ReviewInternational journal of molecular sciences2013
Misfolding and amyloid aggregation of apomyoglobin.
Review in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 37 citations in OpenAlex.
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- Molecular interactions between gelatin-derived carbon quantum dots and Apo-myoglobin: Implications for carbon nanomaterial frameworks.International journal of biological macromolecules · 2024Article
- Unveiling the Potential of Polyphenols as Anti-Amyloid Molecules in Alzheimer's Disease.Current neuropharmacology · 2023Review
- Structural and Functional Characterization of Covalently Modified Proteins Formed By a Glycating Agent, Glyoxal.ACS omega · 2021Article
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- Collagen I Weakly Interacts with the β-Sheets of βJournal of the American Chemical Society · 2020Article
- Confinement Facilitated Protein Stabilization As Investigated by Small-Angle Neutron Scattering.Journal of the American Chemical Society · 2018Article
- Modulating protein amyloid aggregation with nanomaterials.Environmental science. Nano · 2017Article
- Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts.Frontiers in molecular biosciences · 2016Article
- The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.Molecules (Basel, Switzerland) · 2015Review
- Differential effects of glycation on protein aggregation and amyloid formation.Frontiers in molecular biosciences · 2014Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apomyoglobin is an excellent example of a monomeric all α-helical globular protein whose folding pathway has been extensively studied and well characterized. Structural perturbation induced by denaturants or high temperature as well as amino acid substitution have been described to induce misfolding and, in some cases, aggregation. In this article, we review the molecular mechanism of the aggregation process through which a misfolded form of a mutated apomyoglobin aggregates at physiological pH and room temperature forming an amyloid fibril. The results are compared with data showing that either amyloid or aggregate formation occurs under particular denaturing conditions or upon cleavage of the residues corresponding to the C-terminal helix of apomyoglobin. The results are discussed in terms of the sequence regions that are more important than others in determining the amyloid aggregation process.
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What OpenQuestion holds
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.