dc.creatorCambiazo Ayala, Verónica
dc.creatorGonzález, Mauricio
dc.creatorIsamit, Cristián
dc.creatorMaccioni Baraona, Ricardo
dc.date.accessioned2018-12-20T14:10:42Z
dc.date.available2018-12-20T14:10:42Z
dc.date.created2018-12-20T14:10:42Z
dc.date.issued1999
dc.identifierFEBS Letters, Volumen 457, Issue 3, 2018, Pages 343-347
dc.identifier00145793
dc.identifier10.1016/S0014-5793(99)01070-4
dc.identifierhttp://repositorio.uchile.cl/handle/2250/154396
dc.description.abstractThrough 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.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceFEBS Letters
dc.subjectCommon epitope
dc.subjectFunctional feature
dc.subjectHeat shock protein-90
dc.subjectMicrotubule interacting protein-90
dc.subjectProtein domain
dc.subjectSequence homology
dc.titleThe β-isoform of heat shock protein hsp-90 is structurally related with human microtubule-interacting protein Mip-90
dc.typeArtículos de revistas


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