The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Inhibition of insulin amyloid formation by small stress molecules
Open accessAbstract
Amyloidogenic proteins undergo an alternative folding pathway under stressful conditions leading to formation of fibrils having cross β‐sheet structure, which is the hallmark of many neurodegenerative diseases. As a means of surviving against external stress, on the other hand, many microorganisms accumulate small stress molecules to prevent abnormal protein folding and to contribute to protein stability, which hints at the efficacy of the solutes against amyloid formation. The current work demonstrates the effectiveness of small stress molecules such as ectoine, betaine, trehalose, and citrulline on inhibition of insulin amyloid formation in vitro. The inhibitory effects were analyzed by thioflavin T‐induced fluorescence, circular dichroism, and atomic force microscopy. This report suggests that naturally occurring small molecules may serve a function that is typically fulfilled by protein chaperones, and it provides a hint for designing inhibitors against amyloid formation associated with neurodegenerative disorders.
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Cites
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227
Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061
Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand
Tjernberg, L. O., Näslund, J., Lindqvist, F., Johansson, J., Karlström, A. R., Thyberg, J., Terenius, L., & Nordstedt, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8545 · Cited by 963
Cited by
Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142
Extremolytes: natural compounds from extremophiles for versatile applications
Lentzen, G., & Schwarz, T. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0553-9 · Cited by 340
Rodríguez-Navarro, J. A., Rodríguez, L., Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., Cuervo, A. M., García de Yébenes, J., & Mena, M. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.014 · Cited by 298
Davies, J. E., Sarkar, S., & Rubinsztein, D. C. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi422 · Cited by 207
Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., de Yébenes, J. G., & Mena, M. A. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.01.008 · Cited by 114
Metadata
- Authors
- Arora, A., Ha, C., & Park, C. B.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2004-04-09
- Volume
- 564
- Issue
- 1-2
- Pages
- 121-125
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1979306731
- Cited by
- 228
- References
- 3
- FWCI
- 4.94
- Type
- journal article
- Language
- en
- Open access
- bronze
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