"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
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MeSH Number(s) |
G02.111.570.820.709.275.500 G02.111.570.820.709.600.500
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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
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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 |
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2003 | 0 | 1 | 1 |
2004 | 0 | 4 | 4 |
2005 | 1 | 1 | 2 |
2006 | 0 | 6 | 6 |
2007 | 0 | 2 | 2 |
2008 | 0 | 3 | 3 |
2009 | 0 | 1 | 1 |
2010 | 0 | 1 | 1 |
2011 | 0 | 1 | 1 |
2012 | 0 | 2 | 2 |
2013 | 0 | 6 | 6 |
2014 | 0 | 3 | 3 |
2015 | 0 | 2 | 2 |
2016 | 0 | 4 | 4 |
2017 | 1 | 24 | 25 |
2018 | 4 | 19 | 23 |
2019 | 0 | 4 | 4 |
2020 | 0 | 6 | 6 |
2021 | 0 | 5 | 5 |
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Below are the most recent publications written about "Amino Acid Motifs" by people in Profiles.
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Variable posttranslational modifications of severe acute respiratory syndrome coronavirus 2 nucleocapsid protein. Glycobiology. 2021 09 20; 31(9):1080-1092.
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Sequence requirements of the FFAT-like motif for specific binding to VAP-A are revealed by NMR. FEBS Lett. 2021 09; 595(17):2248-2256.
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The ß-link motif in protein architecture. Acta Crystallogr D Struct Biol. 2021 Aug 01; 77(Pt 8):1040-1049.
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The Antiviral Effect of the Chemical Compounds Targeting DED/EDh Motifs of the Viral Proteins on Lymphocytic Choriomeningitis Virus and SARS-CoV-2. Viruses. 2021 06 24; 13(7).
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Emergence and spread of a SARS-CoV-2 lineage A variant (A.23.1) with altered spike protein in Uganda. Nat Microbiol. 2021 08; 6(8):1094-1101.
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Fe-S cofactors in the SARS-CoV-2 RNA-dependent RNA polymerase are potential antiviral targets. Science. 2021 07 09; 373(6551):236-241.
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A weak COPI binding motif in the cytoplasmic tail of SARS-CoV-2 spike glycoprotein is necessary for its cleavage, glycosylation, and localization. FEBS Lett. 2021 07; 595(13):1758-1767.
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Arginine methylation of SARS-Cov-2 nucleocapsid protein regulates RNA binding, its ability to suppress stress granule formation, and viral replication. J Biol Chem. 2021 07; 297(1):100821.
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CD8+ T cells specific for an immunodominant SARS-CoV-2 nucleocapsid epitope display high naive precursor frequency and TCR promiscuity. Immunity. 2021 05 11; 54(5):1066-1082.e5.
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Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells. Viruses. 2021 03 25; 13(4).