ArticleBiophysical journal2020
Structural Consequences of Multisite Phosphorylation in the BAK1 Kinase Domain.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Mechanism of MEK1 activation by phosphorylation.Biophysical journal · 2026Article
- Mastering the balance: BAK1's dual roles in steering plant growth and immunity.Horticulture research · 2025Article
- Interactions between Inhibitors and 5-Lipoxygenase: Insights from Gaussian Accelerated Molecular Dynamics and Markov State Models.International journal of molecular sciences · 2024Article
- SWEET family transporters act as water conducting carrier proteins in plants.bioRxiv : the preprint server for biology · 2024Article
- Thirty years of molecular dynamics simulations on posttranslational modifications of proteins.Physical chemistry chemical physics : PCCP · 2022Review
- Binding Analysis Using Accelerated Molecular Dynamics Simulations and Future Perspectives.Advances and applications in bioinformatics and chemistry : AABC · 2022Review
- Activation loop phosphorylation of a non-RD receptor kinase initiates plant innate immune signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation.Biophysical journal · 2021Article
- Phosphorylation-induced changes in the PDZ domain of Dishevelled 3.Scientific reports · 2021Article
- Gaussian accelerated molecular dynamics (GaMD): principles and applications.Wiley interdisciplinary reviews. Computational molecular scienceArticle
Corrections and comments
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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
Multisite phosphorylation is an important mechanism of post-translational control of protein kinases. The effects of combinations of possible phosphorylation states on protein kinase activity are difficult to study experimentally because of challenges in isolating a particular phosphorylation state; surprising little effort on this topic has been expended in computational studies. To understand the effects of multisite phosphorylation on the plant protein kinase brassinosteroid insensitive 1-associated kinase 1 (BAK1) conformational ensemble, we performed Gaussian accelerated molecular dynamics simulations on eight BAK1 mod-forms involving phosphorylation of the four activation-loop threonine residues and binding of ATP-Mg
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