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dc.contributor.authorGanfornina Álvarez, María Dolores 
dc.contributor.authorSánchez Romero, Diego 
dc.contributor.authorGreene, Lesley H.
dc.contributor.authorFlower, Darren R.
dc.date.accessioned2014-09-24T17:17:45Z
dc.date.available2014-09-24T17:17:45Z
dc.date.issued2005
dc.identifier.citationAkerstrom, Bo; Borregaard, Niels; Flower, Darren R.; Salier, Jean-Phillippe (coords.). Molecular Biology Intelligence Unit: Lipocalins. Georgetown, Texas, 2005, p. 17-27es
dc.identifier.urihttp://uvadoc.uva.es/handle/10324/6262
dc.descriptionProducción Científicaes
dc.description.abstractLipocalins are remarkable in their diversity, as manifest at the levels of protein sequence and protein function. At the level of 3-dimensional structure, however, they are very similar. The lipocalins are also part of a larger protein superfamily: the calycins, which also includes the fatty acid binding proteins, adivins, a group of metalloproteinase inhibitors, and triabin. The superfamily is characterised by a similar structure (a repeated +1 topology B-barrel) and by the conservation of a remarkable structural signature. In this review, both of these aspects are explored.es
dc.format.mimetypeapplication/pdfes
dc.language.isoenges
dc.publisherLandes Biosciencees
dc.publisherEurekah.comes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectLipocainases
dc.titleThe Lipocalin Protein Family: Protein Sequence, Structure and Relationship to the Calycin Superfamilyes
dc.typeinfo:eu-repo/semantics/bookPartes
dc.identifier.publicationfirstpage17es
dc.identifier.publicationlastpage27es
dc.identifier.publicationtitleMolecular Biology Intelligence Unites
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International


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