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<dc:creator>Ganfornina Álvarez, María Dolores</dc:creator>
<dc:creator>Sánchez Romero, Diego</dc:creator>
<dc:creator>Greene, Lesley H.</dc:creator>
<dc:creator>Flower, Darren R.</dc:creator>
<dc:date>2005</dc:date>
<dc:description>Producción Científica</dc:description>
<dc:description>Lipocalins 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.</dc:description>
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<dc:identifier>http://uvadoc.uva.es/handle/10324/6262</dc:identifier>
<dc:language>eng</dc:language>
<dc:publisher>Landes Bioscience</dc:publisher>
<dc:publisher>Eurekah.com</dc:publisher>
<dc:subject>Lipocainas</dc:subject>
<dc:title>The Lipocalin Protein Family: Protein Sequence, Structure and Relationship to the Calycin Superfamily</dc:title>
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