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Molecular chaperone activity and biological regulatory actions of the TPR-domain immunophilins FKBP51 and FKBP52
(Bentham Science Publishers, 2014-05)
Immunophilins comprise a family of intracellular proteins with peptidyl-prolyl-(cis/trans)-isomerase activity. These foldases are abundant, ubiquitous, and able to bind immunosuppressant drugs, from which the term immunophilin ...
Functions of Hsp90-Binding FKBP immunophilins
(Springer, 2015)
Hsp90 functionally interacts with a broad array of client proteins, but in every case examined Hsp90 is accompanied by one or more co-chaperones. One class of co-chaperone contains a tetratricopeptide repeat domain that ...
TPR-Domain immunophilin FKBP51 is a major mitochondrial protein that protects cells against oxidative stress
(American Society For Biochemistry And Molecular Biology, 2011-07-05)
Confocal microscopy images revealed that the tetratricopeptide repeat motif (TPR) domain immunophilin FKBP51 shows colocalization with the specific mitochondrial marker MitoTracker. Signal specificity was tested with ...
Dynamic mitochondrial–nuclear redistribution of the immunophilin FKBP51 is regulated by the PKA signaling pathway to control gene expression during adipocyte differentiation
(Company of Biologists, 2013-12)
Glucocorticoids play an important role in adipogenesis via the glucocorticoid receptor (GR) that forms a heterocomplex with Hsp90•Hsp70 and one high molecular weight immunophilin FKBP51 or FKBP52. When 3T3-L1 preadipocytes ...
Adipogenesis is Under Surveillance of Hsp90 and the High Molecular Weight Immunophilin FKBP51
(Taylor & Francis, 2015-05)
Adipose tissue plays a central role in the control of energy balance as well as in the maintenance of metabolic homeostasis. It was not until recently that the first evidences of the role of heat shock protein (Hsp) 90 and ...
Estudio del rol de los antidepresivos como moduladores de la SUMOilación y su efecto en la actividad de la co-chaperona de Hsp90 FKBP51 en el contexto neuroendócrinoStudy of the role of antidepressants as modulators of SUMOconjugation and its effect on the activity of Hsp90 co-chaperone FKBP51 in the neuroendocrine context
(2019-03-19)
La actividad del receptor de glucocorticoides (GR) se encuentra regulada por un complejo multiproteico que incluye a la co-chaperona FKBP (FK506 binding protein) 51. FKBP51 es un potente inhibidor de la función del GR. ...
Biological relevance of Hsp90-binding immunophilins in cancer development and treatment
(John Wiley & Sons Inc, 2016-02)
Immunophilins are a family of intracellular receptors for immunosuppressive drugs. Those immunophilins that are related to immunosuppression are the smallest proteins of the family, i.e., FKBP12 and CyPA, whereas the other ...
Peptidyl‐Prolyl Isomerase Activity of Immunophilins Could Be the Mere Consequence of Protein Complex Organization
(John Wiley & Sons Inc, 2020-05)
Immunophilins comprise a family of proteins characterized by the presence of a specific sequence that usually shows peptidyl‐prolyl‐(cis/trans )‐isomerase (PPIase) activity, i.e., the reversible cis/trans interconversion ...
La redistribución dinámica mitocondria-núcleo de la inmunofilina fkbp51 es regulada por pka para modular la expresión de genes durante el proceso de adipogénesisThe dynamic mitochondria-nuclear redistribution of FKBP51 during the process of adipocyte differentiation is regulated by PKA
(Medicina (Buenos Aires), 2013-11)
Los glucocorticoides tienen un papel central en la adipogénesis, por su unión al receptor RG cito-plasmático formando parte de un heterocomplejo también integrado por una inmunofilina (INM) de alto peso molecular, FKBP51 ...
Hsp90-binding immunophilins as a potential new platform for drug treatment
(Future Science, 2013-04)
Immunophilins are proteins that contain a PPIase domain as a family signature. Low-molecular-weight immunophilins were first described associated to immunosuppressive action and protein folding. Recent studies of other ...