A pair of peptides inhibits seeding of the hormone transporter transthyretin into amyloid fibrils
Open accessAbstract
The tetrameric protein transthyretin is a transporter of retinol and thyroxine in blood, cerebrospinal fluid, and the eye, and is secreted by the liver, choroid plexus, and retinal epithelium, respectively. Systemic amyloid deposition of aggregated transthyretin causes hereditary and sporadic amyloidoses. A common treatment of patients with hereditary transthyretin amyloidosis is liver transplantation. However, this procedure, which replaces the patient's variant transthyretin with the WT protein, can fail to stop subsequent cardiac deposition, ultimately requiring heart transplantation. We recently showed that preformed amyloid fibrils present in the heart at the time of surgery can template or seed further amyloid aggregation of native transthyretin. Here we assess possible interventions to halt this seeding, using biochemical and EM assays. We found that chemical or mutational stabilization of the transthyretin tetramer does not hinder amyloid seeding. In contrast, binding of the peptide inhibitor TabFH2 to ex vivo fibrils efficiently inhibits amyloid seeding by impeding self-association of the amyloid-driving strands F and H in a tissue-independent manner. Our findings point to inhibition of amyloid seeding by peptide inhibitors as a potential therapeutic approach.
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
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Short peptides with altered amino acid sequences that target cross-sectional interfaces have been successfully employed in capping of various amyloid fibrils and inhibition of seeding.
“Notably, short peptides with altered amino acid sequences that target the cross-sectional interfaces of aggregation-prone regions have been successfully employed in the capping of various amyloid fibrils and the inhibition of seeding (63, 64, 65, 66).”
From MAP2 caps tau fibrils and inhibits aggregation (2023) · cites this paper as [64]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
ON THE BINDING OF CONGO RED BY AMYLOID
Puchtler, H., Sweat, F., & Levine, M. I. (1962) · Journal of Histochemistry & Cytochemistry · doi:10.1177/10.3.355 · Cited by 1,136 · see citing works
Tafamidis for transthyretin familial amyloid polyneuropathy
Coelho, T., Maia, L. F., SILVA, A. C. F. D., Waddington‐Cruz, M., Planté‐Bordeneuve, V., Lozeron, P., Suhr, O. B., Campistol, J. M., Conceição, I. M., Schmidt, H., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e3182661eb1 · Cited by 812 · see citing works
Self-citationTafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade
Bulawa, C., Connelly, S., DeVit, M. J., Wang, L., Weigel, C., Fleming, J., Packman, J., Powers, E. T., Wiseman, R. L., Foss, T. R., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121005109 · Cited by 750 · see citing works
Repurposing Diflunisal for Familial Amyloid Polyneuropathy
Berk, J. L., Suhr, O. B., Obici, L. P., Sekijima, Y., Zeldenrust, S. R., Yamashita, T., Heneghan, M. A., Gorevic, P. D., Litchy, W. J., Wiesman, J. F., et al. (2013) · JAMA · doi:10.1001/jama.2013.283815 · Cited by 709 · see citing works
Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics
Hammarström, P., Wiseman, R. L., Powers, E. T., & Kelly, J. W. (2003) · Science · doi:10.1126/science.1079589 · Cited by 526 · see citing works
Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation
Sievers, S. A., Karanicolas, J., Chang, H. W., Zhao, A., Jiang, L., Zirafi, O., Stevens, J. T., Münch, J., Baker, D. A., & Eisenberg, D. S. (2011) · Nature · doi:10.1038/nature10154 · Cited by 459 · see citing works
Self-citationSenile Systemic Amyloidosis: Clinical Features at Presentation and Outcome
Pinney, J. H., Whelan, C. J., Petrie, A., Dungu, J. N., Banypersad, S. M., Sattianayagam, P. T., Wechalekar, A. D., Gibbs, S. D., Venner, C. P., Wassef, N., et al. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000098 · Cited by 372 · see citing works
Inhibiting transthyretin amyloid fibril formation via protein stabilization
Miroy, G. J., Lai, Z., Lashuel, H. A., Peterson, S., Strang, C. J., & Kelly, J. W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15051 · Cited by 347 · see citing works
A Designed Inhibitor of p53 Aggregation Rescues p53 Tumor Suppression in Ovarian Carcinomas
Soragni, A., Janzen, D. M., Johnson, L. M., Lindgren, A. G., Thai-Quynh Nguyen, A., Tiourin, E., Soriaga, A. B., Lu, J., Jiang, L., Faull, K. F., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2015.12.002 · Cited by 341 · see citing works
