ArticlePloS one2011
Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 61 citations in OpenAlex.
- Methotrexate for Drug Repurposing as an Anti-Aggregatory Agent to Mercuric Treated α-Chymotrypsinogen-A.The protein journal · 2024Article
- Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.RSC advances · 2023Review
- AnAnnals of medicine · 2023Article
- Human RAD51 Protein Forms Amyloid-like AggregatesInternational journal of molecular sciences · 2022Article
- Full-length TDP-43 and its C-terminal domain form filamentsAmyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2021Article
- Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.International journal of molecular sciences · 2021Article
- Accumulation of storage proteins in plant seeds is mediated by amyloid formation.PLoS biology · 2020Article
- Silica-based solid-phase extraction of cross-linked nucleic acid-bound proteins.Life science alliance · 2018Article
- Formation of multimeric antibodies for self-delivery of active monomers.Drug delivery · 2017Article
- Downsizing a pullulanase to a small molecule with improved soluble expression and secretion efficiency in Escherichia coli.Microbial cell factories · 2016Article
- Article
- Enhancing the secretion efficiency and thermostability of a Bacillus deramificans pullulanase mutant (D437H/D503Y) by N-terminal domain truncation.Applied and environmental microbiology · 2015Article
- TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.PloS one · 2014Article
- Folding the proteome.Trends in biochemical sciences · 2013Review
- Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The assembly of soluble proteins into ordered fibrillar aggregates with cross-β structure is an essential event of many human diseases. The polypeptides undergoing aggregation are generally small in size. To explore if the small size is a primary determinant for the formation of amyloids under pathological conditions we have created two databases of proteins, forming amyloid-related and non-amyloid deposits in human diseases, respectively. The size distributions of the two protein populations are well separated, with the systems forming non-amyloid deposits appearing significantly larger. We have then investigated the propensity of the 486-residue hexokinase-B from Saccharomyces cerevisiae (YHKB) to form amyloid-like fibrils in vitro. This size is intermediate between the size distributions of amyloid and non-amyloid forming proteins. Aggregation was induced under conditions known to be most effective for amyloid formation by normally globular proteins: (i) low pH with salts, (ii) pH 5.5 with trifluoroethanol. In both situations YHKB aggregated very rapidly into species with significant β-sheet structure, as detected using circular dichroism and X-ray diffraction, but a weak Thioflavin T and Congo red binding. Moreover, atomic force microscopy indicated a morphology distinct from typical amyloid fibrils. Both types of aggregates were cytotoxic to human neuroblastoma cells, as indicated by the MTT assay. This analysis indicates that large proteins have a high tendency to form toxic aggregates, but low propensity to form regular amyloid in vivo and that such a behavior is intrinsically determined by the size of the protein, as suggested by the in vitro analysis of our sample protein.
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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.