Protein Conformation, beta-Strand
"Protein Conformation, beta-Strand" 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.
A secondary structure of proteins where the amino (N-H) groups of a polypeptide backbone, three to ten amino acids in length, establish hydrogen bonds with the carbonyl (C=O) groups in the backbone of adjacent strands. These may form a beta-sheet, where the side chains of the adjacent strands point in the same direction.
| Descriptor ID |
D000072757
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| MeSH Number(s) |
G02.111.570.820.709.600.750
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| Concept/Terms |
Protein Conformation, beta-Strand- Protein Conformation, beta-Strand
- Conformation, beta-Strand Protein
- Conformations, beta-Strand Protein
- Protein Conformation, beta Strand
- Protein Conformations, beta-Strand
- beta-Strand Protein Conformation
- beta-Strand Protein Conformations
- beta-Strands
- beta Strands
- beta-Stranded Structures
- beta Stranded Structures
- beta-Stranded Structure
- beta-Strand
- beta Strand
beta-Sheet- beta-Sheet
- beta Sheet
- beta-Pleated Sheet
- Sheet, beta-Pleated
- Sheets, beta-Pleated
- beta Pleated Sheet
- beta-Pleated Sheets
- beta-Sheets
- beta Sheets
- Protein Conformation, beta-Sheet
- Conformation, beta-Sheet Protein
- Conformations, beta-Sheet Protein
- Protein Conformation, beta Sheet
- Protein Conformations, beta-Sheet
- beta-Sheet Protein Conformation
- beta-Sheet Protein Conformations
|
Below are MeSH descriptors whose meaning is more general than "Protein Conformation, beta-Strand".
Below are MeSH descriptors whose meaning is more specific than "Protein Conformation, beta-Strand".
This graph shows the total number of publications written about "Protein Conformation, beta-Strand" by people in this website by year, and whether "Protein Conformation, beta-Strand" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2016 | 0 | 1 | 1 |
| 2017 | 0 | 19 | 19 |
| 2018 | 1 | 9 | 10 |
| 2019 | 0 | 4 | 4 |
| 2020 | 0 | 10 | 10 |
| 2021 | 0 | 5 | 5 |
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Below are the most recent publications written about "Protein Conformation, beta-Strand" by people in Profiles.
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In silico identification of novel SARS-COV-2 2'-O-methyltransferase (nsp16) inhibitors: structure-based virtual screening, molecular dynamics simulation and MM-PBSA approaches. J Enzyme Inhib Med Chem. 2021 Dec; 36(1):727-736.
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SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma. Proc Natl Acad Sci U S A. 2021 09 07; 118(36).
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V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity. J Virol. 2021 07 26; 95(16):e0061721.
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Evolutionary insights into the furin cleavage sites of SARS-CoV-2 variants from humans and animals. Arch Virol. 2021 Sep; 166(9):2541-2549.
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Can molecular mimicry explain the cytokine storm of SARS-CoV-2?: An in silico approach. J Med Virol. 2021 Sep; 93(9):5350-5357.
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Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies. Structure. 2021 07 01; 29(7):655-663.e4.
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A metal ion orients SARS-CoV-2 mRNA to ensure accurate 2'-O methylation of its first nucleotide. Nat Commun. 2021 06 02; 12(1):3287.
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Functional landscape of SARS-CoV-2 cellular restriction. Mol Cell. 2021 06 17; 81(12):2656-2668.e8.
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Interaction of small molecules with the SARS-CoV-2 papain-like protease: In silico studies and in vitro validation of protease activity inhibition using an enzymatic inhibition assay. J Mol Graph Model. 2021 05; 104:107851.
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A potential solution to avoid overdose of mixed drugs in the event of Covid-19: Nanomedicine at the heart of the Covid-19 pandemic. J Mol Graph Model. 2021 05; 104:107834.