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FK506 binding protein 10

FKBP65, 65-kDa FK506-binding protein, FKBP10
The protein encoded by this gene belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. This protein localizes to the endoplasmic reticulum and acts as a molecular chaperone. Alternatively spliced variants encoding different isoforms have been reported, but their biological validity has not been determined.[provided by RefSeq, Nov 2009] (from NCBI)
Top mentioned proteins: CIs, LEPRE1, cyclophilin B, CAN, COL1A1
Papers on FKBP65
Inhibition of the FKBP family of peptidyl prolyl isomerases induces abortive translocation and degradation of the cellular prion protein.
Williams et al., Edmonton, Canada. In Mol Biol Cell, Feb 2016
In mouse cells, depletion of ER luminal FKBP10 was almost as potent as FK506 in attenuating expression of PrP(C).
Homozygous sequence variants in the FKBP10 gene underlie osteogenesis imperfecta in consanguineous families.
Ahmad et al., Islamabad, Pakistan. In J Hum Genet, Dec 2015
It is one of the rare forms of skeletal deformity caused by sequence variants in at least 14 different genes, including FKBP10 (MIM 607063) encoding protein FKBP65.
FK506-Binding Protein 10, a Potential Novel Drug Target for Idiopathic Pulmonary Fibrosis.
Eickelberg et al., München, Germany. In Am J Respir Crit Care Med, Sep 2015
FK506-binding protein 10 (FKBP10) is a collagen chaperone, mutations of which have been indicated in the reduction of extracellular matrix stiffness (e.g., in osteogenesis imperfecta).
HSP47 and FKBP65 cooperate in the synthesis of type I procollagen.
Cohn et al., Los Angeles, United States. In Hum Mol Genet, May 2015
Among these include mutations in the genes SERPINH1 and FKBP10, which encode the type I procollagen chaperones HSP47 and FKBP65, respectively, and predominantly produce a moderately severe form of OI.
Diet-induced unresolved ER stress hinders KRAS-driven lung tumorigenesis.
Coppari et al., Genève, Switzerland. In Cell Metab, Feb 2015
Whole-genome transcriptional analyses revealed FKBP10 as one of the most downregulated chaperones in tumors of the HCD-pre-tumor-onset group.
Bruck syndrome - a rare syndrome of bone fragility and joint contracture and novel homozygous FKBP10 mutation.
Nasirabadi et al., Shīrāz, Iran. In Endokrynol Pol, 2014
According to the genotype, it has been classified into types 1 and 2. Recently, mutations in FKBP10, localised to chromosome 17q21, have been identified in some patients of Bruck syndrome.
Development of a high-throughput resequencing array for the detection of pathogenic mutations in osteogenesis imperfecta.
Han et al., China. In Plos One, 2014
The mutations in this disorder have been widely reported to be on various exonal hotspots of the candidate genes, including COL1A1, COL1A2, CRTAP, LEPRE1, and FKBP10, thus creating a great demand for precise genetic tests.
Novel Deletion of SERPINF1 Causes Autosomal Recessive Osteogenesis Imperfecta Type VI in Two Brazilian Families.
Perez et al., São Paulo, Brazil. In Mol Syndromol, 2014
Autosomal recessive osteogenesis imperfecta (OI) accounts for 10% of all OI cases, and, currently, mutations in 10 genes (CRTAP, LEPRE1, PPIB, SERPINH1, FKBP10, SERPINF1, SP7, BMP1, TMEM38B, and WNT1) are known to be responsible for this form of the disease.
What is new in genetics and osteogenesis imperfecta classification?
Zabel et al., Belo Horizonte, Brazil. In J Pediatr (rio J), 2014
After 2006, mutations were identified in the CRTAP, FKBP10, LEPRE1, PLOD2, PPIB, SERPINF1, SERPINH1, SP7, WNT1, BMP1, and TMEM38B genes, associated with recessive OI and mutation in the IFITM5 gene associated with dominant OI.
Osteogenesis imperfecta due to mutations in non-collagenous genes: lessons in the biology of bone formation.
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.
A small molecule inhibitor of ETV1, YK-4-279, prevents prostate cancer growth and metastasis in a mouse xenograft model.
Üren et al., Baltimore, United States. In Plos One, 2013
Expression of ETV1 target genes MMP7, FKBP10 and GLYATL2 were reduced in YK-4-279 treated animals.
Novel mutations in FKBP10 and PLOD2 cause rare Bruck syndrome in Chinese patients.
Li et al., Beijing, China. In Plos One, 2013
The novel compound heterozygous mutations c.764_772dupACGTCCTCC (p.255_257dupHisValLeu) in exon 5 and c.1405G>T (p.Gly469X) in exon 9 of FKBP10 were identified in one proband.
Bone collagen: new clues to its mineralization mechanism from recessive osteogenesis imperfecta.
Weis et al., Seattle, United States. In Calcif Tissue Int, 2013
They include CRTAP, LEPRE1, and PPIB, which encode three proteins forming the prolyl 3-hydroxylase complex; PLOD2 and FKBP10, which encode, respectively, lysyl hydroxylase 2 and a foldase required for its activity in forming mature cross-links in bone collagen; SERPINH1, which encodes the collagen chaperone HSP47; SERPINF1, which encodes pigment epithelium-derived factor required for osteoid mineralization; and BMP1, which encodes the type I procollagen C-propeptidase.
New genes in bone development: what's new in osteogenesis imperfecta.
Blissett et al., Bethesda, United States. In J Clin Endocrinol Metab, 2013
Next, defects in collagen chaperones, HSP47 and FKBP65, lead to improper procollagen folding and deficient collagen cross-linking in matrix, respectively.
[Mutations of noncollagen genes in osteogenesis imperfecta--implications of the gene products in collagen biosynthesis and pathogenesis of disease].
Galicka, In Postepy Hig Med Dosw (online), 2011
The latest findings added to the spectrum of OI-causing and collagen-influencing factors other chaperones (HSP47 and FKBP65) and protein BMP-1, which emphasizes the complexity of collagen folding and secretion as well as their importance in bone formation.
Expression of FK506 binding protein 65 (FKBP65) is decreased in epithelial ovarian cancer cells compared to benign tumor cells and to ovarian epithelium.
Birkenkamp-Demtroder et al., Malmö, Sweden. In Tumour Biol, 2011
The differential expression of FKBP65 indicates a role in ovarian physiology as well as in ovarian tumor development
Mutations in FKBP10 cause both Bruck syndrome and isolated osteogenesis imperfecta in humans.
Alkuraya et al., Riyadh, Saudi Arabia. In Am J Med Genet A, 2011
Mutations in FKBP10 cause both Bruck syndrome and isolated osteogenesis imperfecta in humans.
Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome.
Lee et al., Houston, United States. In J Bone Miner Res, 2011
FKBP10 mutations are a cause of recessive osteogenesis imperfecta and Bruck syndrome.
Effect of FKBP65, a putative elastin chaperone, on the coacervation of tropoelastin in vitro.
Ananthanarayanan et al., Hamilton, Canada. In Biochem Cell Biol, 2010
FKBP65 may act as an elastin chaperone in vivo by controlling both the coacervation and the maturation stages of its selfassembly into fibrils.
Mutations in FKBP10 can cause a severe form of isolated Osteogenesis imperfecta.
Sander et al., München, Germany. In Bmc Med Genet, 2010
Homozygosity mapping identified FKBP10 as a candidate gene, and sequencing revealed a base pair exchange that causes a C-terminal premature stop codon in this gene.
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