"Amino Acid Motifs" 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.
Three-dimensional protein structural elements that are composed of a combination of secondary structures. They include HELIX-LOOP-HELIX MOTIFS and ZINC FINGERS. Motifs are typically the most conserved regions of PROTEIN DOMAINS and are critical for domain function. However, the same motif may occur in proteins or enzymes with different functions.
| Descriptor ID |
D020816
|
| MeSH Number(s) |
G02.111.570.820.709.275.500 G02.111.570.820.709.600.500
|
| Concept/Terms |
Amino Acid Motifs- Amino Acid Motifs
- Amino Acid Motif
- Motif, Amino Acid
- Motifs, Amino Acid
- Protein Motifs
- Motif, Protein
- Motifs, Protein
- Protein Motif
Protein Structure, Supersecondary- Protein Structure, Supersecondary
- Protein Structures, Supersecondary
- Supersecondary Protein Structures
- Supersecondary Protein Structure
|
Below are MeSH descriptors whose meaning is more general than "Amino Acid Motifs".
Below are MeSH descriptors whose meaning is more specific than "Amino Acid Motifs".
This graph shows the total number of publications written about "Amino Acid Motifs" by people in this website by year, and whether "Amino Acid Motifs" was a major or minor topic of these publications.
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click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2000 | 0 | 4 | 4 |
| 2001 | 0 | 3 | 3 |
| 2002 | 0 | 2 | 2 |
| 2003 | 0 | 3 | 3 |
| 2004 | 0 | 3 | 3 |
| 2005 | 0 | 3 | 3 |
| 2006 | 0 | 7 | 7 |
| 2007 | 0 | 2 | 2 |
| 2008 | 0 | 4 | 4 |
| 2009 | 0 | 5 | 5 |
| 2010 | 1 | 2 | 3 |
| 2011 | 0 | 4 | 4 |
| 2012 | 0 | 2 | 2 |
| 2013 | 0 | 1 | 1 |
| 2014 | 0 | 4 | 4 |
| 2015 | 0 | 4 | 4 |
| 2016 | 0 | 1 | 1 |
| 2017 | 0 | 5 | 5 |
| 2018 | 0 | 2 | 2 |
| 2019 | 0 | 1 | 1 |
| 2021 | 1 | 3 | 4 |
| 2022 | 0 | 1 | 1 |
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Below are the most recent publications written about "Amino Acid Motifs" by people in Profiles.
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Structure of the Acinetobacter baumannii PmrA receiver domain and insights into clinical mutants affecting DNA binding and promoting colistin resistance. J Biochem. 2022 Jan 07; 170(6):787-800.
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Genetic fusions favor tumorigenesis through degron loss in oncogenes. Nat Commun. 2021 11 18; 12(1):6704.
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Structure-Function Analysis of Two Interacting Vaccinia Proteins That Are Critical for Viral Morphogenesis: L2 and A30.5. J Virol. 2022 01 26; 96(2):e0157721.
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The intrinsic kinase activity of BRD4 spans its BD2-B-BID domains. J Biol Chem. 2021 11; 297(5):101326.
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Sec24C is an HIV-1 host dependency factor crucial for virus replication. Nat Microbiol. 2021 04; 6(4):435-444.
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An intramembrane sensory circuit monitors sortase A-mediated processing of streptococcal adhesins. Sci Signal. 2019 05 07; 12(580).
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Control of mRNA decapping by autoinhibition. Nucleic Acids Res. 2018 07 06; 46(12):6318-6329.
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Nonnative Energetic Frustrations in Protein Folding at Residual Level: A Simulation Study of Homologous Immunoglobulin-like ?-Sandwich Proteins. Int J Mol Sci. 2018 May 18; 19(5).
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The ShcD phosphotyrosine adaptor subverts canonical EGF receptor trafficking. J Cell Sci. 2017 Sep 01; 130(17):2808-2820.
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Two EF-hand motifs in ryanodine receptor calcium release channels contribute to isoform-specific regulation by calmodulin. Cell Calcium. 2017 09; 66:62-70.