The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Uncovering the Mechanism of Aggregation of Human Transthyretin
Open accessAbstract
The tetrameric thyroxine transport protein transthyretin (TTR) forms amyloid fibrils upon dissociation and monomer unfolding. The aggregation of transthyretin has been reported as the cause of the life-threatening transthyretin amyloidosis. The standard treatment of familial cases of TTR amyloidosis has been liver transplantation. Although aggregation-preventing strategies involving ligands are known, understanding the mechanism of TTR aggregation can lead to additional inhibition approaches. Several models of TTR amyloid fibrils have been proposed, but the segments that drive aggregation of the protein have remained unknown. Here we identify β-strands F and H as necessary for TTR aggregation. Based on the crystal structures of these segments, we designed two non-natural peptide inhibitors that block aggregation. This work provides the first characterization of peptide inhibitors for TTR aggregation, establishing a novel therapeutic strategy.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Overview of the CCP 4 suite and current developments
Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353
Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., et al. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-18 · Cited by 773
Cited by
Structure-based inhibitors of amyloid beta core suggest a common interface with tau
Griner, S. L., Seidler, P., Bowler, J., Murray, K. A., Yang, T. P., Sahay, S., Sawaya, M. R., Cascio, D., Rodriguez, J. A., Philipp, S., et al. (2019) · eLife · doi:10.7554/elife.46924 · Cited by 121
Self-citationA pair of peptides inhibits seeding of the hormone transporter transthyretin into amyloid fibrils
Saelices, L., Nguyen, B. A., Chung, K., Wang, Y., Ortega, A., Lee, J. H., Coelho, T., Bijzet, J., Benson, M. D., & Eisenberg, D. S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005257 · Cited by 43
Self-citationStructural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12
Tai, M. D. S., Ochoa, L., Flydal, M. I., Velasco-Carneros, L., Muntaner, J., Santiago, C., Gamiz-Arco, G., Moro, F., Jung-KC, K., Gil-Cantero, D., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57733-6 · Cited by 16
Metadata
- Authors
- Saelices, L., Johnson, L. M., Liang, W. Y., Sawaya, M. R., Cascio, D., Ruchala, P., Whitelegge, J., Jiang, L., Riek, R., & Eisenberg, D. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 290
- Issue
- 48
- Pages
- 28932-28943
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2266690651
- Cited by
- 158
- References
- 2
- FWCI
- 6.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Uncovering the Mechanism of Aggregation of Human Transthyretin. https://app.cochat.ai/papers/10.1074/jbc.m115.659912
- The paper
- Saelices, L., Johnson, L. M., Liang, W. Y., Sawaya, M. R., Cascio, D., Ruchala, P., Whitelegge, J., Jiang, L., Riek, R., & Eisenberg, D. S. (2015). Uncovering the Mechanism of Aggregation of Human Transthyretin. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m115.659912
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
