ReviewProteomes2014
Dynamic New World: Refining Our View of Protein Structure, Function and Evolution.
Review in Proteomes, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed.
- Nitroxide spin, non-canonical amino acids and SDSL-EPR spectroscopy: a winning combination for protein dynamics studies.European biophysics journal : EBJ · 2026Article
- Article
- Benchmarking Free Energy Calculations: Analysis of Single and Double Mutations Across Two Simulation Software Platforms for Two Protein Systems.bioRxiv : the preprint server for biology · 2025Article
- Conformational modulation of intrinsically disordered transactivation domains for cancer therapy.PNAS nexus · 2025Review
- Intrinsic Disorder and Other Malleable Arsenals of Evolved Protein Multifunctionality.Journal of molecular evolution · 2024Review
- Kinetic coherence underlies the dynamics of disordered proteins.RSC advances · 2021Article
- What's in a name? From "fluctuation fit" to "conformational selection": rediscovery of a concept.History and philosophy of the life sciences · 2021Article
- Selective cross-linking of coinciding protein assemblies by in-gel cross-linking mass spectrometry.The EMBO journal · 2021Article
- Improving the Accuracy of Protein Thermostability Predictions for Single Point Mutations.Biophysical journal · 2020Article
- Reduced alphabet of prebiotic amino acids optimally encodes the conformational space of diverse extant protein folds.BMC evolutionary biology · 2019Article
- Evolution of a novel chimeric maltotriose transporter in Saccharomyces eubayanus from parent proteins unable to perform this function.PLoS genetics · 2019Article
- The BackMAP Python module: how a simpler Ramachandran number can simplify the life of a protein simulator.PeerJ · 2018Article
- An exhaustive survey of regular peptide conformations using a new metric for backbone handedness (PeerJ · 2017Article
- Article
- Article
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
No grant is acknowledged in the PubMed record.
Abstract
Proteins are crucial to the functioning of all lifeforms. Traditional understanding posits that a single protein occupies a single structure ("fold"), which performs a single function. This view is radically challenged with the recognition that high structural dynamism-the capacity to be extra "floppy"-is more prevalent in functional proteins than previously assumed. As reviewed here, this dynamic take on proteins affects our understanding of protein "structure", function, and evolution, and even gives us a glimpse into protein origination. Specifically, this review will discuss historical developments concerning protein structure, and important new relationships between dynamism and aspects of protein sequence, structure, binding modes, binding promiscuity, evolvability, and origination. Along the way, suggestions will be provided for how key parts of textbook definitions-that so far have excluded membership to intrinsically disordered proteins (IDPs)-could be modified to accommodate our more dynamic understanding of proteins.
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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.