The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Macromolecular Crowding Accelerates Amyloid Formation by Human Apolipoprotein C-II
Open accessAbstract
Human apolipoprotein C-II (apoC-II) slowly forms amyloid fibers in lipid-free solutions at physiological pH and salt concentrations (Hatters, D. M., MacPhee, C. E., Lawrence, L. J., Sawyer, W. H., and Howlett, G. J. (2000) Biochemistry 39, 8276--8283). Measurements of the time dependence of solution turbidity, thioflavin T reactivity, and the amount of sedimentable aggregate reveal that the rate and extent of amyloid formation are significantly increased by the addition of an inert polymer, dextran T10, at concentrations exceeding 20 g/liter. High dextran concentrations do not alter the secondary structure of the protein, fiber morphology, or the thioflavin T and Congo Red binding capacity of apoC-II amyloid. Analytical ultracentrifugation studies show that monomeric apoC-II does not associate significantly with dextran. The observed dependence of the overall rate of amyloid formation on dextran concentration may be accounted for quantitatively by a simple model for nonspecific volume exclusion. The model predicts that an increase in the fractional volume occupancy of macromolecules in a physiological fluid can nonspecifically accelerate the formation of amyloid fibers by any amyloidogenic protein.
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Conformational constraints for amyloid fibrillation: the importance of being unfolded
Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.12.008 · Cited by 1,015
Unusual biophysics of intrinsically disordered proteins
Uversky, V. N. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.008 · Cited by 566
What Macromolecular Crowding Can Do to a Protein
Kuznetsova, I., Turoverov, K., & Uversky, V. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151223090 · Cited by 564
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges
Hall, D., & Minton, A. P. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(03)00167-5 · Cited by 488
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Metadata
- Authors
- Hatters, D. M., Minton, A. P., & Howlett, G. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-03
- Volume
- 277
- Issue
- 10
- Pages
- 7824-7830
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2033212454
- Cited by
- 274
- References
- 44
- FWCI
- 7.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
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