ArticleThe Journal of biological chemistry2014
Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
- FAIM Inhibits Insulin Amyloidogenesis through a Noncanonical Aggregation Pathway.bioRxiv : the preprint server for biology · 2026Article
- Raman Spectroscopic Insights of Phase-Separated Insulin Aggregates.ACS physical chemistry Au · 2024Article
- Hairpin trimer transition state of amyloid fibril.Nature communications · 2024Article
- Article
- Modulation of Insulin Amyloid Fibrillization in Imidazolium-Based Ionic Liquids with Hofmeister Series Anions.International journal of molecular sciences · 2023Article
- Evaluation of fluorescence-based viability stains in cells dissociated from scleractinian coral Pocillopora damicornis.Scientific reports · 2022Article
- Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain.Molecules (Basel, Switzerland) · 2022Article
- Multistep growth of amyloid intermediates and its inhibition toward exploring therapeutic way: A case study using insulin B chain and fibrinogen.Biophysics and physicobiology · 2022Article
- Comparative study of the hydrophobic interaction effect of pH and ionic strength on aggregation/emulsification of Congo red and amyloid fibrillation of insulin.BBA advances · 2022Article
- Singular value decomposition analysis of the secondary structure features contributing to the circular dichroism spectra of model proteins.Biochemistry and biophysics reports · 2021Article
- Downstream processing of recombinant human insulin and its analogues production fromBioresources and bioprocessing · 2021Review
- Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin.International journal of molecular sciences · 2020Article
- Trehalose Effect on the Aggregation of Model Proteins into Amyloid Fibrils.Life (Basel, Switzerland) · 2020Article
- Recent progress on understanding the mechanisms of amyloid nucleation.Biophysical reviews · 2018Review
- A specific form of prefibrillar aggregates that functions as a precursor of amyloid nucleation.Scientific reports · 2018Article
- Equilibrium Ensembles for Insulin Folding from Bias-Exchange Metadynamics.Biophysical journal · 2017Article
- Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis.Scientific reports · 2017Article
- The emergence of superstructural order in insulin amyloid fibrils upon multiple rounds of self-seeding.Scientific reports · 2016Article
- Lysozyme Mutants Accumulate in Cells while Associated at their N-terminal Alpha-domain with the Endoplasmic Reticulum Chaperone GRP78/BiP.International journal of biological sciences · 2016Article
- Early aggregation preceding the nucleation of insulin amyloid fibrils as monitored by small angle X-ray scattering.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils are supramolecular assemblies, the deposition of which is associated with many serious diseases including Alzheimer, prion, and Huntington diseases. Several smaller aggregates such as oligomers and protofibrils have been proposed to play a role in early stages of the fibrillation process; however, little is known about how these species contribute to the formation of mature amyloid fibrils with a rigid cross-β structure. Here, we identified a new pathway for the formation of insulin amyloid fibrils at a high concentration of salt in which mature fibrils were formed in a stepwise manner via a prefibrillar intermediate: minute prefibrillar species initially accumulated, followed by the subsequent formation of thicker amyloid fibrils. Fourier transform infrared spectra suggested the sequential formation of two types of β-sheets with different strength hydrogen bonds, one of which was developed concomitantly with the mutual assembly of the prefibrillar intermediate to form mature fibrils. Interestingly, fibril propagation and cellular toxicity appeared only after the later step of structural organization, and a comparison of β-sheet regions between the prefibrillar intermediate and mature fibrils using proteolysis led to the proposal of specific regions essential for manifestation of these properties.
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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.