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Regulation of FKBP51 and FKBP52 functions by post-translational modifications
(Portland Press, 2019-10)
FKBP51 and FKBP52 are two iconic members of the family of peptidyl-prolyl-(cis/trans)-isomerases (EC: 5.2.1.8), which comprises proteins that catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds in unfolded ...
Hsp90-binding immunophilin FKBP51 forms complexes with hTERT enhancing telomerase activity
(Elsevier, 2016-05-17)
FK506-binding proteins are members of the immunophilin family of proteins. Those immunophilins associated to the 90-kDa-heat-shock protein, Hsp90, have been proposed as potential modulators of signalling cascade factors ...
Proof that the high molecular weight immunophilin FKBP52 mediates the in vivo neuroregenerative effect of the macrolide FK506
(Pergamon-Elsevier Science Ltd, 2020-12)
The immunosuppressant drug FK506 (or tacrolimus) is a macrolide that binds selectively to immunophilins belonging to the FK506-binding protein (FKBP) subfamily, which are abundantly expressed proteins in neurons of the ...
Biological actions of the hsp90-binding immunophilins FKBP51 and FKBP52
(Multidisciplinary Digital Publishing Institute, 2019-08)
Immunophilins are a family of proteins whose signature domain is the peptidylprolylisomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) through ...
Immunophilins FKBP51 and FKBP52
(MDPI, 2019)
Immunophilins are a family of proteins whose signature domain is the peptidylprolyl-isomerase domain. High molecular weight immunophilins are characterized by the additional presence of tetratricopeptide-repeats (TPR) ...
NF-κB transcriptional activity is modulated by FK506-binding proteins FKBP51 and FKBP52: a role for peptidyl-prolyl isomerase activity
(American Society for Biochemistry and Molecular Biology, 2014-08)
Hsp90 binding immunophilins FKBP51 and FKBP52 modulate steroid receptor trafficking and hormone-dependent biological responses. With the purpose to expand this model to other nuclear factors that are also subject to ...
The Hsp90-binding immunophilin FKBP52 fosters neurodifferentiation and neuroregeneration in murine models
(Shenyang Editorial Dept Neural Regeneration Res, 2021-02)
The term immunophilin involves a family of proteins whose signature domain shows peptidyl-prolyl-(cis/trans)-isomerase (PPIase) enzymatic activity, i.e., the reversible cis/trans interconversion of Xaa-Pro bonds (Erlejman ...
FKBP51 and FKBP52 in signaling and disease
(Elsevier, 2011-12)
FKBP51 and FKBP52 are diverse regulators of steroid hormone receptor signaling, including receptor maturation, hormone binding and nuclear translocation. Although structurally similar, they are functionally divergent, which ...
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 ...