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 |
---|
1997 | 0 | 1 | 1 |
1998 | 0 | 1 | 1 |
2000 | 0 | 1 | 1 |
2003 | 0 | 4 | 4 |
2004 | 0 | 2 | 2 |
2005 | 0 | 3 | 3 |
2006 | 0 | 1 | 1 |
2007 | 0 | 3 | 3 |
2008 | 0 | 2 | 2 |
2009 | 0 | 4 | 4 |
2011 | 0 | 5 | 5 |
2012 | 0 | 4 | 4 |
2013 | 0 | 1 | 1 |
2014 | 0 | 2 | 2 |
2016 | 1 | 1 | 2 |
2019 | 1 | 0 | 1 |
2024 | 1 | 0 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "NIMA-Interacting Peptidylprolyl Isomerase" by people in Profiles.
-
Stereospecific NANOG PEST Stabilization by Pin1. Biochemistry. 2024 05 07; 63(9):1067-1074.
-
An IRAK1-PIN1 signalling axis drives intrinsic tumour resistance to radiation therapy. Nat Cell Biol. 2019 02; 21(2):203-213.
-
ERK Activation Globally Downregulates miRNAs through Phosphorylating Exportin-5. Cancer Cell. 2016 Nov 14; 30(5):723-736.
-
Mitochondria-Translocated PGK1 Functions as a Protein Kinase to Coordinate Glycolysis and the TCA Cycle in Tumorigenesis. Mol Cell. 2016 Mar 03; 61(5):705-719.
-
SCP phosphatases suppress renal cell carcinoma by stabilizing PML and inhibiting mTOR/HIF signaling. Cancer Res. 2014 Dec 01; 74(23):6935-46.
-
Chlamydia trachomatis-induced alterations in the host cell proteome are required for intracellular growth. Cell Host Microbe. 2014 Jan 15; 15(1):113-24.
-
The prolyl isomerase pin1 regulates mRNA levels of genes with short half-lives by targeting specific RNA binding proteins. PLoS One. 2014; 9(1):e85427.
-
The peptidyl-prolyl isomerase Pin1 up-regulation and proapoptotic function in dopaminergic neurons: relevance to the pathogenesis of Parkinson disease. J Biol Chem. 2013 Jul 26; 288(30):21955-71.
-
Pin1 regulates the dynamics of c-Myc DNA binding to facilitate target gene regulation and oncogenesis. Mol Cell Biol. 2013 Aug; 33(15):2930-49.
-
SENP1 deSUMOylates and regulates Pin1 protein activity and cellular function. Cancer Res. 2013 Jul 01; 73(13):3951-62.