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 |
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2002 | 0 | 1 | 1 |
2017 | 2 | 0 | 2 |
2018 | 1 | 1 | 2 |
2019 | 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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Suppression of c-Myc using 10058-F4 exerts caspase-3-dependent apoptosis and intensifies the antileukemic effect of vincristine in pre-B acute lymphoblastic leukemia cells. J Cell Biochem. 2019 08; 120(8):14004-14016.
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Pin1 Is Involved in HDAC6-mediated Cancer Cell Motility. Int J Med Sci. 2018; 15(13):1573-1581.
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A metabolic function of FGFR3-TACC3 gene fusions in cancer. Nature. 2018 01 11; 553(7687):222-227.
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Conjugates of 18ß-glycyrrhetinic acid derivatives with 3-(1H-benzo[d]imidazol-2-yl)propanoic acid as Pin1 inhibitors displaying anti-prostate cancer ability. Bioorg Med Chem. 2017 10 15; 25(20):5441-5451.
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The Essential Role of Pin1 via NF-?B Signaling in Vascular Inflammation and Atherosclerosis in ApoE-/- Mice. Int J Mol Sci. 2017 Mar 16; 18(3).
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Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus. Antiviral Res. 2016 Feb; 126:1-7.
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Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes. Proc Natl Acad Sci U S A. 2002 Feb 05; 99(3):1335-40.