The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Native State Kinetic Stabilization as a Strategy To Ameliorate Protein Misfolding Diseases: A Focus on the Transthyretin Amyloidoses
Abstract
Small molecule-mediated protein stabilization inside or outside of the cell is a promising strategy to treat protein misfolding/misassembly diseases. Herein we focus on the transthyretin (TTR) amyloidoses and demonstrate that preferential ligand binding to and stabilization of the native state over the dissociative transition state raises the kinetic barrier of dissociation (rate-limiting for amyloidogenesis), slowing and in many cases preventing TTR amyloid fibril formation. Since T119M-TTR subunit incorporation into tetramers otherwise composed of disease-associated subunits also imparts kinetic stability on the tetramer and ameliorates amyloidosis in humans, it is likely that small molecule-mediated native state kinetic stabilization will also alleviate TTR amyloidoses.
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
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Cited by
Clinical and biomarker changes in dominantly inherited Alzheimer's disease
Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814
The amyloid state and its association with protein misfolding diseases.
Knowles, T. P. J., Vendruscolo, M., & Dobson, C. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3810 · Cited by 2,382
Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149
Self-citationHsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis
Wang, X., Venable, J., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J., Gurkan, C., Kellner, W., Matteson, J., Plutner, H., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.043 · Cited by 601
Self-citationOS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD
Christianson, J. C., Shaler, T. A., Tyler, R. E., & Kopito, R. R. (2008) · Nature Cell Biology · doi:10.1038/ncb1689 · Cited by 509
Modulators of Protein–Protein Interactions
Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497
Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles
Meade, R. M., Fairlie, D. P., & Mason, J. M. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0329-1 · Cited by 404
A molecular mechanism for transthyretin amyloidogenesis
Yee, A. W., Aldeghi, M., Blakeley, M. P., Ostermann, A., Mas, P. J., Moulin, M., de Sanctis, D., Bowler, M. W., Mueller-Dieckmann, C., Mitchell, E. P., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08609-z · Cited by 139
Cell and molecular biology of transthyretin and thyroid hormones
Richardson, S. J. (2007) · International Review of Cytology · doi:10.1016/s0074-7696(07)58003-4 · Cited by 116
Chemoselective small molecules that covalently modify one lysine in a non-enzyme protein in plasma
Choi, S., Connelly, S., Reixach, N., Wilson, I. A., & Kelly, J. W. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.281 · Cited by 90
Self-citationEmerging Therapies in Transthyretin Amyloidosis – A New Wave of Hope After Years of Stagnancy?
Müller, M. L., Butler, J., & Heidecker, B. (2020) · European Journal of Heart Failure · doi:10.1002/ejhf.1695 · Cited by 74
(2023) · doi:10.1021/acschemneuro.3c00007 · Cited by 8
Metadata
- Authors
- Johnson, S. M., Wiseman, R. L., Sekijima, Y., Green, N. S., Adamski-Werner, S. L., & Kelly, J. W.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-09-21
- Volume
- 38
- Issue
- 12
- Pages
- 911-921
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W2162710350
- Cited by
- 303
- References
- 1
- FWCI
- 5.07
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.