Self-citationTransthyretin Aggregation under Partially Denaturing Conditions Is a Downhill Polymerization
Hurshman, A. R., White, J. T., Powers, E. T., & Kelly, J. W. (2004) · Biochemistry · doi:10.1021/bi049621l · Cited by 340 · see citing works
Structure-based inhibitors of tau aggregation
Seidler, P. M., Boyer, D. R., Rodríguez, J. A., Sawaya, M. R., Cascio, D., Murray, K. A., Gonen, T., & Eisenberg, D. S. (2017) · Nature Chemistry · doi:10.1038/nchem.2889 · Cited by 338 · see citing works
Self-citationBergström, J. J. E., Gustavsson, Å., Hellman, U., Sletten, K., Murphy, C. L., Weiss, D. T., Solomon, A., Olofsson, B., & Westermark, P. (2005) · The Journal of Pathology · doi:10.1002/path.1759 · Cited by 248 · see citing works
Adamski‐Werner, S. L., Palaninathan, S. K., Sacchettini, J. C., & Kelly, J. W. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm030347n · Cited by 231 · see citing works
Comparison of Lethal and Nonlethal Transthyretin Variants and Their Relationship to Amyloid Disease
McCutchen, S. L., Lai, Z., Miroy, G. J., Kelly, J. W., & Colón, W. (1995) · Biochemistry · doi:10.1021/bi00041a032 · Cited by 200 · see citing works
The Pathway by Which the Tetrameric Protein Transthyretin Dissociates
Foss, T. R., Wiseman, R. L., & Kelly, J. W. (2005) · Biochemistry · doi:10.1021/bi051608t · Cited by 194 · see citing works
Yazaki, M., Tokuda, T., Nakamura, A., Higashikata, T., Koyama, J., Higuchi, K., Harihara, Y., Baba, S., Kametani, F., & Ikeda, S. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3203 · Cited by 168 · see citing works
Uncovering the Mechanism of Aggregation of Human Transthyretin
Saelices, L., Johnson, L. M., Liang, W. Y., Sawaya, M. R., Cascio, D., Ruchala, P. P., Whitelegge, J. P., Jiang, L., Riek, R., & Eisenberg, D. S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.659912 · Cited by 160 · see citing works
Self-citationDiflunisal for ATTR Cardiac Amyloidosis
Castaño, A., Helmke, S. T., Alvarez, J., Delisle, S., & Maurer, M. S. (2012) · Congestive Heart Failure · doi:10.1111/j.1751-7133.2012.00303.x · Cited by 156 · see citing works
Lozeron, P., Théaudin, M., Mincheva, Z., Ducot, B., Lacroix, C., Adams, D., & French Network for FAP (CORNAMYL) (2013) · European Journal of Neurology · doi:10.1111/ene.12225 · Cited by 129 · see citing works
Sekijima, Y., Tojo, K., Morita, H., Koyama, J., & Ikeda, S. (2015) · Amyloid · doi:10.3109/13506129.2014.997872 · Cited by 128 · see citing works
Liver transplantation and transthyretin amyloidosis
Benson, M. D. (2012) · Muscle & Nerve · doi:10.1002/mus.23521 · Cited by 115 · see citing works
Self-citationWaddington‐Cruz, M., Amass, L., Keohane, D. J., Schwartz, J., Li, H., & Gundapaneni, B. K. (2016) · Amyloid · doi:10.1080/13506129.2016.1207163 · Cited by 109 · see citing works
Planté‐Bordeneuve, V., Gorram, F., Salhi, H., Nordine, T., Ayache, S. S., Corvoisier, P. L., Azoulay, D., Féray, C., Damy, T., & Lefaucheur, J. (2016) · Journal of Neurology · doi:10.1007/s00415-016-8337-3 · Cited by 108 · see citing works
Amyloid seeding of transthyretin by ex vivo cardiac fibrils and its inhibition
Saelices, L., Chung, K., Lee, J. H., Cohn, W., Whitelegge, J. P., Benson, M. D., & Eisenberg, D. S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805131115 · Cited by 98 · see citing works
Self-citationNovel conformation-specific monoclonal antibodies against amyloidogenic forms of transthyretin
Higaki, J. N., Chakrabartty, A., Galant, N. J., Hadley, K. C., Hammerson, B., Nijjar, T., Torres, R., Tapia, J. R., Salmans, J., Barbour, R., et al. (2016) · Amyloid · doi:10.3109/13506129.2016.1148025 · Cited by 88 · see citing works
A Review of Tafamidis for the Treatment of Transthyretin-Related Amyloidosis
Waddington‐Cruz, M., & Benson, M. D. (2015) · Neurology and Therapy · doi:10.1007/s40120-015-0031-3 · Cited by 80 · see citing works
Self-citationTransthyretin amyloidosis: an under-recognized neuropathy and cardiomyopathy
Galant, N. J., Westermark, P., Higaki, J. N., & Chakrabartty, A. (2017) · Clinical Science · doi:10.1042/cs20160413 · Cited by 79 · see citing works
Coelho, T., Chorão, R., Sousa, A., Alves, I. L., Torres, M. F., & Saraiva, M. J. (1996) · Neuromuscular Disorders · doi:10.1016/0960-8966(96)88826-2 · Cited by 61 · see citing works
Self-citationHazenberg, B. P. C., Limburg, P. C., Bijzet, J., & van Rijswijk, M. H. (1999) · Annals of the Rheumatic Diseases · doi:10.1136/ard.58.2.96 · Cited by 54 · see citing works
