ReviewCell systems2021
Fundamentals to function: Quantitative and scalable approaches for measuring protein stability.
Review in Cell systems, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- pH-Dependent Stability and Cooperativity of Protein Unfolding from Differential Scanning Calorimetry Using FitFoldData.Biomolecules · 2026Article
- Quantifying protein unfolding kinetics with a high-throughput microfluidic platform.Cell systems · 2026Article
- Deep phenotyping of EHMT1 ankyrin repeat domain missense variants in Kleefstra syndrome by multi-tiered structural genomics analyses at atomic resolution.Human molecular genetics · 2026Article
- Towards routine accurate electron-density studies of biological macromolecules.Acta crystallographica. Section D, Structural biology · 2026Article
- The prevalence of protein misfolding as a mechanism for hereditary deafness.PLoS genetics · 2026Article
- Thermostability Engineering in Therapeutic Antioxidant Enzymes: From Molecular Fundamentals to Oxidative Stress Applications.International journal of molecular sciences · 2026Review
- Advances and opportunities for computational interrogation of plant proteins.The Plant journal : for cell and molecular biology · 2026Review
- Structural Genomics Defines PBRM1 Bromodomain Variant Function in ccRCC.Human mutation · 2026Article
- The effectiveness of selection in a species affects the direction of amino acid frequency evolution.bioRxiv : the preprint server for biology · 2025Article
- Protein-adaptive differential scanning fluorimetry using conformationally responsive dyes.Nature biotechnology · 2025Article
- Enhancing therapeutic antibody profiling: orthogonal strategies for stability and quality assessment.Frontiers in pharmacology · 2025Article
- A combinatorially complete epistatic fitness landscape in an enzyme active site.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Functional and in silico analysis of ATP8A2 and other P4-ATPase variants associated with human genetic diseases.Disease models & mechanisms · 2024Article
- Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024Review
- Protocol for performing and optimizing differential scanning fluorimetry experiments.STAR protocols · 2023Article
- Quantitation of autoinhibitory defects in pathogenic SHP2 mutants by differential scanning fluorimetry.Analytical biochemistry · 2023Article
- Homologous Pairs of Low and High Temperature Originating Proteins Spanning the Known Prokaryotic Universe.Scientific data · 2023Article
- Folding stabilities of ribosome-bound nascent polypeptides probed by mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?International journal of molecular sciences · 2022Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Folding a linear chain of amino acids into a three-dimensional protein is a complex physical process that ultimately confers an impressive range of diverse functions. Although recent advances have driven significant progress in predicting three-dimensional protein structures from sequence, proteins are not static molecules. Rather, they exist as complex conformational ensembles defined by energy landscapes spanning the space of sequence and conditions. Quantitatively mapping the physical parameters that dictate these landscapes and protein stability is therefore critical to develop models that are capable of predicting how mutations alter function of proteins in disease and informing the design of proteins with desired functions. Here, we review the approaches that are used to quantify protein stability at a variety of scales, from returning multiple thermodynamic and kinetic measurements for a single protein sequence to yielding indirect insights into folding across a vast sequence space. The physical parameters derived from these approaches will provide a foundation for models that extend beyond the structural prediction to capture the complexity of conformational ensembles and, ultimately, their function.
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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.