2022 - Research.com Biology and Biochemistry in Argentina Leader Award
2010 - Fellow of John Simon Guggenheim Memorial Foundation
His primary scientific interests are in Cell biology, Glucocorticoid receptor, Hsp90, FKBP52 and Cytoplasm. His work on Dynein and Nuclear pore as part of general Cell biology research is often related to Immunophilins, thus linking different fields of science. His work deals with themes such as Heat shock protein, Molecular biology and Nitric oxide, which intersect with Glucocorticoid receptor.
His biological study spans a wide range of topics, including Plasma protein binding and Chaperone. FKBP52 is the subject of his research, which falls under Biochemistry. His Cytoplasm research is multidisciplinary, relying on both Cytoskeleton and Geldanamycin.
His primary areas of study are Cell biology, Hsp90, Immunophilins, Receptor and Glucocorticoid receptor. His Cell biology research is multidisciplinary, incorporating perspectives in Tetratricopeptide, Transcription factor and Heat shock protein. His Hsp90 study necessitates a more in-depth grasp of Biochemistry.
The Receptor study combines topics in areas such as Nuclear receptor and Endocrinology. His Glucocorticoid receptor study combines topics from a wide range of disciplines, such as Molecular biology and Western blot. His FKBP52 research integrates issues from Transport protein, FKBP, Nuclear pore and Bioinformatics.
The scientist’s investigation covers issues in Cell biology, Hsp90, Immunophilins, FKBP52 and Signal transduction. He integrates many fields in his works, including Cell biology and Trophoblast. His studies deal with areas such as Cancer research, Glucocorticoid receptor, Chaperone and Docking as well as Hsp90.
Mario D. Galigniana focuses mostly in the field of Chaperone, narrowing it down to topics relating to Receptor and, in certain cases, Nuclear receptor and Transcription factor. The concepts of his FKBP52 study are interwoven with issues in Cellular differentiation, Mechanism of action, Tetratricopeptide, Neurite and Neurotrophin. His work is dedicated to discovering how Signal transduction, Transcriptional regulation are connected with Cypa, Intracellular and Cyclophilin A and other disciplines.
His primary areas of investigation include FKBP52, Cell biology, Immunophilins, Hsp90 and Cellular differentiation. He has researched FKBP52 in several fields, including Transport protein, Scaffold protein, Acetylation and Transcriptional regulation. Mario D. Galigniana combines subjects such as Nuclear export signal, Nuclear matrix, Tetratricopeptide, Nuclear transport and Nuclear protein with his study of Hsp90.
His studies in Cellular differentiation integrate themes in fields like Chaperone, Protein folding, Receptor, Signal transduction and Protein structure.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement.
William B Pratt;Mario D Galigniana;Jennifer M Harrell;Donald B DeFranco.
Cellular Signalling (2004)
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 *
Mario D. Galigniana;Christine Radanyi;Jack Michel Renoir;Paul R. Housley.
Journal of Biological Chemistry (2001)
Role of molecular chaperones in steroid receptor action.
William B Pratt;Mario D Galigniana;Yoshihiro Morishima;Patrick J M Murphy.
Essays in Biochemistry (2004)
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.
Journal of Biological Chemistry (1997)
A model for the cytoplasmic trafficking of signalling proteins involving the hsp90-binding immunophilins and p50cdc37.
William B Pratt;Adam M Silverstein;Mario D Galigniana.
Cellular Signalling (1999)
Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein.
Adam M. Silverstein;Mario D. Galigniana;Kimon C. Kanelakis;Christine Radanyi.
Journal of Biological Chemistry (1999)
Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton
Mario D. Galigniana;Jennifer L. Scruggs;James Herrington;Michael J. Welsh.
Molecular Endocrinology (1998)
FKBP51 and FKBP52 in Signaling and Disease
Cheryl L. Storer;Chad A. Dickey;Mario Daniel Galigniana;Theo Rein.
Trends in Endocrinology and Metabolism (2011)
The role of DnaJ-like proteins in glucocorticoid receptor.hsp90 heterocomplex assembly by the reconstituted hsp90.p60.hsp70 foldosome complex.
Kurt D. Dittmar;Maria Banach;Mario D. Galigniana;William B. Pratt.
Journal of Biological Chemistry (1998)
Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus.
Michael J. Czar;Mario D. Galigniana;and Adam M. Silverstein;William B. Pratt.
Biochemistry (1997)
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