dc.creator | Cambiazo Ayala, Verónica | |
dc.creator | González, Mauricio | |
dc.creator | Isamit, Cristián | |
dc.creator | Maccioni Baraona, Ricardo | |
dc.date.accessioned | 2018-12-20T14:10:42Z | |
dc.date.available | 2018-12-20T14:10:42Z | |
dc.date.created | 2018-12-20T14:10:42Z | |
dc.date.issued | 1999 | |
dc.identifier | FEBS Letters, Volumen 457, Issue 3, 2018, Pages 343-347 | |
dc.identifier | 00145793 | |
dc.identifier | 10.1016/S0014-5793(99)01070-4 | |
dc.identifier | http://repositorio.uchile.cl/handle/2250/154396 | |
dc.description.abstract | Through major research advances in the study of cytoskeletal organization, an integrated view of the complexity of this system has emerged. Recent findings on the microtubule-interacting protein Mip-90, which associates with microtubules and actin filaments in different cell domains, have shed light on its roles in cytoskeletal regulation. In order to study structural features of Mip-90, we sequenced several peptide fragments. A comparative sequence analysis revealed a high degree of similarity between the primary structure of this protein and the human heat shock protein of 90 kDa (hsp-90). Taken together, the present studies indicate the identity between Mip-90 and the the β-isoform of hsp-90 (hsp-90β). Western blot assays with an anti-hsp-90 monoclonal antibody showed cross-reactivity of hsp-90 and Mip-90 affinity purified from HeLa cells. Furthermore, the observed structural identity of Mip-90 with the hsp-90β was sustained by immunoblot assays using monoclonal antibodies that spec | |
dc.language | en | |
dc.rights | http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ | |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 Chile | |
dc.source | FEBS Letters | |
dc.subject | Common epitope | |
dc.subject | Functional feature | |
dc.subject | Heat shock protein-90 | |
dc.subject | Microtubule interacting protein-90 | |
dc.subject | Protein domain | |
dc.subject | Sequence homology | |
dc.title | The β-isoform of heat shock protein hsp-90 is structurally related with human microtubule-interacting protein Mip-90 | |
dc.type | Artículos de revistas | |