ArticleJournal of molecular biology2016
Structural Dynamics in Ras and Related Proteins upon Nucleotide Switching.
Article in Journal of molecular biology, 2016. 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
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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.
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.
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Who cites it
22 citing papers in PubMed.
- Structural Dynamics of Rho GTPases.Journal of molecular biology · 2025Review
- Deep Learning Approaches for the Prediction of Protein Functional Sites.Molecules (Basel, Switzerland) · 2025Review
- Article
- Allosteric site variants affect GTP hydrolysis on Ras.Protein science : a publication of the Protein Society · 2023Article
- Mechanisms of isoform-specific residue influence on GTP-bound HRas, KRas, and NRas.Biophysical journal · 2022Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Protection of the Prodomain α1-Helix Correlates with Latency in the Transforming Growth Factor-β Family.Journal of molecular biology · 2022Article
- A saturation-mutagenesis analysis of the interplay between stability and activation in Ras.eLife · 2022Article
- GLOBAL AND TARGETED PROFILING OF GTP-BINDING PROTEINS IN BIOLOGICAL SAMPLES BY MASS SPECTROMETRY.Mass spectrometry reviews · 2021Review
- Mechanistic basis for ubiquitin modulation of a protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- R-Ras GTPases Signaling Role in Myelin Neurodegenerative Diseases.International journal of molecular sciences · 2020Review
- Structural basis of the atypical activation mechanism of KRASThe Journal of biological chemistry · 2019Article
- Investigation of GTP-dependent dimerization of G12X K-Ras variants using ultraviolet photodissociation mass spectrometry.Chemical science · 2019Article
- Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments.Nature methods · 2019Review
- Tissue-Specific Oncogenic Activity of KRASCancer discovery · 2019Article
- Glycyrrhetinic acid binds to the conserved P-loop region and interferes with the interaction of RAS-effector proteins.Acta pharmaceutica Sinica. B · 2019Article
- Predicting X-ray solution scattering from flexible macromolecules.Protein science : a publication of the Protein Society · 2018Article
- The K-Ras, N-Ras, and H-Ras Isoforms: Unique Conformational Preferences and Implications for Targeting Oncogenic Mutants.Cold Spring Harbor perspectives in medicine · 2018Review
- Novel K-Ras G12C Switch-II Covalent Binders Destabilize Ras and Accelerate Nucleotide Exchange.Journal of chemical information and modeling · 2018Article
- KRAS Switch Mutants D33E and A59G Crystallize in the State 1 Conformation.Biochemistry · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Structural dynamics of Ras proteins contributes to their activity in signal transduction cascades. Directly targeting Ras proteins with small molecules may rely on the movement of a conserved structural motif, switch II. To understand Ras signaling and advance Ras-targeting strategies, experimental methods to measure Ras dynamics are required. Here, we demonstrate the utility of hydrogen-deuterium exchange (HDX) mass spectrometry (MS) to measure Ras dynamics by studying representatives from two branches of the Ras superfamily, Ras and Rho. A comparison of differential deuterium exchange between active (GMPPNP-bound) and inactive (GDP-bound) proteins revealed differences between the families, with the most notable differences occurring in the phosphate-binding loop and switch II. The P-loop exchange signature correlated with switch II dynamics observed in molecular dynamics simulations focused on measuring main-chain movement. HDX provides a means of evaluating Ras protein dynamics, which may be useful for understanding the mechanisms of Ras signaling, including activated signaling of pathologic mutants, and for targeting strategies that rely on protein dynamics.
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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.