Peptidylprolyl Isomerase

Known as: Peptidylprolyl Isomerase [Chemical/Ingredient], Isomerase, Prolyl, PPIase 
An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.
National Institutes of Health

Papers overview

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Review
2007
Review
2007
Protein phosphorylation regulates many cellular processes by causing changes in protein conformation. The prolyl isomerase PIN1… (More)
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Highly Cited
2007
Highly Cited
2007
The tumor-suppressor function of p53 relies on its transcriptional activity, which is modulated by post-translational… (More)
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Highly Cited
2007
Highly Cited
2007
Certain histocompatibility leukocyte antigen (HLA) alleles are associated with improved clinical outcomes for individuals… (More)
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Highly Cited
2007
Highly Cited
2007
This corrects the article DOI: 10.1038/nature04543 
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Highly Cited
2003
Highly Cited
2003
Hsp90 is required for the normal activity of steroid receptors, and in steroid receptor complexes it is typically bound to one of… (More)
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Highly Cited
2002
Highly Cited
2002
p53 is activated in response to various genotoxic stresses resulting in cell cycle arrest or apoptosis. It is well documented… (More)
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Highly Cited
1996
Highly Cited
1996
THE NIMA kinase is essential for progression through mitosis in Aspergillus nidulans1–6, and there is evidence for a similar… (More)
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Highly Cited
1994
Highly Cited
1994
CYCLOPHILINS are a family of proteins that bind the immunosuppressant cyclosporin A, possess peptidyl–prolylcis–trans isomerase… (More)
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Highly Cited
1991
Highly Cited
1991
CYCLOSPORINA and FK506 inhibit T- and B-cell activation and other processes essential to an effective immune response1–3. In T… (More)
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Highly Cited
1989
Highly Cited
1989
CYCLOSPORIN A and the newly discovered immunosuppressant, FK-506, are potent inhibitors of T cell activation1. In addition to… (More)
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