Browse our PPID Proteins (PPID)

Full name:
Peptidylprolyl Isomerase D Proteins (PPID)
On are 23 Peptidylprolyl Isomerase D (PPID) Proteins from 11 different suppliers available. Additionally we are shipping PPID Antibodies (106) and PPID Kits (19) and many more products for this protein. A total of 160 PPID products are currently listed.
4930564J03Rik, cyp-40, cypd, PPID, Ppidl, Ppif, wu:fb18b07, zgc:86711
list all proteins Gene Name GeneID UniProt
PPID 5481 Q08752
PPID 361967 Q6DGG0
PPID 67738 Q9CR16

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PPID Proteins (PPID) by Origin

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Top referenced PPID Proteins

  1. Human PPID Protein expressed in Escherichia coli (E. coli) - ABIN667706 : Machida, Ohta, Osada: Suppression of apoptosis by cyclophilin D via stabilization of hexokinase II mitochondrial binding in cancer cells. in The Journal of biological chemistry 2006 (PubMed)
    Show all 2 references for 667706

  2. 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 (PubMed)
    Show all 2 references for 1315874

More Proteins for PPID Interaction Partners

Human Peptidylprolyl Isomerase D (PPID) interaction partners

  1. Data show that cyclophilin 40 (CyP40) interacts with and dissolves amyloids forming proteins tau and alpha-synuclein aggregates.

  2. This review discusses previous studies to provide comprehensive information on the physiological role of cyclophilin D as well as PTP opening in the cell that can be taken into consideration for the development of new PTP inhibitors. [review]

  3. The influx of unfolded p53 (show TP53 Proteins) into the mitochondrial matrix in response to oxidative stress indirectly activates the normally inhibited CypD (show CYPD Proteins) by displacing it from Trap1 (show TRAP1 Proteins) complexes. This activates CypD's isomerase activity. Liberated CypD (show CYPD Proteins) then isomerizes multiple proteins including p53 (show TP53 Proteins) (causing p53 (show TP53 Proteins) aggregation) and the structural components of the mPTP (show PTPN2 Proteins) pore, inducing pore opening.

  4. The present study is to investigate the role of CypD (show CYPD Proteins) in regulating the mitochondrial dynamics relevant to oxidative stress induced (show SQSTM1 Proteins) neuron dysfunctions.

  5. CyPD (show CYPD Proteins) regulates mitochondrial metabolism, and likely cell survival, by promoting more efficient electrons flow through the respiratory chain via increased supercomplex formation

  6. cyclophilin D (show PPIF Proteins) may modify mitochondrial features by inducing the translocation of molecules to the mitochondria through the mechanism associated with cellular energy metabolism

  7. The thermodynamics of binding of Cyp-40 to Hsp90 (show HSP90 Proteins) shows remarkable temperature sensitivity in the physiological temperature range.

  8. cyclophilin-D (show PPIF Proteins) protein could increase oxidative stress and cause endothelial cell injury and apoptosis. cyclophilin-D (show PPIF Proteins) protein is the key factor in reactive oxygen species-induced mitochondrial damage, leading to apoptosis of endothelial cells.

  9. Results show that CypD interacts with SPG7 and VDAC to form the mitochondrial permeability transition pore complex (PTP)and its CsA-binding region is necessary for PTP formation.

  10. molecular determinants necessary for Cyclophilin D (show PPIF Proteins) activity regulation and binding to proposed pore constituents thereby regulating the mitochondrial permeability transition pore.

Cow (Bovine) Peptidylprolyl Isomerase D (PPID) interaction partners

  1. LKT-mediated cell death involve dynamin-2 (show DNM2 Proteins) and cyclophilin D (show PPIF Proteins).

Mouse (Murine) Peptidylprolyl Isomerase D (PPID) interaction partners

  1. Murine eosinophil necrosis is regulated in vitro and in vivo by cyclophilin D (show PPIF Proteins).

  2. Cyclophilin D (show PPIF Proteins) is an important but non-obligatory regulator of mitoflash activity in cardiac muscle, whereas it is dispensable in the skeletal muscle, due in part to differential cyclophilin D (show PPIF Proteins) expression.

  3. Suggest that cyclosporin A-mediated CypD (show CYPD Proteins) inhibition may provide a promising therapeutic potential for protecting retinal ganglion cells against ischemic injury-mediated mitochondrial dysfunction.

  4. Loss of CypD (show CYPD Proteins) results in changes in a number of mitochondrial proteins and metabolic pathways.

  5. CypD (show CYPD Proteins) directs mitochondria-to-nuclei inflammatory gene expression in normal and tumor cells

  6. BAX (show BAX Proteins)/BAK (show BAK1 Proteins)-independent cell death did not require Cyclophilin D (CypD (show CYPD Proteins)) expression, an important regulator of the mitochondrial permeability transition pore

  7. At the whole muscle level, lack of cyclophilin-D (show PPIF Proteins) does not protect against muscle atrophy, release of mitochondrial pro-apoptotic factors and activation of caspases following denervation.

  8. mitochondrial permeability transition was increased by hypoxia-reoxygenation but was less in normoxic and hypoxia-reoxygenation Ppif(-/-) than wild type tubules

  9. These findings point to a possible role of immunophilin (show FKBP1A Proteins) signal transduction pathways in astrocytic modulation of neuronal activity at the tripartite synapse.

  10. Cyclophilin D (show PPIF Proteins) deficiency protects against acetaminophen-induced oxidant stress and liver injury.

PPID Protein Profile

Protein Summary

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.

Alternative names and synonyms associated with PPID

  • peptidylprolyl isomerase D (PPID)
  • peptidylprolyl isomerase D (Ppid)
  • peptidylprolyl isomerase D (ppid)
  • peptidylprolyl isomerase D (cyclophilin D) (Ppid)
  • peptidylprolyl isomerase D (cyclophilin D) (ppid)
  • 4930564J03Rik protein
  • cyp-40 protein
  • cypd protein
  • PPID protein
  • Ppidl protein
  • Ppif protein
  • wu:fb18b07 protein
  • zgc:86711 protein

Protein level used designations for PPID

peptidylprolyl isomerase D , peptidylprolyl isomerase D (cyclophilin D) , 40 kDa peptidyl-prolyl cis-trans isomerase D , PPIase D , cyclophilin 40 , cyclophilin D , cyclophilin-40 , 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

737256 Pan troglodytes
5481 Homo sapiens
361967 Rattus norvegicus
415155 Danio rerio
428725 Gallus gallus
475481 Canis lupus familiaris
281420 Bos taurus
67738 Mus musculus
447715 Xenopus laevis
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