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.
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Journal ArticleDOI
Subnuclear Localization of C/EBPβ Is Regulated by Growth Hormone and Dependent on MAPK
TL;DR: Nuclear redistribution introduces a new level of transcriptional regulation in GH action, since GH-mediated phosphorylation and nuclear redistribution of C/EBPβ may be coordinated to achieve spatial-temporal control of gene expression.
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Biological Actions of the Hsp90-binding Immunophilins FKBP51 and FKBP52
Nadia R Zgajnar,Sonia A. De Leo,Cecilia M Lotufo,Alejandra G. Erlejman,Graciela Piwien-Pilipuk,Mario D. Galigniana,Mario D. Galigniana +6 more
TL;DR: The biology of these events and some mechanistic aspects are discussed, which regulate a variety of biological processes such as steroid receptor action, transcriptional activity, protein conformation, protein trafficking, cell differentiation, apoptosis, cancer progression, telomerase activity, cytoskeleton architecture, etc.
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Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex.
Mario D. Galigniana,Mario D. Galigniana,Yoshihiro Morishima,Philippe Gallay,William B. Pratt +4 more
TL;DR: It is shown that cyclophilin A exists in native heterocomplexes containing cytoplasmic dynein that can be formed in cell-free systems and suggested that CyP-A may perform a general function related to the binding of cargo for retrograde movement along microtubules.
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Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation
Mario D. Galigniana,Jennifer M. Harrell,Paul R. Housley,Cam Patterson,Stephen K. Fisher,William B. Pratt +5 more
TL;DR: It is shown that GFP-GR expressed in hormone-free neurons is localized in both cytoplasm and neurites, and upon treatment with dexamethasone (DEX), it moves to the nucleus, the first evidence for a linkage between receptor trafficking along neurites and receptor degradation by the proteasome.
Journal ArticleDOI
hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1.
Kimon C. Kanelakis,Patrick J. Murphy,Mario D. Galigniana,Yoshihiro Morishima,Shinichi Takayama,John C. Reed,David O. Toft,William B. Pratt +7 more
TL;DR: It is shown that immunodepletion of Hip from reticulocyte lysate or addition of high levels of Hip to the purified five-protein system does not affect GR and it is concluded that Hip is not a component of the assembly machinery but that it could play a regulatory role in opposition to BAG-1.