ArticleCell reports2020
Thermodynamic and Evolutionary Coupling between the Native and Amyloid State of Globular Proteins.
Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed.
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
- TAF15 amyloids propagate via defined motifs in a prion-like fashion.Nature communications · 2026Article
- Thermodynamic Frontiers in Hemoglobin-Inspired Polymer Science for Diagnosis and Modulation of Neurodegenerative Diseases.Cell biochemistry and function · 2026Review
- Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026Article
- Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturation.Nature communications · 2025Article
- Peptidomimetics Targeting the Amyloidogenicity of Nucleophosmin 1 Mutations in Acute Myeloid Leukemia.Chembiochem : a European journal of chemical biology · 2025Article
- Comprehensive protein datasets and benchmarking for liquid-liquid phase separation studies.Genome biology · 2025Article
- Chemical Evolution of Early Macromolecules: From Prebiotic Oligopeptides to Self-Organizing Biosystems via Amyloid Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Co-translational protein aggregation and ribosome stalling as a broad-spectrum antibacterial mechanism.Nature communications · 2025Article
- Unravelling the Complexity of Amyloid Peptide Core Interfaces.Journal of chemical information and modeling · 2024Article
- Solvent induced amyloid polymorphism and the uncovering of the elusive class 3 amyloid topology.Communications biology · 2024Article
- An end-to-end approach for single-cell infrared absorption spectroscopy of bacterial inclusion bodies: from AFM-IR measurement to data interpretation of large sample sets.Journal of nanobiotechnology · 2024Article
- CORDAX web server: an online platform for the prediction and 3D visualization of aggregation motifs in protein sequences.Bioinformatics (Oxford, England) · 2024Article
- N-glycosylation as a eukaryotic protective mechanism against protein aggregation.Science advances · 2024Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Viruses and amyloids - a vicious liaison.Prion · 2023Review
- Polymorphic amyloid nanostructures of hormone peptides involved in glucose homeostasis display reversible amyloid formation.Nature communications · 2023Article
- Exploiting the intrinsic misfolding propensity of the KRAS oncoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- New pyrimidine-N-β-D-glucosides: synthesis, biological evaluation, and molecular docking investigations.Turkish journal of chemistry · 2023Article
- Nephroprotective mechanisms of Rhizoma Chuanxiong and Radix et Rhizoma Rhei against acute renal injury and renal fibrosis based on network pharmacology and experimental validation.Frontiers in pharmacology · 2023Article
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
The amyloid-like aggregation propensity present in most globular proteins is generally considered to be a secondary side effect resulting from the requirements of protein stability. Here, we demonstrate, however, that mutations in the globular and amyloid state are thermodynamically correlated rather than simply associated. In addition, we show that the standard genetic code couples this structural correlation into a tight evolutionary relationship. We illustrate the extent of this evolutionary entanglement of amyloid propensity and globular protein stability. Suppressing a 600-Ma-conserved amyloidogenic segment in the p53 core domain fold is structurally feasible but requires 7-bp substitutions to concomitantly introduce two aggregation-suppressing and three stabilizing amino acid mutations. We speculate that, rather than being a corollary of protein evolution, it is equally plausible that positive selection for amyloid structure could have been a driver for the emergence of globular protein structure.
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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.