The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses
Open accessAbstract
Small molecules that bind to normally unoccupied thyroxine (T4) binding sites within transthyretin (TTR) in the blood stabilize the tetrameric ground state of TTR relative to the dissociative transition state and dramatically slow tetramer dissociation, the rate-limiting step for the process of amyloid fibril formation linked to neurodegeneration and cell death. These so-called TTR kinetic stabilizers have been designed using structure-based principles and one of these has recently been shown to halt the progression of a human TTR amyloid disease in a clinical trial, providing the first pharmacologic evidence that the process of amyloid fibril formation is causative. Structure-based design has now progressed to the point where highly selective, high affinity TTR kinetic stabilizers that lack undesirable off-target activities can be produced with high frequency.
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Cites
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
Naylor, H. M., & Newcomer, M. E. (1999) · Biochemistry · doi:10.1021/bi982291i · Cited by 188
Crystal Structure of the Transthyretin–Retinoic‐Acid Complex
Zanotti, G., D'acunto, M. R., Malpeli, G., Folli, C., & Berni, R. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.563_b.x · Cited by 40
Cited by
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
Bartels, T., Choi, J. G., & Selkoe, D. J. (2011) · Nature · doi:10.1038/nature10324 · Cited by 1,263
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
Hereditary transthyretin amyloidosis: a model of medical progress for a fatal disease
Adams, D., Koike, H., Slama, M., & Coelho, T. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0210-4 · Cited by 448
Targeting protein aggregation for the treatment of degenerative diseases
Eisele, Y. S., Monteiro, C., Fearns, C., Encalada, S. E., Wiseman, R. L., Powers, E. T., & Kelly, J. W. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4593 · Cited by 419
Self-citationJackson, S. E. (2012) · Topics in Current Chemistry · doi:10.1007/128_2012_356 · Cited by 338
Metadata
- Authors
- Connelly, S., Choi, S., Johnson, S. M., Kelly, J. W., & Wilson, I. A.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 20
- Issue
- 1
- Pages
- 54-62
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2011540010
- Cited by
- 176
- References
- 3
- FWCI
- 8.86
- Type
- journal article
- Language
- en
- Open access
- green
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- Connelly, S., Choi, S., Johnson, S. M., Kelly, J. W., & Wilson, I. A. (2010). Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses. Current Opinion in Structural Biology. https://doi.org/10.1016/j.sbi.2009.12.009
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