ArticleProtein science : a publication of the Protein Society2019
Side chain electrostatic interactions and pH-dependent expansion of the intrinsically disordered, highly acidic carboxyl-terminus of γ-tubulin.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Disordered but rhythmic-the role of intrinsic protein disorder in eukaryotic circadian timing.FEBS letters · 2026Review
- MEDOC: A Fast, Scalable, and Mathematically Exact Algorithm for the Site-Specific Prediction of the Protonation Degree in Large Disordered Proteins.Journal of chemical information and modeling · 2025Article
- Dissecting the pH Sensitivity of Kinesin-Driven Transport.The journal of physical chemistry. B · 2024Article
- Driving forces of the complex formation between highly charged disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Influence of gelatin type on physicochemical properties of electrospun nanofibers.Scientific reports · 2023Article
- PKAD-2: New entries and expansion of functionalities of the database of experimentally measured pKa's of proteins.Journal of computational biophysics and chemistry · 2023Article
- Article
- DispHred: A Server to Predict pH-Dependent Order-Disorder Transitions in Intrinsically Disordered Proteins.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Intramolecular electrostatic attraction and repulsion strongly influence the conformational sampling of intrinsically disordered proteins and domains (IDPs). In order to better understand this complex relationship, we have used nuclear magnetic resonance to measure side chain pK
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Registered trials
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