ArticleHFSP journal2007
Characterization of the nucleation barriers for protein aggregation and amyloid formation.
Article in HFSP journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 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.
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Who cites it
46 citing papers in PubMed, 142 citations in OpenAlex.
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- Big versus small: The impact of aggregate size in disease.Protein science : a publication of the Protein Society · 2023Review
- The Impact of the Cellular Environment and Aging on Modeling Alzheimer's Disease in 3D Cell Culture Models.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Review
- Amyloidogenesis: What Do We Know So Far?International journal of molecular sciences · 2022Review
- Side Chain Geometry Determines the Fibrillation Propensity of a Minimal Two-Beads-per-Residue Peptide Model.The journal of physical chemistry. B · 2022Article
- Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022Review
- Time-Prolonged Release of Tumor-Targeted Protein-MMAE Nanoconjugates from Implantable Hybrid Materials.Pharmaceutics · 2022Article
- Computational Models for the Study of Protein Aggregation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Diverse Aggregation Kinetics Predicted by a Coarse-Grained Peptide Model.The journal of physical chemistry. B · 2021Article
- Robust nucleation control via crisscross polymerization of highly coordinated DNA slats.Nature communications · 2021Article
- Mechanisms and therapeutic potential of interactions between human amyloids and viruses.Cellular and molecular life sciences : CMLS · 2021Review
- Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches.Computational and structural biotechnology journal · 2021Review
- Sequence-Dependent Nanofiber Structures of Phenylalanine and Isoleucine Tripeptides.International journal of molecular sciences · 2020Article
- Thermodynamics of Huntingtin Aggregation.Biophysical journal · 2020Article
- Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide.Nature chemistry · 2020Article
- Disentangling the Amyloid Pathways: A Mechanistic Approach to Etiology.Frontiers in neuroscience · 2020Article
- Alpha-Synuclein Is a Target of Fic-Mediated Adenylylation/AMPylation: Possible Implications for Parkinson's Disease.Journal of molecular biology · 2019Article
- Structural Analysis of a Trimer of βBiophysical journal · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the complexity and the specificity of the amino acid code, a variety of peptides and proteins unrelated in sequence and function exhibit a common behavior and assemble into highly organized amyloid fibrils. The formation of such aggregates is often described by a nucleation and growth mechanism, in which the proteins involved also form intermediate oligomeric aggregates before they reorganize and grow into ordered fibrils with a characteristic cross-beta structure. It is extremely difficult to experimentally obtain an accurate description of the early stages of this phenomenon due to the transient nature and structural heterogeneity of the oligomeric precursors. We investigate here the phenomenon of ordered aggregation by using the recently introduced tube model of polypeptide chains in conjunction with the generic hypothesis of amyloid formation. Under conditions where oligomer formation is a rare event-the most common conditions for forming amyloid fibrils by experiment-we calculate directly the nucleation barriers associated with oligomer formation and conversion into cross-beta structure in order to reveal the nature of these species, determine the critical nuclei, and characterize their dependence on the hydrophobicity of the peptides and the thermodynamic parameters associated with aggregation and amyloid formation.
Identifiers
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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.