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FKBP14 gene

Known as: FKBP14, FK506-BINDING PROTEIN 14, FLJ20731 
National Institutes of Health

Related topics

Related topics

3 relations
FKBP11 geneFKBP22

Broader (1)

Genes

Papers overview

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2020
2020
The novel missense mutation Met48Lys in FKBP22 changes its structure and functions
Mutations in the FKBP14 gene encoding FKBP22 (FK506 Binding Protein 22 kDa) cause kyphoscoliotic Ehlers-Danlos Syndrome (kEDS… 
2019
2019
Prognostic Significance of FKBP14 in Gastric Cancer
Introduction Although our understanding on gastric cancer biology is better than a decade ago, its practical effect on screening… 
2018
2018
MiR-361 inhibits osteosarcoma cell lines invasion and proliferation by targeting FKBP14.
OBJECTIVE MicroRNAs have been reported to contribute to the development of osteosarcoma via negatively regulating the target… 
2018
2018
Inhibition and Substrate Specificity Properties of FKBP22 from a Psychrotrophic Bacterium, Shewanella sp. SIB1
SIB1 FKBP22 is a peptidyl prolyl cis–trans isomerase (PPIase) member from a psychrotrophic bacterium, Shewanella sp. SIB1… 
2017
2017
Inhibitory effects of FKBP14 on human cervical cancer cells.
The FK506-binding protein 14 (FKBP14), which belongs to a subfamily of immunophilins, has been implicated in various biochemical… 
2016
2016
Determining the roles of a conserved tyrosine residue in a Mip-like peptidyl-prolyl cis-trans isomerase.
2014
2014
FKBP14‐related Ehlers‐Danlos syndrome: Expansion of the phenotype to include vascular complications
Biallelic mutations in FKBP14 cause a recessive form of Ehlers‐Danlos syndrome (EDS) characterized by progressive kyphoscoliosis… 
2014
2014
Inhibitor-Induced Conformational Stabilization and Structural Alteration of a Mip-Like Peptidyl Prolyl cis-trans Isomerase and Its C-Terminal Domain
FKBP22, an Escherichia coli-encoded PPIase (peptidyl-prolyl cis-trans isomerase) enzyme, shares substantial identity with the Mip… 
2012
2012
The helix located between the two domains of a mip-like peptidyl-prolyl cis-trans isomerase is crucial for its structure, stability, and protein folding ability.
FKBP22, a PPIase (peptidyl-prolyl cis-trans isomerase) produced by Escherichia coli, binds FK506 and rapamycin (both… 
2007
2007
FKBP22 is part of chaperone/folding catalyst complexes in the endoplasmic reticulum of Neurospora crassa
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