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Peptidylprolyl isomerase B

cyclophilin B, CyPB, PPIB
The protein encoded by this gene is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression. Variants have been identified in this protein that give rise to recessive forms of osteogenesis imperfecta. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: CIs, CsA, CAN, Peptidylprolyl Isomerase, HAD
Papers using cyclophilin B antibodies
LuSIV cells: a reporter cell line for the detection and quantitation of a single cycle of HIV and SIV replication
Matano Tetsuro et al., In Retrovirology, 1999
... LLC-MK2 (normal) and CypA-KD cells were subjected to the immunoblot analysis using anti-α-tubulin, anti-CypA and anti-CypB antibodies (Abcam Inc., Cambridge, MA) (left ...
Papers on cyclophilin B
Cyclophilin B enhances HIV-1 infection.
Belshan et al., Omaha, United States. In Virology, Feb 2016
UNASSIGNED: Cyclophilin B (CypB) is a member of the immunophilin family and intracellular chaperone.
Research Resource: A Dual Proteomic Approach Identifies Regulated Islet Proteins During β-Cell Mass Expansion In Vivo.
Ahnfelt-Rønne et al., Denmark. In Mol Endocrinol, Jan 2016
These included several proteins, not previously associated with pregnancy-induced islet expansion, such as CLIC1, STMN1, MCM6, PPIB, NEDD4, and HLTF.
Reference genes for valid gene expression studies on rat dental, periodontal and alveolar bone tissue by means of RT-qPCR with a focus on orthodontic tooth movement and periodontitis.
Römer et al., Regensburg, Germany. In Ann Anat, Jan 2016
RESULTS: PPIB/YWHAZ were the most stabile reference genes for the combined dental, periodontal and alveolar bone tissue of the rat overall, in untreated animals and rats with additional periodontitis, whereas PPIB/B2M performed best in orthodontically treated rats with YWHAZ ranking third.
Alzheimer's disease-causing proline substitutions lead to presenilin 1 aggregation and malfunction.
Cohen et al., Jerusalem, Israel. In Embo J, Dec 2015
These substitutions were found to prevent the endoplasmic reticulum (ER)-resident chaperone, cyclophilin B, from assisting presenilin 1 to fold properly, leading to its aggregation, deposition in the ER, reduction of γ-secretase activity, and impaired mitochondrial distribution and function.
The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease.
Dickey et al., Tampa, United States. In J Neurochem, Apr 2015
Moreover, Pin1, FKBP12, FKBP52, cyclophilin (Cyp) A, CypB, and CypD have been shown to also regulate Ab production or the toxicity associated with Ab pathology.
Mutational characterization of the P3H1/CRTAP/CypB complex in recessive osteogenesis imperfecta.
Paula et al., Vitória, Brazil. In Genet Mol Res, 2014
The LEPRE1, CRTAP, and PPIB genes encode proteins that form the P3H1/CRTAP/CypB complex, which is responsible for posttranslational modifications of type I collagen.
Cyclophilin inhibition as potential therapy for liver diseases.
Naoumov, Basel, Switzerland. In J Hepatol, 2014
The extracellular fractions of CypA and CypB are potent pro-inflammatory mediators.
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
RECENT FINDINGS: Bone-restricted interferon-induced transmembrane (IFITM)-like protein (BRIL) and pigment epithelium-derived factor (PEDF) defects cause types V and VI osteogenesis imperfecta via defective bone mineralization, while defects in cartilage-associated protein (CRTAP), prolyl 3-hydroxylase 1 (P3H1), and cyclophilin B (CYPB) cause types VII-IX osteogenesis imperfecta via defective collagen post-translational modification.
Functional aspects of extracellular cyclophilins.
Schiene-Fischer et al., In Biol Chem, 2014
The extracellular fractions of the cyclophilins CypA and CypB are involved in the control of cell-cell communication.
Cyclophilin B attenuates the expression of TNF-α in lipopolysaccharide-stimulated macrophages through the induction of B cell lymphoma-3.
Allain et al., Villeneuve-d'Ascq, France. In J Immunol, 2012
these findings suggest an unexpected role for cyclophilin B in attenuation of the responses of proinflammatory macrophages
Release of overexpressed CypB activates ERK signaling through CD147 binding for hepatoma cell resistance to oxidative stress.
Choe et al., Seoul, South Korea. In Apoptosis, 2012
CypB has an essential function in protecting hepatoma cells against oxidative stress through binding to CD147 and regulating the ERK pathway
Spatiotemporal behavior of nuclear cyclophilin B indicates a role in RNA transcription.
Van Oostveldt et al., Gent, Belgium. In Int J Mol Med, 2012
CypB interacts with these proteins and is involved in ribosome biogenesis and RNA transcription.
Comparing human pancreatic cell secretomes by in vitro aptamer selection identifies cyclophilin B as a candidate pancreatic cancer biomarker.
White et al., Durham, United States. In J Clin Invest, 2012
Cyclophilin B is a candidate pancreatic cancer biomarker.
A major prolactin-binding complex on human milk fat globule membranes contains cyclophilins A and B: the complex is not the prolactin receptor.
Walker et al., Riverside, United States. In Am J Physiol Endocrinol Metab, 2012
First report of a unique, multicomponent, high-capacity milk fat reservoir of prolactin as a bilayer-bound complex with cyclophilins A and B in human milk.
Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding.
Marini et al., Bethesda, United States. In N Engl J Med, 2010
They had a homozygous start-codon mutation in the peptidyl-prolyl isomerase B gene (PPIB), which results in a lack of cyclophilin B (CyPB), the third component of the complex.
Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta.
Marini et al., Bethesda, United States. In Nat Genet, 2007
CRTAP forms a complex with cyclophilin B and prolyl 3-hydroxylase 1, which is encoded by LEPRE1 and hydroxylates one residue in type I collagen, alpha1(I)Pro986.
CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta.
Lee et al., Houston, United States. In Cell, 2006
CRTAP can form a complex with P3H1 and cyclophilin B (CYPB), and Crtap-/- bone and cartilage collagens show decreased prolyl 3-hydroxylation.
Noninvasive diagnosis of renal-allograft rejection by measurement of messenger RNA for perforin and granzyme B in urine.
Suthanthiran et al., New York City, United States. In N Engl J Med, 2001
Messenger RNA (mRNA) encoding the cytotoxic proteins perforin and granzyme B and a constitutively expressed cyclophilin B gene were measured with the use of a competitive, quantitative polymerase chain reaction, and the level of expression was correlated with allograft status.
Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B.
Goff et al., New York City, United States. In Cell, 1993
Cyclosporin A efficiently disrupts the Gag-CyPA interaction and less efficiently disrupts the Gag-CyPB interaction.
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