ArticlePLoS computational biology2009
Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.
Article in PLoS computational biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 81 citations in OpenAlex.
- β-Amyloid (Aβ) and Human Cathelicidin LL-37: Two Sides of the Same Coin?International journal of molecular sciences · 2026Review
- Inhibitory effect of Fisetin against the aggregation process of SOD1 E100K mutant: computer-based drug design as a potential therapeutic for ALS disease.Frontiers in chemistry · 2025Article
- Directed disruption of IL2 aggregation and receptor binding sites produces designer biologics with enhanced specificity and improved production capacity.Computational and structural biotechnology journal · 2025Article
- CORDAX web server: an online platform for the prediction and 3D visualization of aggregation motifs in protein sequences.Bioinformatics (Oxford, England) · 2024Article
- Biophysical Evidence for the Amyloid Formation of a Recombinant Rab2 Isoform ofProtein and peptide letters · 2024Article
- Expanding the Landscape of Amyloid Sequences with CARs-DB: A Database of Polar Amyloidogenic Peptides from Disordered Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A3DyDB: exploring structural aggregation propensities in the yeast proteome.Microbial cell factories · 2023Article
- Trigger factor both holds and folds its client proteins.Nature communications · 2022Article
- CARs-DB: A Database of Cryptic Amyloidogenic Regions in Intrinsically Disordered Proteins.Frontiers in molecular biosciences · 2022Article
- MAPRE2 mutations result in altered human cranial neural crest migration, underlying craniofacial malformations in CSC-KT syndrome.Scientific reports · 2021Article
- Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association.Computational and structural biotechnology journal · 2021Article
- Article
- Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities.Nature communications · 2020Article
- Thermodynamic and Evolutionary Coupling between the Native and Amyloid State of Globular Proteins.Cell reports · 2020Article
- Computational prediction of protein aggregation: Advances in proteomics, conformation-specific algorithms and biotechnological applications.Computational and structural biotechnology journal · 2020Review
- Hidden Aggregation Hot-Spots on Human Apolipoprotein E: A Structural Study.International journal of molecular sciences · 2019Article
- The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region.International journal of molecular sciences · 2018Article
- Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling.BMC structural biology · 2018Article
- Prediction and Reduction of the Aggregation of Monoclonal Antibodies.Journal of molecular biology · 2017Article
- Insulin Fibrillization at Acidic and Physiological pH Values is Controlled by Different Molecular Mechanisms.The protein journal · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein aggregation underlies a wide range of human disorders. The polypeptides involved in these pathologies might be intrinsically unstructured or display a defined 3D-structure. Little is known about how globular proteins aggregate into toxic assemblies under physiological conditions, where they display an initially folded conformation. Protein aggregation is, however, always initiated by the establishment of anomalous protein-protein interactions. Therefore, in the present work, we have explored the extent to which protein interaction surfaces and aggregation-prone regions overlap in globular proteins associated with conformational diseases. Computational analysis of the native complexes formed by these proteins shows that aggregation-prone regions do frequently overlap with protein interfaces. The spatial coincidence of interaction sites and aggregating regions suggests that the formation of functional complexes and the aggregation of their individual subunits might compete in the cell. Accordingly, single mutations affecting complex interface or stability usually result in the formation of toxic aggregates. It is suggested that the stabilization of existing interfaces in multimeric proteins or the formation of new complexes in monomeric polypeptides might become effective strategies to prevent disease-linked aggregation of globular proteins.
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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.