NIMA-Interacting Peptidylprolyl Isomerase
"NIMA-Interacting Peptidylprolyl Isomerase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A highly-conserved peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated SERINE- or THREONINE-PROLINE (pSer/Thr-Pro) motifs and causes conformational changes in certain proteins associated with the CELL CYCLE. It displays a preference for an acidic residue N-terminal to the isomerized proline bond and regulates MITOSIS, possibly by attenuating the mitosis-promoting activity of NIMA-RELATED KINASE 1.
| Descriptor ID |
D000072340
|
| MeSH Number(s) |
D08.811.399.325.500.700
|
| Concept/Terms |
NIMA-Interacting Peptidylprolyl Isomerase- NIMA-Interacting Peptidylprolyl Isomerase
- Isomerase, NIMA-Interacting Peptidylprolyl
- NIMA Interacting Peptidylprolyl Isomerase
- Peptidylprolyl Isomerase, NIMA-Interacting
- PIN1 Protein
- Pin1 Peptidylprolyl Isomerase
- Isomerase, Pin1 Peptidylprolyl
- Peptidylprolyl Isomerase, Pin1
- Peptidyl-Prolyl Cis-Trans Isomerase Pin1
- Peptidyl Prolyl Cis Trans Isomerase Pin1
|
Below are MeSH descriptors whose meaning is more general than "NIMA-Interacting Peptidylprolyl Isomerase".
Below are MeSH descriptors whose meaning is more specific than "NIMA-Interacting Peptidylprolyl Isomerase".
This graph shows the total number of publications written about "NIMA-Interacting Peptidylprolyl Isomerase" by people in this website by year, and whether "NIMA-Interacting Peptidylprolyl Isomerase" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2002 | 0 | 1 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "NIMA-Interacting Peptidylprolyl Isomerase" by people in Profiles.
-
Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions. J Biol Chem. 2002 Jun 21; 277(25):23054-64.