ArticleProceedings of the National Academy of Sciences of the United States of America2020
Properties of protein unfolded states suggest broad selection for expanded conformational ensembles.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
31 citing papers in PubMed, 61 citations in OpenAlex.
- AF-CALVADOS: AlphaFold-guided simulations of multi-domain proteins at the proteome level.Protein science : a publication of the Protein Society · 2026Article
- Cell-Free-Based Thermophilic Biocatalyst for the Synthesis of Amino Acids from One-Carbon Feedstocks.ACS synthetic biology · 2025Article
- Global Analysis of Aggregation Determinants in Small Protein Domains.bioRxiv : the preprint server for biology · 2025Article
- OsmoFold: A high-throughput tool for predicting the impact of osmolytes on protein structure.Biophysical journal · 2025Article
- Identification of an on-pathway intermediate illuminates the kinetic competition between protein folding and misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unfolding of the Villin Headpiece Domain: Revealing Structural Heterogeneity with Time-Resolved X-Ray Solution Scattering and Markov State Modeling.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- piRNA processing within non-membrane structures is governed by constituent proteins and their functional motifs.The FEBS journal · 2025Review
- Measuring the Thermal Unfolding of Lysozyme: A Critical Comparison of Differential Scanning Fluorimetry and Differential Scanning Calorimetry.ChemistryOpen · 2025Article
- Molecular determinants of condensate composition.Molecular cell · 2025Review
- The role of intrinsically disordered regions of SARS-CoV-2 nucleocapsid and non-structural protein 1 proteins.Frontiers in chemistry · 2025Review
- Discovery of an on-pathway protein folding intermediate illuminates the kinetic competition between folding and misfolding.bioRxiv : the preprint server for biology · 2024Article
- Heterogeneous folding landscapes and predetermined breaking points within a protein family.Protein science : a publication of the Protein Society · 2024Article
- Physics-Based Machine Learning Trains Hamiltonians and Decodes the Sequence-Conformation Relation in the Disordered Proteome.Journal of chemical theory and computation · 2024Article
- Unlocking the unfolded structure of ubiquitin: Combining time-resolved x-ray solution scattering and molecular dynamics to generate unfolded ensembles.The Journal of chemical physics · 2024Article
- Intrinsically disordered regions are poised to act as sensors of cellular chemistry.Trends in biochemical sciences · 2023Review
- Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Generation of unfolded outer membrane protein ensembles defined by hydrodynamic properties.European biophysics journal : EBJ · 2023Article
- Getting Smaller by Denaturation: Acid-Induced Compaction of Antibodies.The journal of physical chemistry letters · 2023Article
- Interpreting Transient Interactions of Intrinsically Disordered Proteins.The journal of physical chemistry. B · 2023Article
- Deep mining of the protein energy landscape.Structural dynamics (Melville, N.Y.) · 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
7 authors at 2 institutions in 1 country.
Funding
Abstract
Much attention is being paid to conformational biases in the ensembles of intrinsically disordered proteins. However, it is currently unknown whether or how conformational biases within the disordered ensembles of foldable proteins affect function in vivo. Recently, we demonstrated that water can be a good solvent for unfolded polypeptide chains, even those with a hydrophobic and charged sequence composition typical of folded proteins. These results run counter to the generally accepted model that protein folding begins with hydrophobicity-driven chain collapse. Here we investigate what other features, beyond amino acid composition, govern chain collapse. We found that local clustering of hydrophobic and/or charged residues leads to significant collapse of the unfolded ensemble of pertactin, a secreted autotransporter virulence protein from
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.