 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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| 2007 | 0 | 1 | 1 | | 2009 | 0 | 1 | 1 | | 2017 | 1 | 0 | 1 | | 2018 | 1 | 0 | 1 | | 2019 | 1 | 0 | 1 | | 2020 | 1 | 1 | 2 | | 2021 | 1 | 0 | 1 | | 2022 | 1 | 1 | 2 | | 2023 | 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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Lee E, Redzic JS, Saviola AJ, Li X, Ebmeier CC, Kutateladze TG, Hansen KC, Zhao R, Ahn N, Sluchanko NN, Eisenmesser E. Molecular insight into the specific interactions of the SARS-Coronavirus-2 nucleocapsid with RNA and host protein. Protein Sci. 2023 04; 32(4):e4603.
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Nashaat S, Henen MA, El-Messery SM, Eisa H. New Benzimidazoles Targeting Breast Cancer: Synthesis, Pin1 Inhibition, 2D NMR Binding, and Computational Studies. Molecules. 2022 Aug 17; 27(16).
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Born A, Soetbeer J, Henen MA, Breitgoff F, Polyhach Y, Jeschke G, V?geli B. Ligand-specific conformational change drives interdomain allostery in Pin1. Nat Commun. 2022 08 04; 13(1):4546.
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Born A, Soetbeer J, Breitgoff F, Henen MA, Sgourakis N, Polyhach Y, Nichols PJ, Strotz D, Jeschke G, V?geli B. Reconstruction of Coupled Intra- and Interdomain Protein Motion from Nuclear and Electron Magnetic Resonance. J Am Chem Soc. 2021 10 06; 143(39):16055-16067.
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Nichols PJ, Born A, Henen MA, Strotz D, Jones DN, Delaglio F, V?geli B. Reducing the measurement time of exact NOEs by non-uniform sampling. J Biomol NMR. 2020 Dec; 74(12):717-739.
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Nashaat S, Henen MA, El-Messery SM, Eisa H. Synthesis, state-of-the-art NMR-binding and molecular modeling study of new benzimidazole core derivatives as Pin1 inhibitors: Targeting breast cancer. Bioorg Med Chem. 2020 06 01; 28(11):115495.
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Born A, Henen MA, V?geli B. Activity and Affinity of Pin1 Variants. Molecules. 2019 Dec 20; 25(1).
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Born A, Nichols PJ, Henen MA, Chi CN, Strotz D, Bayer P, Tate SI, Peng JW, V?geli B. Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery. Biomol NMR Assign. 2019 04; 13(1):85-89.
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Nichols PJ, Born A, Henen MA, Strotz D, Orts J, Olsson S, G?ntert P, Chi CN, V?geli B. The Exact Nuclear Overhauser Enhancement: Recent Advances. Molecules. 2017 Jul 14; 22(7).
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Eichner T, Kutter S, Labeikovsky W, Buosi V, Kern D. Molecular Mechanism of Pin1-Tau Recognition and Catalysis. J Mol Biol. 2016 05 08; 428(9 Pt A):1760-75.
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