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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

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)

G02.111.570.790.709.600.040.752

Concept/Terms

Proline-Rich Protein Domains

Proline-Rich Peptide Domains

Below are MeSH descriptors whose meaning is more general than "Proline-Rich Protein Domains".

Biological Sciences [G]
Chemical Phenomena [G02]
Biochemical Phenomena [G02.111]
Molecular Structure [G02.111.570]
Molecular Conformation [G02.111.570.790]
Protein Conformation [G02.111.570.790.709]
Protein Structure, Secondary [G02.111.570.790.709.600]
Amino Acid Motifs [G02.111.570.790.709.600.040]
Proline-Rich Protein Domains [G02.111.570.790.709.600.040.752]

Below are MeSH descriptors whose meaning is related to "Proline-Rich Protein Domains".

Below are MeSH descriptors whose meaning is more specific than "Proline-Rich Protein Domains".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Proline-Rich Protein Domains" by people in Harvard Catalyst Profiles by year, and whether "Proline-Rich Protein Domains" was a major or minor topic of these publication.

Bar chart showing 7 publications over 6 distinct years, with a maximum of 2 publications in 2019

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
1994	0	1	1
1996	0	1	1
2012	0	1	1
2014	0	1	1
2017	0	1	1
2019	1	1	2

Below are the most recent publications written about "Proline-Rich Protein Domains" by people in Profiles.

Polyphosphate Initiates Tau Aggregation through Intra- and Intermolecular Scaffolding. Biophys J. 2019 08 20; 117(4):717-728.

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The integrity of the FOG-2 LXCXE pRb-binding motif is required for small intestine homeostasis. Exp Physiol. 2019 07; 104(7):1074-1089.

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Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain. RNA. 2017 06; 23(6):968-981.

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Multimerization of a Proline-Rich Antimicrobial Peptide, Chex-Arg20, Alters Its Mechanism of Interaction with the Escherichia coli Membrane. Chem Biol. 2015 Sep 17; 22(9):1250-8.

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Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria. Amino Acids. 2014 Oct; 46(10):2287-94.

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Proline-rich region of non-muscle myosin light chain kinase modulates kinase activity and endothelial cytoskeletal dynamics. Microvasc Res. 2014 Sep; 95:94-102.

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AKAP79 modulation of L-type channels involves disruption of intramolecular interactions in the CaV1.2 subunit. Channels (Austin). 2012 May-Jun; 6(3):157-65.

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Phase transitions in the assembly of multivalent signalling proteins. Nature. 2012 Mar 07; 483(7389):336-40.

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Mechanism of host cell MAPK/ERK-2 incorporation into lentivirus particles: characterization of the interaction between MAPK/ERK-2 and proline-rich-domain containing capsid region of structural protein Gag. J Mol Biol. 2011 Jul 22; 410(4):681-97.

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Conformational changes in salivary proline-rich protein 1 upon adsorption to calcium phosphate crystals. Langmuir. 2007 Oct 23; 23(22):11200-5.

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