dc.creator | Scheps, Karen | |
dc.creator | Hasenahuer, Marcia Anahí | |
dc.creator | Parisi, Gustavo Daniel | |
dc.creator | Fornasari, Maria Silvina | |
dc.creator | Pennesi, Sandra P. | |
dc.creator | Erramouspe, Beatriz | |
dc.creator | Basack, Felisa N. | |
dc.creator | Veber, Ernesto S. | |
dc.creator | Aversa, Luis | |
dc.creator | Elena, Graciela | |
dc.creator | Varela, Viviana | |
dc.date.accessioned | 2020-05-15T19:22:00Z | |
dc.date.accessioned | 2022-10-15T01:09:09Z | |
dc.date.available | 2020-05-15T19:22:00Z | |
dc.date.available | 2022-10-15T01:09:09Z | |
dc.date.created | 2020-05-15T19:22:00Z | |
dc.date.issued | 2014-10 | |
dc.identifier | Scheps, Karen; Hasenahuer, Marcia Anahí; Parisi, Gustavo Daniel; Fornasari, Maria Silvina; Pennesi, Sandra P.; et al.; Hb Wilde and Hb Patagonia: two novel elongated beta-globin variants causing dominant beta-thalassemia; Wiley; European Journal Of Haematology; 94; 10-2014; 498-503 | |
dc.identifier | 1600-0609 | |
dc.identifier | http://hdl.handle.net/11336/105265 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4328388 | |
dc.description.abstract | We describe here the molecular and hematological characteristics of novel frameshift mutations in exon 2 of the HBB gene (in heterozygous state) found in two Argentinean pediatric patients with dominant b-thalassemia-like features. In Hb Wilde, HBB:c.270_273delTGAG(p.Glu90Cysfs*67), we detected the deletion of the third base of the codon 89 (T) and the codon 90 (GAG), whereas in Hb Patagonia, HBB: c.296_297dupGT(p.Asp99Trpfs*59), the frameshift mutation was due to a duplication of a ‘GT’ dinucleotide after the second base of codon 98 (GTG). The Hb Patagonia and Hb Wilde mutations would result in elongated b-globin chains with modified C-terminal sequences and a total of 155 and 157 amino acids residues, respectively. Based on bioinformatics and structural analysis, as well as protein modeling, we predict that the elongated b-globins would affect the formation of the ab dimers and their stability, which would further support the mechanism for the observed clinical features in both patients. | |
dc.language | eng | |
dc.publisher | Wiley | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/ejh.12456/abstract | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/ejh.12456 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | elongated beta-globin | |
dc.subject | protein structure | |
dc.subject | dominant beta-thalassemia | |
dc.subject | frameshift mutations | |
dc.title | Hb Wilde and Hb Patagonia: two novel elongated beta-globin variants causing dominant beta-thalassemia | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |