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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

FK506 binding protein 11, 19 kDa

FKBP11, FK506-binding protein, FKBP19
FKBP11 belongs to the FKBP family of peptidyl-prolyl cis/trans isomerases, which catalyze the folding of proline-containing polypeptides. The peptidyl-prolyl isomerase activity of FKBP proteins is inhibited by the immunosuppressant compounds FK506 and rapamycin (Rulten et al., 2006 [PubMed 16596453]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: CD1, CAN, CIs, FKBP51, ACID
Papers on FKBP11
Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin.
New
Yoon et al., Singapore, Singapore. In Nucleic Acids Res, Feb 2016
UNASSIGNED: The nuclear immunophilin FKBP25 interacts with chromatin-related proteins and transcription factors and is suggested to interact with nucleic acids.
Associations Between Self-Reported and Objectively Recorded Early Life Stress, FKBP5 Polymorphisms, and Depressive Symptoms in Midlife.
New
Räikkönen et al., Helsinki, Finland. In Biol Psychiatry, Dec 2015
BACKGROUND: FK506-binding protein 51 is involved in hypothalamic-pituitary-adrenal axis regulation.
Epigenetic regulation of autophagy by the methyltransferase EZH2 through an MTOR-dependent pathway.
New
Zhu et al., Beijing, China. In Autophagy, Nov 2015
Here we report that the methyltransferase EZH2 (enhancer of zeste 2 polycomb repressive complex 2 subunit) epigenetically represses several negative regulators of the MTOR (mechanistic target of rapamycin [serine/threonine kinase]) pathway, such as TSC2, RHOA, DEPTOR, FKBP11, RGS16 and GPI.
Bcl-2 and FKBP12 bind to IP3 and ryanodine receptors at overlapping sites: the complexity of protein-protein interactions for channel regulation.
Review
New
Bultynck et al., Leuven, Belgium. In Biochem Soc Trans, Jun 2015
The 12- and 12.6-kDa FK506-binding proteins, FKBP12 (12-kDa FK506-binding protein) and FKBP12.6 (12.6-kDa
The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease.
Review
New
Dickey et al., Tampa, United States. In J Neurochem, Apr 2015
PPIases, including Pin1, FK506-binding protein (FKBP) 52, FKBP51, and FKBP12, have been shown to interact with and regulate tau biology.
Association between FKBP5 Functional Polymorphisms and Completed Suicide.
Płoski et al., Warsaw, Poland. In Neuropsychobiology, 2014
FK506-binding protein 51 (FKBP5), which influences HPA axis activity via glucocorticoid receptors, is supposed to play an important role in the regulation of negative feedback and glucocorticoid resistance.
Chaperoning epigenetics: FKBP51 decreases the activity of DNMT1 and mediates epigenetic effects of the antidepressant paroxetine.
Rein et al., München, Germany. In Sci Signal, 2014
Epigenetic processes, such as DNA methylation, and molecular chaperones, including FK506-binding protein 51 (FKBP51), are independently implicated in stress-related mental disorders and antidepressant drug action.
Functions of the Hsp90-binding FKBP immunophilins.
Review
Cox et al., El Paso, United States. In Subcell Biochem, 2014
Within this class are Hsp90-binding peptidylprolyl isomerases, most of which belong to the FK506-binding protein (FKBP) family.
Osteogenesis imperfecta due to mutations in non-collagenous genes: lessons in the biology of bone formation.
Review
Smith et al., Bethesda, United States. In Curr Opin Pediatr, 2014
Heat shock protein 47 (HSP47) and FK506-binding protein-65 (FKBP65) defects cause types X and XI osteogenesis imperfecta via aberrant collagen crosslinking, folding, and chaperoning, while defects in SP7 transcription factor, wingless-type MMTV integration site family member 1 (WNT1), trimeric intracellular cation channel type b (TRIC-B), and old astrocyte specifically induced substance (OASIS) disrupt osteoblast development.
Mitochondria: FKBP38 and mitochondrial degradation.
Review
Nakayama et al., Fukuoka, Japan. In Int J Biochem Cell Biol, 2014
FK506-binding protein 38 (FKBP38) is a membrane chaperone that is localized predominantly to mitochondria and contains a COOH-terminal tail anchor.
FKBP51 affects cancer cell response to chemotherapy by negatively regulating Akt.
Impact
Wang et al., Rochester, United States. In Cancer Cell, 2009
Here we show that FKBP51 (FK506-binding protein 51) acts as a scaffolding protein for Akt and PHLPP and promotes dephosphorylation of Akt.
Conditional and reversible disruption of essential herpesvirus proteins.
Impact
Borst et al., Hannover, Germany. In Nat Methods, 2009
By fusing a destabilizing domain of the FK506-binding protein to essential cytomegalovirus proteins, we generated virus mutants in which amounts of fusion proteins and viral growth can be regulated by the synthetic ligand shield-1.
Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38.
Impact
Jiang et al., Pittsburgh, United States. In Science, 2007
We show that Rheb regulates mTOR through FKBP38, a member of the FK506-binding protein (FKBP) family that is structurally related to FKBP12.
Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis.
Impact
Nakayama et al., Fukuoka, Japan. In Nat Cell Biol, 2003
Here we show that mitochondrial FK506-binding protein 38 (FKBP38), unlike FKBP12, binds to and inhibits calcineurin in the absence of the immunosuppressant FK506, suggesting that FKBP38 is an inherent inhibitor of this phosphatase.
Calcineurin: form and function.
Review
Impact
Mertz et al., Rochester, United States. In Physiol Rev, 2000
Calcineurin is potently inhibited by immunosuppressant drugs, cyclosporin A and FK506, in the presence of their respective cytoplasmic immunophilin proteins, cyclophilin and FK506-binding protein.
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