ArticleThe Journal of biological chemistry2020
Single-residue physicochemical characteristics kinetically partition membrane protein self-assembly and aggregation.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Mitochondrial Transmembrane β-Barrels: Deducing Thermodynamic Regulators of Folding and Stability.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Real-time monitoring by interferometric light microscopy of phage suspensions for personalised phage therapy.Scientific reports · 2024Article
- Monomeric Amyloid Peptide-induced Toxicity in Human Oligodendrocyte Cell Line and Mouse Brain Primary Mixed-glial Cell Cultures: Evidence for a Neuroprotective Effect of Neurosteroid 3α-O-allyl-allopregnanolone.Neurotoxicity research · 2024Article
- Detergent headgroups control TolC folding in vitro.Biophysical journal · 2023Article
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- Studies on the Structure and Properties of Membrane Phospholipase AMolecules (Basel, Switzerland) · 2021Article
- Evolutionary selection of a 19-stranded mitochondrial β-barrel scaffold bears structural and functional significance.The Journal of biological chemistry · 2020Article
- Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods.Molecules (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Ninety-five percent of all transmembrane proteins exist in kinetically trapped aggregation-prone states that have been directly linked to neurodegenerative diseases. Interestingly, the primary sequence almost invariably avoids off-pathway aggregate formation, by folding reliably into its native, thermodynamically stabilized structure. However, with the rising incidence of protein aggregation diseases, it is now important to understand the underlying mechanism(s) of membrane protein aggregation. Micromolecular physicochemical and biochemical alterations in the primary sequence that trigger the formation of macromolecular cross-β aggregates can be measured only through combinatorial spectroscopic experiments. Here, we developed spectroscopic thermal perturbation with 117 experimental variables to assess how subtle protein sequence variations drive the molecular transition of the folded protein to oligomeric aggregates. Using the
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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.