Proline-Rich Protein Domains
"Proline-Rich Protein Domains" 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.
Protein domains that are enriched in PROLINE. The cyclical nature of proline causes the peptide bonds it forms to have a limited degree of conformational mobility. Therefore the presence of multiple prolines in close proximity to each other can convey a distinct conformational arrangement to a peptide chain.
| Descriptor ID |
D055232
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| MeSH Number(s) |
G02.111.570.820.709.275.750.485
|
| Concept/Terms |
Proline-Rich Protein Domains- Proline-Rich Protein Domains
- Domain, Proline-Rich Protein
- Domains, Proline-Rich Protein
- Proline Rich Protein Domains
- Proline-Rich Protein Domain
- Protein Domain, Proline-Rich
- Protein Domains, Proline-Rich
Proline-Rich Peptide Domains- Proline-Rich Peptide Domains
- Domain, Proline-Rich Peptide
- Domains, Proline-Rich Peptide
- Peptide Domain, Proline-Rich
- Peptide Domains, Proline-Rich
- Proline Rich Peptide Domains
- Proline-Rich Peptide Domain
|
Below are MeSH descriptors whose meaning is more general than "Proline-Rich Protein Domains".
Below are MeSH descriptors whose meaning is more specific than "Proline-Rich Protein Domains".
This graph shows the total number of publications written about "Proline-Rich Protein Domains" by people in this website by year, and whether "Proline-Rich Protein Domains" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2000 | 0 | 1 | 1 |
| 2005 | 0 | 1 | 1 |
| 2007 | 0 | 1 | 1 |
| 2010 | 0 | 1 | 1 |
| 2013 | 0 | 1 | 1 |
| 2016 | 0 | 1 | 1 |
| 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Proline-Rich Protein Domains" by people in Profiles.
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Harris DC, Garcia YA, Samaniego CS, Rowlett VW, Ortiz NR, Payan AN, Maehigashi T, Cox MB. Functional Comparison of Human and Zebra Fish FKBP52 Confirms the Importance of the Proline-Rich Loop for Regulation of Steroid Hormone Receptor Activity. Int J Mol Sci. 2019 Oct 28; 20(21).
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Kawprasertsri S, Pietras RJ, Marquez-Garban DC, Boonyaratanakornkit V. Progesterone receptor (PR) polyproline domain (PPD) mediates inhibition of epidermal growth factor receptor (EGFR) signaling in non-small cell lung cancer cells. Cancer Lett. 2016 May 01; 374(2):279-91.
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Zanforlin T, Bayer-Santos E, Cortez C, Almeida IC, Yoshida N, da Silveira JF. Molecular characterization of Trypanosoma cruzi SAP proteins with host-cell lysosome exocytosis-inducing activity required for parasite invasion. PLoS One. 2013; 8(12):e83864.
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Barylko B, Wang L, Binns DD, Ross JA, Tassin TC, Collins KA, Jameson DM, Albanesi JP. The proline/arginine-rich domain is a major determinant of dynamin self-activation. Biochemistry. 2010 Dec 21; 49(50):10592-4.
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Herr RA, Hung CY, Cole GT. Evaluation of two homologous proline-rich proteins of Coccidioides posadasii as candidate vaccines against coccidioidomycosis. Infect Immun. 2007 Dec; 75(12):5777-87.
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Lan Z, Kurata WE, Martyn KD, Jin C, Lau AF. Novel rab GAP-like protein, CIP85, interacts with connexin43 and induces its degradation. Biochemistry. 2005 Feb 22; 44(7):2385-96.
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Yudowski GA, Efendiev R, Pedemonte CH, Katz AI, Berggren PO, Bertorello AM. Phosphoinositide-3 kinase binds to a proline-rich motif in the Na+, K+-ATPase alpha subunit and regulates its trafficking. Proc Natl Acad Sci U S A. 2000 Jun 06; 97(12):6556-61.