de Zaragoza |
| reponame_str |
Zaguán. Repositorio Digital de la Universidad de Zaragoza |
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Zaguán. Repositorio Digital de la Universidad de Zaragoza |
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1869407767781965824 |
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15,300719 |