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 |
|---|
| 2002 | 0 | 1 | 1 |
| 2007 | 0 | 1 | 1 |
| 2013 | 0 | 1 | 1 |
| 2017 | 1 | 0 | 1 |
| 2020 | 0 | 1 | 1 |
| 2021 | 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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Cis P-tau underlies vascular contribution to cognitive impairment and dementia and can be effectively targeted by immunotherapy in mice. Sci Transl Med. 2021 06 02; 13(596).
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A Hyperactive RelA/p65-Hexokinase 2 Signaling Axis Drives Primary Central Nervous System Lymphoma. Cancer Res. 2020 12 01; 80(23):5330-5343.
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Pin1 Knockout Mice: A Model for the Study of Tau Pathology in Alzheimer's Disease. Methods Mol Biol. 2017; 1523:415-425.
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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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Negative regulation of Pim-1 protein kinase levels by the B56beta subunit of PP2A. Oncogene. 2007 Aug 02; 26(35):5145-53.
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Proteasomal degradation of human peptidyl prolyl isomerase pin1-pointing phospho Bcl2 toward dephosphorylation. Neoplasia. 2002 May-Jun; 4(3):218-27.