ReviewProtein science : a publication of the Protein Society2013
A decade and a half of protein intrinsic disorder: biology still waits for physics.
Review in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 250 papers.
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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.
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Who cites it
250 citing papers in PubMed.
- Article
- An AI-enabled structural atlas decodes kinase specificity across the human proteome.Nature biotechnology · 2026Article
- The GFI1 Gene Family: Evolution, Structure, and Its Role in Immune Responses.Journal of molecular evolution · 2026Article
- Amyloid-β, Tau Protein, α-Synuclein, TDP-43, and FUS in Mixed Pathology: And Intrinsic Disorder to Rule Them All.International journal of molecular sciences · 2026Review
- Integrated Symbiotic Pleiotropy: Long Non-Coding RNAs and Disordered Proteins Interweaving the Functional Layers of the Eukaryotic Cell.International journal of molecular sciences · 2026Review
- Evaluating the Impact of Phosphorylation on the Dynamics of the Tau Protein Proline-Rich Region.Journal of chemical theory and computation · 2026Article
- A Survey of Predicted Protein-Protein Interactions Involving Disordered Regions in Humans.Journal of molecular biology · 2026Article
- Sequence and length-scale dependent dynamics in biocondensates of highly charged disordered proteins.Communications chemistry · 2026Article
- Specificity of the stabilizing interaction between intrinsically disordered protein sequences and G-quadruplexes in RNA.Nucleic acids research · 2026Article
- In silico prediction of the binding structure between vitellogenin and vitellogenin receptor of Haemaphysalis longicornis.The Journal of veterinary medical science · 2025Article
- The C-terminal region ofAustralian journal of chemistry · 2025Article
- Structure and Mechanism of Aminoacyl-tRNA-Protein L/F- and R-transferases.Journal of molecular biology · 2025Review
- Characterization of intrinsically disordered regions through scalar coupling-based solid-state NMR experiments.Biophysics reports · 2025Article
- The intrinsically disordered protein NUPR1 binds to phospholipids.Protein science : a publication of the Protein Society · 2025Article
- Structural, Functional and Inhibitory Annotations of Lumpy Skin Disease Virus Hypothetical Protein LSDV004: An In-Silico Study.Veterinary medicine and science · 2025Article
- Bioinformatics-Based Comparative Analysis of the Human Retina Proteome.Proteomics. Clinical applications · 2025Article
- The effects of retinal disease on intrinsic protein disorder and liquid-liquid‑phase separation.Journal of proteins and proteomics · 2025Article
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- Intrinsic disorder in CYP1B1 and its implications in primary congenital glaucoma pathogenesis.Journal of proteins and proteomics · 2025Article
- An Analysis of Intrinsic Protein Disorder in Antimicrobial Peptides.The protein journal · 2025Article
190 more citing papers are in PubMed but not listed here.
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
The abundant existence of proteins and regions that possess specific functions without being uniquely folded into unique 3D structures has become accepted by a significant number of protein scientists. Sequences of these intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) are characterized by a number of specific features, such as low overall hydrophobicity and high net charge which makes these proteins predictable. IDPs/IDPRs possess large hydrodynamic volumes, low contents of ordered secondary structure, and are characterized by high structural heterogeneity. They are very flexible, but some may undergo disorder to order transitions in the presence of natural ligands. The degree of these structural rearrangements varies over a very wide range. IDPs/IDPRs are tightly controlled under the normal conditions and have numerous specific functions that complement functions of ordered proteins and domains. When lacking proper control, they have multiple roles in pathogenesis of various human diseases. Gaining structural and functional information about these proteins is a challenge, since they do not typically "freeze" while their "pictures are taken." However, despite or perhaps because of the experimental challenges, these fuzzy objects with fuzzy structures and fuzzy functions are among the most interesting targets for modern protein research. This review briefly summarizes some of the recent advances in this exciting field and considers some of the basic lessons learned from the analysis of physics, chemistry, and biology of IDPs.
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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.