ArticleProtein science : a publication of the Protein Society2015
Binding cavities and druggability of intrinsically disordered proteins.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed.
- Small Molecules Targeting the Structural Dynamics of AR-V7 Partially Disordered Proteins Using Deep Ensemble Docking.Journal of chemical theory and computation · 2025Article
- Transcription factors in the development and treatment of immune disorders.Transcription · 2025Review
- 20S proteasome enhancers prevent cytotoxic tubulin polymerization-promoting protein induced α-synuclein aggregation.iScience · 2024Article
- Development of a Cell-Based AlphaLISA Assay for High-Throughput Screening for Small Molecule Proteasome Modulators.ACS omega · 2023Article
- The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs.RSC advances · 2023Review
- Dynamics-Based Regulatory Switches of Type II Antitoxins: Insights into New Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2023Article
- The Intrinsically Disordered Proteins MLLT3 (AF9) and MLLT1 (ENL) - Multimodal Transcriptional Switches With Roles in Normal Hematopoiesis, MLL Fusion Leukemia, and Kidney Cancer.Journal of molecular biology · 2022Review
- Single-molecule analysis of interaction between p53TAD and MDM2 using aerolysin nanopores.Chemical science · 2021Article
- Drugging Fuzzy Complexes in Transcription.Frontiers in molecular biosciences · 2021Article
- Therapeutics-how to treat phase separation-associated diseases.Emerging topics in life sciences · 2020Review
- Targeting Intrinsically Disordered Proteins through Dynamic Interactions.Biomolecules · 2020Review
- Discovery of drugs that directly target the intrinsically disordered region of the androgen receptor.Expert opinion on drug discovery · 2020Review
- Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins.Journal of biosciences · 2020Review
- Targeting transcription factors in cancer - from undruggable to reality.Nature reviews. Cancer · 2019Review
- Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins.Biomolecules · 2019Review
- Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies.International journal of molecular sciences · 2019Review
- Conservation of Potentially Druggable Cavities in Intrinsically Disordered Proteins.ACS omega · 2018Article
- Late metabolic precursors for selective aromatic residue labeling.Journal of biomolecular NMR · 2018Review
- Structured and disordered regions cooperatively mediate DNA-binding autoinhibition of ETS factors ETV1, ETV4 and ETV5.Nucleic acids research · 2017Article
- Structure-based Inhibitor Design for the Intrinsically Disordered Protein c-Myc.Scientific reports · 2016Article
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
To assess the potential of intrinsically disordered proteins (IDPs) as drug design targets, we have analyzed the ligand-binding cavities of two datasets of IDPs (containing 37 and 16 entries, respectively) and compared their properties with those of conventional ordered (folded) proteins. IDPs were predicted to possess more binding cavity than ordered proteins at similar length, supporting the proposed advantage of IDPs economizing genome and protein resources. The cavity number has a wide distribution within each conformation ensemble for IDPs. The geometries of the cavities of IDPs differ from the cavities of ordered proteins, for example, the cavities of IDPs have larger surface areas and volumes, and are more likely to be composed of a single segment. The druggability of the cavities was examined, and the average druggable probability is estimated to be 9% for IDPs, which is almost twice that for ordered proteins (5%). Some IDPs with druggable cavities that are associated with diseases are listed. The optimism versus obstacles for drug design for IDPs is also briefly discussed.
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.