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
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| MeSH Number(s) |
D08.811.399.325.500.700
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| 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
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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.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2012 | 0 | 2 | 2 |
| 2013 | 0 | 3 | 3 |
| 2017 | 1 | 0 | 1 |
| 2020 | 0 | 1 | 1 |
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Below are the most recent publications written about "NIMA-Interacting Peptidylprolyl Isomerase" by people in Profiles.
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Luo ML, Zheng F, Chen W, Liang ZM, Chandramouly G, Tan J, Willis NA, Chen CH, Taveira MO, Zhou XZ, Lu KP, Scully R, Wulf GM, Hu H. Inactivation of the Prolyl Isomerase Pin1 Sensitizes BRCA1-Proficient Breast Cancer to PARP Inhibition. Cancer Res. 2020 07 15; 80(14):3033-3045.
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Xu L, Ren Z, Chow FE, Tsai R, Liu T, Rizzolio F, Boffo S, Xu Y, Huang S, Lippa CF, Gong Y. Pathological Role of Peptidyl-Prolyl Isomerase Pin1 in the Disruption of Synaptic Plasticity in Alzheimer's Disease. Neural Plast. 2017; 2017:3270725.
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La Montagna R, Caligiuri I, Giordano A, Rizzolio F. Pin1 and nuclear receptors: a new language? J Cell Physiol. 2013 Sep; 228(9):1799-801.
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Lucchetti C, Caligiuri I, Toffoli G, Giordano A, Rizzolio F. The prolyl isomerase Pin1 acts synergistically with CDK2 to regulate the basal activity of estrogen receptor a in breast cancer. PLoS One. 2013; 8(2):e55355.
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Rizzolio F, Caligiuri I, Lucchetti C, Fratamico R, Tomei V, Gallo G, Agelan A, Ferrari G, Toffoli G, Klein-Szanto AJ, Giordano A. Dissecting Pin1 and phospho-pRb regulation. J Cell Physiol. 2013 Jan; 228(1):73-7.
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La Montagna R, Caligiuri I, Maranta P, Lucchetti C, Esposito L, Paggi MG, Toffoli G, Rizzolio F, Giordano A. Androgen receptor serine 81 mediates Pin1 interaction and activity. Cell Cycle. 2012 Sep 15; 11(18):3415-20.
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Rizzolio F, Lucchetti C, Caligiuri I, Marchesi I, Caputo M, Klein-Szanto AJ, Bagella L, Castronovo M, Giordano A. Retinoblastoma tumor-suppressor protein phosphorylation and inactivation depend on direct interaction with Pin1. Cell Death Differ. 2012 Jul; 19(7):1152-61.