ArticleThe Journal of biological chemistry2014
Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Histological assessment of cardiac amyloidosis in patients undergoing transcatheter aortic valve replacement.ESC heart failure · 2024Article
- Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity.Molecules (Basel, Switzerland) · 2022Article
- Substrate Specificity and Structural Modeling of Human Carboxypeptidase Z: A Unique Protease with a Frizzled-Like Domain.International journal of molecular sciences · 2020Article
- Structure and Aggregation Mechanisms in Amyloids.Molecules (Basel, Switzerland) · 2020Review
- Causative Links between Protein Aggregation and Oxidative Stress: A Review.International journal of molecular sciences · 2019Review
- Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation.Cells · 2019Article
- Atomic force microscopy for single molecule characterisation of protein aggregation.Archives of biochemistry and biophysics · 2019Review
- Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction.Nature communications · 2018Article
- sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.Biophysical journal · 2017Article
- Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.Biophysical journal · 2017Article
- Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.Biochemistry · 2016Article
- Global metagenomic survey reveals a new bacterial candidate phylum in geothermal springs.Nature communications · 2016Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein aggregation is linked to a growing list of diseases, but it is also an intrinsic property of polypeptides, because the formation of functional globular proteins comes at the expense of an inherent aggregation propensity. Certain proteins can access aggregation-prone states from native-like conformations without the need to cross the energy barrier for unfolding. This is the case of transthyretin (TTR), a homotetrameric protein whose dissociation into its monomers initiates the aggregation cascade. Domains with structural homology to TTR exist in a number of proteins, including the M14B subfamily carboxypeptidases. We show here that the monomeric transthyretin-like domain of human carboxypeptidase D aggregates under close to physiological conditions into amyloid structures, with the population of folded but aggregation-prone states being controlled by the conformational stability of the domain. We thus confirm that the TTR fold keeps a generic residual aggregation propensity upon folding, resulting from the presence of preformed amyloidogenic β-strands in the native state. These structural elements should serve for functional/structural purposes, because they have not been purged out by evolution, but at the same time they put proteins like carboxypeptidase D at risk of aggregation in biological environments and thus can potentially lead to deposition diseases.
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