The Pin1 prolyl isomerase regulates phosphorylation signaling by controlling protein
conformation after phosphorylation, and its upregulation promotes oncogenesis via acting …

The peptidyl-prolyl cis-trans isomerase Pin1 is a pivotal therapeutic target in cancers, but the
regulation of Pin1 protein stability is largely unknown. High Pin1 expression is associated …

Pin1 is a phospho-specific prolyl isomerase that regulates numerous key signaling
molecules and whose deregulation contributes to disease notably cancer. However, since …

Pin1, a conserved eukaryotic peptidyl‐prolyl cis/trans isomerase, has profound effects on
numerous key‐signaling molecules, and its deregulation contributes to disease, particularly …

Pin1, a member of the parvulin family of peptidyl-prolyl cis-trans isomerases (PPIases) has
been implicated in the G2-M transition of the mammalian cell cycle. Pin1 interacts with a …

Phosphorylation of proteins on serine or threonine residues that immediately precede
proline (pSer/Thr‐Pro) is a central signaling mechanism in cell proliferation and …

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) is an evolutionally conserved
and unique enzyme that specifically catalyzes the cis-trans isomerization of phosphorylated …

Emerging evidence demonstrates that RUNX3 is a tumor suppressor in breast cancer.
Inactivation of RUNX3 in mice results in spontaneous mammary gland tumors, and …

Pin1 is the only known peptidyl-prolyl cis–trans isomerase (PPIase) that specifically
recognizes and isomerizes the phosphorylated Serine/Threonine-Proline (pSer/Thr-Pro) …

Proline directed phosphorylation is a key regulatory mechanism controlling the function of
fundamental proteins involved in cell proliferation and oncogenic transformation. Recently …