Title : Rhein exhibits antitumorigenic effects by interfering with the interaction between prolyl isomerase Pin1 and c-Jun.

Pub. Date : 2017 Mar

PMID : 28184937






3 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 The Pin1 protein (or peptidyl-prolyl cis/trans isomerase) specifically catalyzes the cis/trans isomerization of phosphorylated serine/threonine-proline (Ser/Thr-Pro) bonds and plays an important role in many cellular events through the effects of conformational change in the function of c-Jun, its biological substrate. Proline peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens
2 The Pin1 protein (or peptidyl-prolyl cis/trans isomerase) specifically catalyzes the cis/trans isomerization of phosphorylated serine/threonine-proline (Ser/Thr-Pro) bonds and plays an important role in many cellular events through the effects of conformational change in the function of c-Jun, its biological substrate. Proline peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens
3 Since phosphorylation of proteins on Ser/Thr-Pro is a key regulatory mechanism in the control of cell proliferation and transformation, Pin1 has become an attractive molecule in cancer research. Proline peptidylprolyl cis/trans isomerase, NIMA-interacting 1 Homo sapiens