ArticleProtein science : a publication of the Protein Society2006
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Explore antibody repertoire in the era of AI.Acta biochimica et biophysica Sinica · 2025Article
- The Inhibition of Serum Amyloid A Protein Aggregation by a Five-Residue Peptidomimetic: Structural and Morphological Insights.Molecules (Basel, Switzerland) · 2024Article
- Novel Approach for Obtaining Variable Domain of New Antigen Receptor with Different Physicochemical Properties from Japanese Topeshark (Marine drugs · 2023Article
- Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.Frontiers in immunology · 2023Review
- Studying the characteristics of nanobody CDR regions based on sequence analysis in combination with 3D structures.Journal, genetic engineering & biotechnology · 2022Article
- Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes.Chemical reviews · 2021Review
- Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association.Computational and structural biotechnology journal · 2021Article
- Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain.Biophysical chemistry · 2020Review
- Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation.International journal of molecular sciences · 2019Article
- Uncovering the Networks of Topological Neighborhoods in β-Strand and Amyloid β-Sheet Structures.Scientific reports · 2019Article
- Ovalbumin self-assembles into amyloid nanosheets that elicit immune responses and facilitate sustained drug release.The Journal of biological chemistry · 2018Article
- Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.International journal of molecular sciences · 2018Review
- The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.Interface focus · 2017Review
- Melanosomal formation of PMEL core amyloid is driven by aromatic residues.Scientific reports · 2017Article
- Review
- Effect of Cinnamomum Verum Extract on the Amyloid Formation of Hen Egg-white Lysozyme and Study of its Possible Role in Alzheimer's Disease.Basic and clinical neuroscience · 2015Article
- The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of β-Sheets.Journal of molecular biology · 2013Article
- A Phe-rich region in short-wavelength sensitive opsins is responsible for their aggregation in the absence of 11-cis-retinal.FEBS letters · 2013Article
- Article
- Natural biomolecules and protein aggregation: emerging strategies against amyloidogenesis.International journal of molecular sciences · 2012Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among the many parameters that have been proposed to promote amyloid fibril formation is the pi-stacking of aromatic residues. We have studied the amyloid aggregation of several mutants of human muscle acylphosphatase in which an aromatic residue was substituted with a non-aromatic one. The aggregation rate was determined using the Thioflavin T test under conditions in which the variants populated initially an ensemble of partially unfolded conformations. Substitutions in aggregation-promoting fragments of the sequence result in a dramatically decreased aggregation rate of the protein, confirming the propensity of aromatic residues to promote this process. Nevertheless, a statistical analysis shows that the measured decrease of aggregation rate following mutation arises predominantly from a reduction of hydrophobicity and intrinsic beta-sheet propensity. This suggests that aromatic residues favor aggregation because of these factors rather than for their aromaticity.
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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.