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Cyclophilin D protects cell from cell death.
There was increased [Ca(2+)](c), [Ca(2+)](m), mCICR, MPTP opening, and expression of cyclophilin D and decreased DeltaPsim in POAG TM cells compared with control cells.
Mannheimia haemolytica leukotoxin binds cyclophilin D on bovine neutrophil mitochondria.
Binding of signal transducer and activator of transcription 3 (STAT3) to cyclophilin D (CypD) was important for reducing mitochondrial reactive oxygen species (ROS) production after oxidative stress.
these data demonstrate that mitochondria are impaired in aging bone and that CypD deletion protects against this impairment to prevent bone loss. This implicates CypD-regulated MPTP (zeige PTPN2 ELISA Kits) and mitochondrial dysfunction in the impairment of bone cells and in aging-related bone loss.
Ppif (zeige PPID ELISA Kits)+/+ and Ppif (zeige PPID ELISA Kits)-/- eosinophils exhibited no significant difference in apoptosis or secondary necrosis.
Ischemic postconditioning might prevent lethal reperfusion injury through an increased SIRT3 activity and subsequent attenuation of CyPD acetylation at reperfusion.
These findings reveal the role of HAX-1 (zeige HAX1 ELISA Kits) in regulating cyclophilin-D levels via an Hsp90 (zeige HSP90 ELISA Kits)-dependent mechanism, resulting in protection against activation of mPTP (zeige PTPN2 ELISA Kits) and subsequent cell death responses
study identifies a novel signaling pathway composed of E2F1, miR-30b and CypD that regulates myocardial necrosis.
It is concluded that CypD sensitizes the brain mitochondria to PT, and its inhibition by CsA (zeige HSPA9 ELISA Kits) or CypD absence improves the complex I-related mitochondrial function and increases mitochondria stability against Ca(2 (zeige CA2 ELISA Kits)+) stress.
Data indicate that Ppif protein cyclophilin D (CypD)-dependent protein kinase A (PKA)/cAMP regulatory-element-binding (CREB) signaling is responsible for amyloid beta (Abeta)-induced synaptic injury.
Ablation of CypD leads to changes in the mitochondrial acetylome which may contribute to altered mitochondrial metabolism in CypD-deficient mice.
These results suggest a physiologic function for CypD and the mitochondrial permeability transition in the regulation of starvation-induced autophagy.
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 is part of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.
peptidyl-prolyl cis-trans isomerase A
, peptidylprolyl isomerase F (cyclophilin F)
, peptidyl-prolyl cis-trans isomerase F, mitochondrial
, cyclophilin D
, cyclophilin F
, ppiase F
, rotamase F
, peptidylprolyl isomerase F
, PPIase F
, cyclophilin 3
, mitochondrial cyclophilin
, peptidyl-prolyl cis-trans isomerase, mitochondrial
, mitochondrial Cyclophilin D