ArticleInternational journal of molecular sciences2021
KEAP1 Cancer Mutants: A Large-Scale Molecular Dynamics Study of Protein Stability.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed, 14 citations in OpenAlex.
- Antioxidant Activity In Vitro and Protective Effects Against Lipopolysaccharide-Induced Oxidative Stress and Inflammation in RAW264.7 Cells ofFoods (Basel, Switzerland) · 2025Article
- The Impact of Genetic Mutations on the Efficacy of Immunotherapies in Lung Cancer.International journal of molecular sciences · 2024Review
- Protein stability prediction by fine-tuning a protein language model on a mega-scale dataset.PLoS computational biology · 2024Article
- KEAP1 mutation in lung adenocarcinoma promotes immune evasion and immunotherapy resistance.Cell reports · 2023Article
- AlphaFold2: A Role for Disordered Protein/Region Prediction?International journal of molecular sciences · 2022Article
- Matrin3: Disorder and ALS Pathogenesis.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We have performed 280 μs of unbiased molecular dynamics (MD) simulations to investigate the effects of 12 different cancer mutations on Kelch-like ECH-associated protein 1 (KEAP1) (G333C, G350S, G364C, G379D, R413L, R415G, A427V, G430C, R470C, R470H, R470S and G476R), one of the frequently mutated proteins in lung cancer. The aim was to provide structural insight into the effects of these mutants, including a new class of ANCHOR (additionally NRF2-complexed hypomorph) mutant variants. Our work provides additional insight into the structural dynamics of mutants that could not be analyzed experimentally, painting a more complete picture of their mutagenic effects. Notably, blade-wise analysis of the Kelch domain points to stability as a possible target of cancer in KEAP1. Interestingly, structural analysis of the R470C ANCHOR mutant, the most prevalent missense mutation in KEAP1, revealed no significant change in structural stability or NRF2 binding site dynamics, possibly indicating an covalent modification as this mutant's mode of action.
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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.