ReviewIntrinsically disordered proteins
Designing disorder: Tales of the unexpected tails.
Review in Intrinsically disordered proteins. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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Who cites it
11 citing papers in PubMed.
- DispHScan: A Multi-Sequence Web Tool for Predicting Protein Disorder as a Function of pH.Biomolecules · 2021Article
- Toward Cancer Diagnostics of the Tumor Suppressor p53 by Surface Enhanced Raman Spectroscopy.Sensors (Basel, Switzerland) · 2020Review
- Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins.International journal of molecular sciences · 2020Review
- DispHred: A Server to Predict pH-Dependent Order-Disorder Transitions in Intrinsically Disordered Proteins.International journal of molecular sciences · 2020Article
- Simultaneous sensing and imaging of individual biomolecular complexes enabled by modular DNA-protein coupling.Communications chemistry · 2020Article
- Biotin proximity tagging favours unfolded proteins and enables the study of intrinsically disordered regions.Communications biology · 2020Article
- Structural and Functional Properties of the Capsid Protein of Dengue and RelatedInternational journal of molecular sciences · 2019Article
- Raman Evidence of p53-DBD Disorder Decrease upon Interaction with the Anticancer Protein Azurin.International journal of molecular sciences · 2019Article
- Time, space, and disorder in the expanding proteome universe.Proteomics · 2017Article
- Looking at the carcinogenicity of human insulin analogues via the intrinsic disorder prism.Scientific reports · 2016Article
- The intrinsic disorder alphabet. III. Dual personality of serine.Intrinsically disordered proteins · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein tags of various sizes and shapes catalyze progress in biosciences. Well-folded tags can serve to solubilize proteins. Small, unfolded, peptide-like tags have become invaluable tools for protein purification as well as protein-protein interaction studies. Intrinsically Disordered Proteins (IDPs), which lack unique 3D structures, received exponentially increasing attention during the last decade. Recently, large ID tags have been developed to solubilize proteins and to engineer the pharmacological properties of protein and peptide pharmaceuticals. Here, we contrast the complementary benefits and applications of both folded and ID tags based on predictions of ID. Less structure often means more function in a shorter tag.
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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.