M
Mario D. Galigniana
Researcher at Instituto de Biología y Medicina Experimental
Publications - 105
Citations - 5696
Mario D. Galigniana is an academic researcher from Instituto de Biología y Medicina Experimental. The author has contributed to research in topics: Hsp90 & Immunophilins. The author has an hindex of 40, co-authored 99 publications receiving 5257 citations. Previous affiliations of Mario D. Galigniana include Fundación Instituto Leloir & University of Michigan.
Papers
More filters
Journal ArticleDOI
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement.
TL;DR: Evidence that dynamic assembly of heterocomplexes with hsp90 is required for movement to these foci and for the dynamic exchange of transcription factors between chromatin and the nucleoplasm is reviewed.
Journal ArticleDOI
Protein Phosphatase 5 Is a Major Component of Glucocorticoid Receptor·hsp90 Complexes with Properties of an FK506-binding Immunophilin
Adam M. Silverstein,Mario D. Galigniana,Mei-Shya Chen,Janet K. Owens-Grillo,Michael Chinkers,William B. Pratt +5 more
TL;DR: It is proposed that PP5 possesses properties of an immunophilin with low affinity FK506 binding activity and that it determines a major portion of the native GR heterocomplexes in L cell cytosol.
Journal ArticleDOI
Role of molecular chaperones in steroid receptor action.
TL;DR: By forming heterocomplexes with hsp90, the chaperone machinery stabilizes the receptor to degradation by the ubiquitin-proteasome pathway of proteolysis and interacts in very dynamic fashion with the liganded, transformed receptor.
Journal ArticleDOI
Evidence That the Peptidylprolyl Isomerase Domain of the hsp90-binding Immunophilin FKBP52 Is Involved in Both Dynein Interaction and Glucocorticoid Receptor Movement to the Nucleus *
TL;DR: It is shown that cotransfection of 3T3 cells with the FKBP52 PPIase domain and a green fluorescent protein (GFP) glucocorticoid receptor (GR) chimera inhibits dexamethasone-dependent movement of the GFP-GR from the cytoplasm to the nucleus.
Journal ArticleDOI
FKBP51 and FKBP52 in Signaling and Disease
TL;DR: This review summarizes the current understanding of FKBP51 and FK BP52 interactions within the receptor-chaperone complex, their contributions to health and disease, and their potential as therapeutic targets for the treatment of these diseases.