"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.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1999 | 0 | 1 | 1 |
| 2000 | 0 | 3 | 3 |
| 2001 | 0 | 3 | 3 |
| 2002 | 0 | 7 | 7 |
| 2003 | 0 | 4 | 4 |
| 2004 | 0 | 2 | 2 |
| 2005 | 0 | 9 | 9 |
| 2006 | 0 | 1 | 1 |
| 2007 | 1 | 2 | 3 |
| 2010 | 0 | 5 | 5 |
| 2011 | 0 | 1 | 1 |
| 2012 | 0 | 8 | 8 |
| 2013 | 1 | 1 | 2 |
| 2014 | 0 | 2 | 2 |
| 2016 | 0 | 2 | 2 |
| 2017 | 0 | 2 | 2 |
| 2018 | 0 | 1 | 1 |
| 2019 | 0 | 1 | 1 |
| 2020 | 1 | 1 | 2 |
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Below are the most recent publications written about "Amino Acid Motifs" by people in Profiles.
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A Key Motif in the Cholesterol-Dependent Cytolysins Reveals a Large Family of Related Proteins. mBio. 2020 09 29; 11(5).
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Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation. J Bacteriol. 2020 07 09; 202(15).
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Influence of interfacial tryptophan residues on an arginine-flanked transmembrane helix. Biochim Biophys Acta Biomembr. 2020 02 01; 1862(2):183134.
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Ehrlichia type IV secretion system effector Etf-2 binds to active RAB5 and delays endosome maturation. Proc Natl Acad Sci U S A. 2018 09 18; 115(38):E8977-E8986.
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The Intergenic Recombinant HLA-B*46:01 Has a Distinctive Peptidome that Includes KIR2DL3 Ligands. Cell Rep. 2017 05 16; 19(7):1394-1405.
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An engineered transforming growth factor ß (TGF-ß) monomer that functions as a dominant negative to block TGF-ß signaling. J Biol Chem. 2017 04 28; 292(17):7173-7188.
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Hyaluronan synthase control of synthesis rate and hyaluronan product size are independent functions differentially affected by mutations in a conserved tandem B-X7-B motif. Glycobiology. 2017 01; 27(2):154-164.
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Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins. Structure. 2016 09 06; 24(9):1488-98.
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Calcitonin and Amylin Receptor Peptide Interaction Mechanisms: INSIGHTS INTO PEPTIDE-BINDING MODES AND ALLOSTERIC MODULATION OF THE CALCITONIN RECEPTOR BY RECEPTOR ACTIVITY-MODIFYING PROTEINS. J Biol Chem. 2016 Apr 15; 291(16):8686-700.
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Lysine Acetylation Activates Mitochondrial Aconitase in the Heart. Biochemistry. 2015 Jun 30; 54(25):4008-18.