Self-citationObici, L. P., & Merlini, G. (2014) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2014.922541 · Cited by 49 · see citing works
Novel Antibody for the Treatment of Transthyretin Amyloidosis
Hosoi, A., Su, Y., Torikai, M., Jono, H., Ishikawa, D., Soejima, K., Higuchi, H., Guo, J., Ueda, M., Suenaga, G., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.738138 · Cited by 47 · see citing works
Saelices, L., Pokrzywa, M., Pawełek, K., & Eisenberg, D. S. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.09.007 · Cited by 15 · see citing works
Self-citationTafamidis for the Treatment of Hereditary Transthyretin Amyloid Cardiomyopathy: A Case Report
Fujita, T., Inomata, T., Kaida, T., Iida, Y., Ikeda, Y., Nabeta, T., Ishii, S., Maekawa, E., Naruke, T., Koitabashi, T., et al. (2017) · Cardiology · doi:10.1159/000455089 · Cited by 7 · see citing works
Flagged first, then by citations
3 of the 36 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Mechanisms and pathology of protein misfolding and aggregation
Louros, N. N., Schymkowitz, J. W. H., & Rousseau, F. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00647-2 · Cited by 259 · see citing works
Pathophysiology and Therapeutic Approaches to Cardiac Amyloidosis
Griffin, J. M., Rosenblum, H., & Maurer, M. S. (2021) · Circulation Research · doi:10.1161/circresaha.121.318187 · Cited by 216 · see citing works
ATTR Amyloidosis: Current and Emerging Management Strategies
Griffin, J. M., Rosenthal, J., Grodin, J. L., Maurer, M. S., Grogan, M. A., & Cheng, R. K.-H. (2021) · JACC CardioOncology · doi:10.1016/j.jaccao.2021.06.006 · Cited by 169 · see citing works
Luigetti, M., Romano, Â., Paolantonio, A. D., Bisogni, G., & Sabatelli, M. (2020) · Therapeutics and Clinical Risk Management · doi:10.2147/tcrm.s219979 · Cited by 149 · see citing works
Molecular Mechanisms of Cardiac Amyloidosis
Saito, Y., Nakamura, K., & Ito, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010025 · Cited by 57 · see citing works
Molecular mechanisms and emerging therapies in wild-type transthyretin amyloid cardiomyopathy
Wu, D., & Chen, W. (2024) · Heart Failure Reviews · doi:10.1007/s10741-023-10380-9 · Cited by 34 · see citing works
Dissolution of a fibrous peptide by terahertz free electron laser
Kawasaki, T., Tsukiyama∥, K., & Irizawa, A. (2019) · Scientific Reports · doi:10.1038/s41598-019-47011-z · Cited by 33 · see citing works
Russo, M., Gentile, L., Stefano, V. D., Bella, G. D., Minutoli, F., Toscano, A., Brighina, F., Vita, G., & Mazzeo, A. T. (2021) · Brain Sciences · doi:10.3390/brainsci11050545 · Cited by 32 · see citing works
Amyloid seeding as a disease mechanism and treatment target in transthyretin cardiac amyloidosis
Morfino, P., Aimo, A., Panichella, G., Rapezzi, C., & Emdin, M. (2022) · Heart Failure Reviews · doi:10.1007/s10741-022-10237-7 · Cited by 33 · see citing works
Promotion Effect of Succinimide on Amyloid Fibrillation of Hen Egg-White Lysozyme
Fan, W., Xing, L., Chen, N., Zhou, X., Yu, Y., & Liu, S. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b06958 · Cited by 31 · see citing works
Louros, N., Ramakers, M., Michiels, E., Konstantoulea, K., Morelli, C., Garcia, T., Moonen, N., D’Haeyer, S., Goossens, V., Thal, D. R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28955-9 · Cited by 28 · see citing works
The inhibition of cellular toxicity of amyloid-β by dissociated transthyretin
Cao, Q., Anderson, D. H., Liang, W. Y., Chou, J., & Saelices, L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013440 · Cited by 27 · see citing works
Self-citationRole of conformational dynamics in pathogenic protein aggregation
Sun, X., Dyson, H. J., & Wright, P. E. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102280 · Cited by 23 · see citing works
Morfino, P., Aimo, A., Vergaro, G., Sanguinetti, C., Castiglione, V., Franzini, M., Perrone, M. A., & Emdin, M. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15041129 · Cited by 23 · see citing works
Transthyretin mutagenesis: impact on amyloidogenesis and disease
Almeida, Z. L., Vaz, D. C., & Brito, R. M. M. (2024) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2024.2350379 · Cited by 22 · see citing works
Peña‐Díaz, S., Pujols, J., Pinheiro, F., Santos, J., Pallarès, I., Navarro, S., Conde-Giménez, M., García, J., Salvatella, X., Dalfó, E., et al. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.588947 · Cited by 22 · see citing works
Heterotypic amyloid interactions: Clues to polymorphic bias and selective cellular vulnerability?
