ArticleBiophysical journal2020
Protein Dynamics Enables Phosphorylation of Buried Residues in Cdk2/Cyclin-A-Bound p27.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- In Search of Shape in the Unshaped: Constructing Ensembles of Intrinsically Disordered Proteins.Biophysics reviews · 2026Article
- MAVISp: A modular structure-based framework for protein variant effects.Protein science : a publication of the Protein Society · 2026Article
- SDC4 silencing promotes cell cycle arrest at the restriction point (R point) in anoikis-resistant endothelial cells.Cytotechnology · 2026Article
- Elucidation of Proteoforms of Chinese Hamster Ovary (CHO) Phospholipase B-Like 2 (PLBL2) Captured From a Monoclonal Antibody.Biotechnology and bioengineering · 2026Article
- Missense mutations in intrinsically disordered protein regions link pathogenicity and phase separation.The Journal of biological chemistry · 2025Article
- Global comparative structural analysis of responses to protein phosphorylation.Nature communications · 2025Article
- A cell wall-associated kinase phosphorylates NLR immune receptor to negatively regulate resistosome formation.Nature plants · 2025Article
- The fitness cost of spurious phosphorylation.The EMBO journal · 2024Article
- Integrative Proteomics and Phosphoproteomics Profiling of Symptomatic Accessory Navicular Bone Based on Tandem Mass Tag Technology.International journal of general medicine · 2024Article
- The fitness cost of spurious phosphorylation.bioRxiv : the preprint server for biology · 2023Article
- TRAP1 S-nitrosylation as a model of population-shift mechanism to study the effects of nitric oxide on redox-sensitive oncoproteins.Cell death & disease · 2023Article
- How phosphorylation impacts intrinsically disordered proteins and their function.Essays in biochemistry · 2022Article
- Conserved Cdk inhibitors show unique structural responses to tyrosine phosphorylation.Biophysical journal · 2022Article
- Structural-Energetic Basis for Coupling between Equilibrium Fluctuations and Phosphorylation in a Protein Native Ensemble.ACS central science · 2022Article
- Transient exposure of a buried phosphorylation site in an autoinhibited protein.Biophysical journal · 2022Article
- Exosomal‑miR‑1184 derived from mesenchymal stem cells alleviates cisplatin‑associated acute kidney injury.Molecular medicine reports · 2021Article
- Article
- Diffusion of a disordered protein on its folded ligand.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Tale of Two Tyrosines.Biophysical journal · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins carry out a wide range of functions that are tightly regulated in space and time. Protein phosphorylation is the most common post-translation modification of proteins and plays a key role in the regulation of many biological processes. The finding that many phosphorylated residues are not solvent exposed in the unphosphorylated state opens several questions for understanding the mechanism that underlies phosphorylation and how phosphorylation may affect protein structures. First, because kinases need access to the phosphorylated residue, how do such buried residues become modified? Second, once phosphorylated, what are the structural effects of phosphorylation of buried residues, and do they lead to changed conformational dynamics? We have used the ternary complex between p27
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