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
|
| 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 |
|---|
| 1997 | 0 | 1 | 1 |
| 2008 | 0 | 1 | 1 |
| 2010 | 0 | 1 | 1 |
| 2018 | 1 | 0 | 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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De novo apparent loss-of-function mutations in PRR12 in three patients with intellectual disability and iris abnormalities. Hum Genet. 2018 Mar; 137(3):257-264.
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Decoding the intrinsic mechanism that prohibits ALIX interaction with ESCRT and viral proteins. Biochem J. 2010 Dec 15; 432(3):525-34.
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Inhibition of Wnt signaling by the osteoblast-specific transcription factor Osterix. Proc Natl Acad Sci U S A. 2008 May 13; 105(19):6936-41.
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The SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28. J Immunol. 1997 Oct 01; 159(7):3220-9.