ArticleMolecular cell2011
Conformational conversion during amyloid formation at atomic resolution.
Article in Molecular cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed.
- Optimizing Silk Nanoparticle Assembly with Potassium Ions: Effects on Physicochemical Properties and Encapsulation Efficiency.ACS applied bio materials · 2025Article
- Single-molecule nanopore sensing of prolineChemical science · 2025Article
- The mechanism of amyloid fibril growth from Φ-value analysis.Nature chemistry · 2025Article
- Substitution of Met-38 to Ile in γ-synuclein found in two patients with amyotrophic lateral sclerosis induces aggregation into amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller.Nature communications · 2024Article
- Design of Beta-2 Microglobulin Adsorbent Protein Nanoparticles.Biomolecules · 2023Article
- β2-Microglobulin boosts β-amyloid aggregation and neurotoxicity in an Alzheimer's disease model.Nature neuroscience · 2023Article
- βNature neuroscience · 2023Article
- The residual structure of acid-denatured βProtein science : a publication of the Protein Society · 2023Article
- Dendrimers as Antiamyloid Agents.Pharmaceutics · 2022Review
- The residues 4 to 6 at the N-terminus in particular modulate fibril propagation of β-microglobulin.Acta biochimica et biophysica Sinica · 2022Article
- Generating Ensembles of Dynamic Misfolding Proteins.Frontiers in neuroscience · 2022Review
- Global Proteotoxicity Caused by Human βInternational journal of molecular sciences · 2021Article
- In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model.International journal of molecular sciences · 2021Article
- Investigation of D76N βJournal of the American Society for Mass Spectrometry · 2021Article
- Predicting stable binding modes from simulated dimers of the D76N mutant ofComputational and structural biotechnology journal · 2021Article
- Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules.Journal of the American Chemical Society · 2020Article
- Edge Strand Dissociation and Conformational Changes in Transthyretin under Amyloidogenic Conditions.Biophysical journal · 2020Article
- Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity.The Journal of biological chemistry · 2020Article
- The role of the IThe Journal of biological chemistry · 2020Article
21 more citing papers are in PubMed but not listed here.
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5 authors.
Funding
Abstract
Numerous studies of amyloid assembly have indicated that partially folded protein species are responsible for initiating aggregation. Despite their importance, the structural and dynamic features of amyloidogenic intermediates and the molecular details of how they cause aggregation remain elusive. Here, we use ΔN6, a truncation variant of the naturally amyloidogenic protein β(2)-microglobulin (β(2)m), to determine the solution structure of a nonnative amyloidogenic intermediate at high resolution. The structure of ΔN6 reveals a major repacking of the hydrophobic core to accommodate the nonnative peptidyl-prolyl trans-isomer at Pro32. These structural changes, together with a concomitant pH-dependent enhancement in backbone dynamics on a microsecond-millisecond timescale, give rise to a rare conformer with increased amyloidogenic potential. We further reveal that catalytic amounts of ΔN6 are competent to convert nonamyloidogenic human wild-type β(2)m (Hβ(2)m) into a rare amyloidogenic conformation and provide structural evidence for the mechanism by which this conformational conversion occurs.
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