ReviewInternational journal of molecular sciences2022
A Perspective on the (Rise and Fall of) Protein β-Turns.
Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed.
- Green Fabrication of Keratin Nanoparticles from Yak Horn by Steam Flash Explosion: Structure-Property Evolution.Biomolecules · 2026Article
- Simulation of CRISPR/Cas9-mediated gene editing for the Vitellogenin gene in Apis mellifera.Scientific reports · 2026Article
- Advancements in Loop Cyclization Approaches for Enhanced Peptide Therapeutics for Targeting Protein-Protein Interactions.The Journal of organic chemistry · 2025Article
- Geometric descriptors for beta turns.Protein science : a publication of the Protein Society · 2024Article
- Peptide-Mediated Nanocarriers for Targeted Drug Delivery: Developments and Strategies.Pharmaceutics · 2024Review
- Emerging role of carbonyl-carbonyl interactions in the classification of beta turns.Protein science : a publication of the Protein Society · 2024Article
- β-Turn Induction by a Diastereopure Azepane-Derived Quaternary Amino Acid.The Journal of organic chemistry · 2023Article
- Progress of the "Molecular Informatics" Section in 2022.International journal of molecular sciences · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
The β-turn is the third defined secondary structure after the α-helix and the β-sheet. The β-turns were described more than 50 years ago and account for more than 20% of protein residues. Nonetheless, they are often overlooked or even misunderstood. This poor knowledge of these local protein conformations is due to various factors, causes that I discuss here. For example, confusion still exists about the assignment of these local protein structures, their overlaps with other structures, the potential absence of a stabilizing hydrogen bond, the numerous types of β-turns and the software's difficulty in assigning or visualizing them. I also propose some ideas to potentially/partially remedy this and present why β-turns can still be helpful, even in the AlphaFold 2 era.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.