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Human PPID Protein expressed in Wheat germ - ABIN1315874
Nguyen, Stevens, Kohr, Steenbergen, Sack, Murphy: Cysteine 203 of cyclophilin D is critical for cyclophilin D activation of the mitochondrial permeability transition pore. in The Journal of biological chemistry 2011
Show all 2 Pubmed References
Data show that cyclophilin 40 (CyP40) interacts with and dissolves amyloids forming proteins tau and alpha-synuclein aggregates.
The thermodynamics of binding of Cyp-40 to Hsp90 shows remarkable temperature sensitivity in the physiological temperature range.
cyclophilin-D protein could increase oxidative stress and cause endothelial cell injury and apoptosis. cyclophilin-D protein is the key factor in reactive oxygen species-induced mitochondrial damage, leading to apoptosis of endothelial cells.
Cyp40 binds to C2I in vitro and in intact cells, it also interacts with the enzyme components of iota toxin and CDT, suggesting a common principle for this toxin family.
The Photorhabdus toxins TccC3 and TccC5 interacted with Hsp90, FKBP51, Cyp40 and CypA, suggesting a role of these host cell factors in translocation and/or refolding of the ADP-ribosyltransferases.
this is the first report establishing an important role for Cyp40 in lymphoma.
Data show that disruption of FKBP51 and Cyp40 in AI C4-2 cells caused only a small reduction in proliferation.
cyclophilin D suppresses apoptotic cell death via a mitochondrial hexokinase II-dependent mechanism in cancer cells
CyP40 chaperone function then, is localized within the linker that forms a binding cleft with potential to accommodate non-native substrates
CyP40 is found in the cell nucleus after 3-methylchloranthrene treatment and appears to promote the dioxin response element binding form of the AhR/Arnt heterodimer.
CypD-mediated mitochondrial permeability transition pore is directly linked to the cellular and synaptic perturbations observed in the pathogenesis of Alzheimer's disease.
Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic effect
The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein has been shown to possess PPIase activity and, similar to other family members, can bind to the immunosuppressant cyclosporin A.
peptidylprolyl isomerase D
, peptidylprolyl isomerase D (cyclophilin D)
, 40 kDa peptidyl-prolyl cis-trans isomerase D
, PPIase D
, cyclophilin 40
, cyclophilin D
, cyclophilin-related protein
, peptidyl-prolyl cis-trans isomerase D
, rotamase D
, 40 kDa peptidyl-prolyl cis-trans isomerase
, Cyclophilin D
, estrogen receptor-binding cyclophilin
, cytoplasmic cyclophilin D