Louros, N. N., Schymkowitz, J. W. H., & Rousseau, F. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.11.007 · Cited by 21 · see citing works
Rational Drug Design of Peptide-Based Therapies for Sickle Cell Disease
Olubiyi, O. O., Olagunju, M. O., & Strodel, B. (2019) · Molecules · doi:10.3390/molecules24244551 · Cited by 18 · see citing works
Pedretti, R., Wang, L., Yakubovska, A., Zhang, Q. S., Nguyen, B. A., Grodin, J. L., Masri, A., & Saelices, L. (2024) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2024.05.013 · Cited by 16 · see citing works
Self-citationAdvances in Treatment of ATTRv Amyloidosis: State of the Art and Future Prospects
Russo, M., Gentile, L., Toscano, A., Aguennouz, M., Vita, G., & Mazzeo, A. (2020) · Brain Science · doi:10.3390/brainsci10120952 · Cited by 17 · see citing works
MAP2 caps tau fibrils and inhibits aggregation
Holden, M. R., Krzesinski, B. J., Weismiller, H. A., Shady, J. R., & Margittai, M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104891 · Cited by 13 · see citing works
Etiological Treatment of Cardiac Amyloidosis: Standard of Care and Future Directions
Chen, Y. F. F., Aimo, A., Castiglione, V., Chubuchna, O., Morfino, P., Fabiani, I., Buda, G., Emdin, M., & Vergaro, G. (2025) · Current Heart Failure Reports · doi:10.1007/s11897-025-00701-4 · Cited by 13 · see citing works
Fragment-Based Ab Initio Phasing of Peptidic Nanocrystals by MicroED
Richards, L. S., Flores, M. D., Millán, C., Glynn, C. A., Zee, C.-T., Sawaya, M. R., Gallagher-Jones, M., Borges, R. J., Usón, I., & Rodríguez, J. A. (2023) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.2c00082 · Cited by 12 · see citing works
Pathophysiology of Cardiac Amyloidosis
Morfino, P., Aimo, A., Franzini, M., Vergaro, G., Castiglione, V., Panichella, G., Limongelli, G., & Emdin, M. (2024) · Heart Failure Clinics · doi:10.1016/j.hfc.2024.02.002 · Cited by 11 · see citing works
Luo, Y.-C., & Jing, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218207 · Cited by 9 · see citing works
Zhou, J., Li, Y., Geng, J., Zhou, H., Liu, L., & Peng, X. (2023) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001478 · Cited by 9 · see citing works
Current and emerging treatment options for transthyretin amyloid cardiomyopathy
Vergaro, G., Chen, Y. F. F., Ioannou, A., Panichella, G., Castiglione, V., Aimo, A., Emdin, M., & Fontana, M. (2025) · Heart · doi:10.1136/heartjnl-2024-325184 · Cited by 7 · see citing works
Zhang, Y., Zhu, Y., Yue, H., Zhao, Q., & Li, H. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.982276 · Cited by 6 · see citing works
Optimizing drug therapies in cardiac amyloidosis.
