Protein Structure, Quaternary
"Protein Structure, Quaternary" 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.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
Descriptor ID |
D020836
|
MeSH Number(s) |
G02.111.570.820.709.550
|
Concept/Terms |
Protein Structure, Quaternary- Protein Structure, Quaternary
- Protein Structures, Quaternary
- Quaternary Protein Structures
- Quaternary Protein Structure
|
Below are MeSH descriptors whose meaning is more general than "Protein Structure, Quaternary".
Below are MeSH descriptors whose meaning is more specific than "Protein Structure, Quaternary".
This graph shows the total number of publications written about "Protein Structure, Quaternary" by people in this website by year, and whether "Protein Structure, Quaternary" 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 |
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2003 | 0 | 1 | 1 |
2004 | 0 | 3 | 3 |
2005 | 1 | 0 | 1 |
2006 | 1 | 0 | 1 |
2007 | 0 | 1 | 1 |
2008 | 1 | 1 | 2 |
2010 | 0 | 1 | 1 |
2011 | 0 | 2 | 2 |
2012 | 0 | 1 | 1 |
2013 | 0 | 1 | 1 |
2016 | 0 | 3 | 3 |
2017 | 0 | 10 | 10 |
2018 | 2 | 8 | 10 |
2019 | 0 | 2 | 2 |
2020 | 0 | 3 | 3 |
2021 | 0 | 8 | 8 |
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Below are the most recent publications written about "Protein Structure, Quaternary" by people in Profiles.
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Impact of temperature on the affinity of SARS-CoV-2 Spike glycoprotein for host ACE2. J Biol Chem. 2021 10; 297(4):101151.
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Water-Triggered, Irreversible Conformational Change of SARS-CoV-2 Main Protease on Passing from the Solid State to Aqueous Solution. J Am Chem Soc. 2021 08 25; 143(33):12930-12934.
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The method utilized to purify the SARS-CoV-2 N protein can affect its molecular properties. Int J Biol Macromol. 2021 Oct 01; 188:391-403.
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Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity. Science. 2021 08 06; 373(6555).
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A Trimeric Hydrophobic Zipper Mediates the Intramembrane Assembly of SARS-CoV-2 Spike. J Am Chem Soc. 2021 06 16; 143(23):8543-8546.
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Comparative protein structure network analysis on 3CLpro from SARS-CoV-1 and SARS-CoV-2. Proteins. 2021 09; 89(9):1216-1225.
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Comparative Perturbation-Based Modeling of the SARS-CoV-2 Spike Protein Binding with Host Receptor and Neutralizing Antibodies: Structurally Adaptable Allosteric Communication Hotspots Define Spike Sites Targeted by Global Circulating Mutations. Biochemistry. 2021 05 18; 60(19):1459-1484.
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Structural insight into SARS-CoV-2 neutralizing antibodies and modulation of syncytia. Cell. 2021 06 10; 184(12):3192-3204.e16.
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B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV. Cell. 2021 06 10; 184(12):3205-3221.e24.
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The SARS-CoV-2 Spike variant D614G favors an open conformational state. Sci Adv. 2021 04; 7(16).