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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

Related topics

Related topics

37 relations

Broader (5)

Amino Acid IsomerasesBacterial ProteinsCarrier ProteinsCyclophilins
FKBP1A wt AlleleFKBP6 geneIn BloodLRR1 gene

Narrower (12)

FkpA protein, E coliILPA protein, Aeromonas hydrophilaImmunophilinsMip protein, Legionella pneumophila

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2002
Highly Cited
2002
The prolyl isomerase Pin1 reveals a mechanism to control p53 functions after genotoxic insults
The tumour suppressor p53 is important in the cell decision to either arrest cell cycle progression or induce apoptosis in… 
Highly Cited
2002
Highly Cited
2002
Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes
Phosphorylation of proteins on serine/threonine residues preceding proline is a key signaling mechanism. The conformation and… 
Highly Cited
1999
Highly Cited
1999
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
The role of molecular chaperones in assisting the folding of newly synthesized proteins in the cytosol is poorly understood. In… 
Highly Cited
1998
Highly Cited
1998
The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins.
Phosphorylation of mitotic proteins on the Ser/Thr-Pro motifs has been shown to play an important role in regulating mitotic… 
Highly Cited
1996
Highly Cited
1996
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Highly Cited
1996
Highly Cited
1996
New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
A global search for extracytoplasmic folding catalysts in Escherichia coli was undertaken using different genetic systems that… 
Highly Cited
1996
Highly Cited
1996
SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.
Little is known about either the process of periplasmic protein folding or how information concerning the folding state in this… 
Highly Cited
1995
Highly Cited
1995
X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex
Highly Cited
1992
Highly Cited
1992
Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activity.
Calcineurin, a Ca2+, calmodulin-dependent protein phosphatase, was recently found to bind with high affinity to two different… 
Highly Cited
1990
Highly Cited
1990
Probing immunosuppressant action with a nonnatural immunophilin ligand
The immunosuppressants FK506 and rapamycin bind to the same immunophilin, FK506 binding protein (FKBP), and inhibit distinct… 
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