Younis, M. F., Ogbu, I., & Kalra, D. K. (2024) · Pharmacology and Therapeutics · doi:10.1016/j.pharmthera.2024.108758 · Cited by 6 · see citing works
Structures and Dynamics of β-Rich Oligomers of ATTR (105–115) Assembly
Liang, L., Zhang, Y., Zhu, Y., Bai, J., Ni, Y., Wan, J., Yue, H., Zhao, Q., & Li, H. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00574 · Cited by 5 · see citing works
Mechanism of inhibition of acid-mediated transthyretin aggregation by designed peptides
Sun, X., Pedretti, R., Dyson, H. J., Saelices, L., & Wright, P. E. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110594 · Cited by 4 · see citing works
Self-citationHazarika, Z., & Jha, A. N. (2024) · Inorganica Chimica Acta · doi:10.1016/j.ica.2024.121923 · Cited by 4 · see citing works
The Discovery and Development of Transthyretin Amyloidogenesis Inhibitors: What are the Lessons?
Zhong, B., Huang, X., Zheng, Y., Guo, X., & Wu, L. (2021) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0248 · Cited by 2 · see citing works
Biomarkers in Subclinical Transthyretin Cardiac Amyloidosis
Gulati, J. S., Pedretti, R., HENDREN, N. S., Kozlitina, J., Saelices, L., Roth, L. R., & Grodin, J. L. (2025) · Current Heart Failure Reports · doi:10.1007/s11897-025-00696-y · Cited by 2 · see citing works
Self-citationBhattacharya, P., & Mittal, S. (2025) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.70046 · Cited by 1 · see citing works
Yan, X., Cao, Y., Xu, Z., Zhu, Y., Zhao, Q., Li, H., & Chen, Y. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp03218k · Cited by 1 · see citing works
The Physical Driving Forces of Conformational Transition for TTR91–96 with Proline Mutations
Cao, Y., Xia, P., Zhu, Y., Zhao, Q., & Li, H. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01464 · Cited by 1 · see citing works
Treatment Updates for Neuropathy in Hereditary Transthyretin Amyloidosis
King, D., Lau, K. H. V., & Kaku, M. C. (2023) · Current Treatment Options in Neurology · doi:10.1007/s11940-023-00754-7 · Cited by 1 · see citing works
Advances in understanding, diagnosis and targeting ATTR cardiomyopathy: a review
Kulak, M., Lang, M., Waśniewski, M., & Lange, N. (2024) · European Journal of Translational and Clinical Medicine · doi:10.31373/ejtcm/189121
Liu, Y., Li, X., Xin, A., Zhang, Y., & Zhang, J. (2025) · International Journal of Medical Sciences · doi:10.7150/ijms.101888
Kim, M. K., Cho, S., Choi, Y., & Jung, D. (2025) · Journal of Experimental & Biomedical Sciences/Biomedical Science Letters · doi:10.15616/bsl.2025.31.1.49
Ghosh, S., Khanra, D., Kala, C., Krishna, V., & Thakur, A. (2025) · Journal of Association of Physicians of India · doi:10.59556/japi.73.1050
Quantifying species-specific binding affinities of transthyretin aggregation inhibitors
Sun, X., Dyson, H. J., & Wright, P. E. (2026) · Biophysical Reports · doi:10.1016/j.bpr.2026.100274
- Authors
- Saelices, L., Nguyen, B. A., Chung, K., Wang, Y., Ortega, A., Lee, J. H., Coelho, T., Bijzet, J., Benson, M. D., & Eisenberg, D. S.
- Affiliations
- Howard Hughes Medical Institute (US)
- Hospital de Santo António (PT)
- University Medical Center Groningen (NL)
- Indiana University Indianapolis (US)
- Corresponding author
- Eisenberg, David S.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-04
- Volume
- 294
- Issue
- 15
- Pages
- 6130-6141
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC6463714
- OpenAlex
- W2911892577
- Cited by
- 43
- References
- 36
- Citations by year
- 2026: 1 · 2025: 9 · 2024: 9 · 2023: 7 · 2022: 3 · 2021: 6 · 2020: 5 · 2019: 3
- FWCI
- 1.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, cc-by)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- IUScholarWorks (Indiana University) (submittedVersion)
- Purdue University Indianapolis (Indiana University) (submittedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion, cc-by)
- PMC
- Funders
- HHS | National Institutes of Health (AG048120)
- Amyloidosis Foundation (20160759, 20170827)
- Howard Hughes Medical Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- prealbumin, amyloid fibrils, amyloid seeding, hereditary transthyretin amyloidosis, peptide inhibitors, tetramer stabilization, amyloid fibril formation, amyloidosis treatment
- MeSH terms
- Aged, Aged, 80 and over, Amyloid, Female, Humans, Male, Middle Aged, Peptides, Prealbumin, Amyloid Neuropathies, Familial, Protein Aggregates
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
