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Conformational control of integrin subtype selectivity in isoDGR peptide motifs: A biological switch
dc.contributor.author | Frank, A.O. |
dc.contributor.author | Otto, E. |
dc.contributor.author | Mas Moruno, Carlos |
dc.contributor.author | Schiller, H. |
dc.contributor.author | Marinelli, L. |
dc.contributor.author | Cosconati, S. |
dc.contributor.author | Bochen, A. |
dc.contributor.author | Vossmeyer, D. |
dc.contributor.author | Zahn, G. |
dc.contributor.author | Stragies, R. |
dc.contributor.author | Novellino, E. |
dc.contributor.author | Kessler, H. |
dc.contributor.other | Universitat Politècnica de Catalunya. Departament de Ciència dels Materials i Enginyeria Metal·lúrgica |
dc.date.accessioned | 2014-05-05T07:54:34Z |
dc.date.created | 2010 |
dc.date.issued | 2010 |
dc.identifier.citation | Frank, A.O. [et al.]. Conformational control of integrin subtype selectivity in isoDGR peptide motifs: A biological switch. "Angewandte chemie. International edition", 2010, vol. 49, núm. 48, p. 9278-9281. |
dc.identifier.issn | 1433-7851 |
dc.identifier.uri | http://hdl.handle.net/2117/22807 |
dc.description.abstract | Thumbnail image of graphical abstract The rearrangement of asparagine to isoaspartate (isoD) is responsible for the deactivation of many functional proteins. However, the isoDGR motif, which is optimally presented as a conformationally controlled cyclic pentapeptide, binds selectively to a5ß1 integrin (see the docking model) with an affinity comparable to that of the peptidic antitumor agent Cilengitide |
dc.format.extent | 4 p. |
dc.language.iso | eng |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Spain |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/es/ |
dc.subject | Àrees temàtiques de la UPC::Enginyeria dels materials |
dc.subject.lcsh | Peptides |
dc.subject.other | cyclic pentapeptides |
dc.subject.other | integrin ligands |
dc.subject.other | isoDGR sequence |
dc.subject.other | NMR spectroscopy |
dc.subject.other | peptides |
dc.title | Conformational control of integrin subtype selectivity in isoDGR peptide motifs: A biological switch |
dc.type | Article |
dc.subject.lemac | Pèptids |
dc.identifier.doi | 10.1002/anie.201004363 |
dc.description.peerreviewed | Peer Reviewed |
dc.relation.publisherversion | http://onlinelibrary.wiley.com/doi/10.1002/anie.201004363/abstract |
dc.rights.access | Restricted access - publisher's policy |
local.identifier.drac | 13620329 |
dc.description.version | Postprint (published version) |
dc.date.lift | 10000-01-01 |
local.citation.author | Frank, A.O.; Otto, E.; Mas-Moruno, C.; Schiller, H.; Marinelli, L.; Cosconati, S.; Bochen, A.; Vossmeyer, D.; Zahn, G.; Stragies, R.; Novellino, E.; Kessler, H. |
local.citation.publicationName | Angewandte chemie. International edition |
local.citation.volume | 49 |
local.citation.number | 48 |
local.citation.startingPage | 9278 |
local.citation.endingPage | 9281 |
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