The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
The Role of Thiols and Disulfides on Protein Stability
Open accessAbstract
There has been a tremendous increase in the number of approved drugs derived from recombinant proteins; however, their development as potential drugs has been hampered by their instability that causes difficulty to formulate them as therapeutic agents. It has been shown that the reactivity of thiol and disulfide functional groups could catalyze chemical (i.e., oxidation and beta-elimination reactions) and physical (i.e., aggregation and precipitation) degradations of proteins. Because most proteins contain a free Cys residue or/and a disulfide bond, this review is focused on their roles in the physical and chemical stability of proteins. The effect of introducing a disulfide bond to improve physical stability of proteins and the mechanisms of degradation of disulfide bond were discussed. The qualitative/quantitative methods to determine the presence of thiol in the Cys residue and various methods to derivatize thiol group for improving protein stability were also illustrated.
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Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,311
Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
Sedlak, J., & Lindsay, R. H. (1968) · Analytical Biochemistry · doi:10.1016/0003-2697(68)90092-4 · Cited by 8,077
The Anatomy and Taxonomy of Protein Structure
Richardson, J. S. (1981) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,375
Cadherin Cell Adhesion Receptors as a Morphogenetic Regulator
Takeichi, M. (1991) · Science · doi:10.1126/science.2006419 · Cited by 3,284
Wishart, D., & Sykes, B. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00175245 · Cited by 2,143
Wishart, D. S., Sykes, B. D., & Richards, F. M. (1992) · Biochemistry · doi:10.1021/bi00121a010 · Cited by 2,051
Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
Wishart, D. S., Sykes, B. D., & Richards, F. M. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90214-q · Cited by 1,902
Stability of Protein Pharmaceuticals
Manning, M. C., Patel, K., & Borchardt, R. T. (1989) · Pharmaceutical Research · doi:10.1023/a:1015929109894 · Cited by 1,078
Disulfide Bonds and Protein Folding
Wedemeyer, W. J., Welker, E., Narayan, M., & Scheraga, H. A. (2000) · Biochemistry · doi:10.1021/bi992922o · Cited by 621
Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4′-dithiodipyridine
Riener, C. K., Kada, G., & Gruber, H. J. (2002) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-002-1347-2 · Cited by 564
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The biology of reactive sulfur species (RSS)
Gruhlke, M. C. H., & Slusarenko, A. J. (2012) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2012.03.016 · Cited by 274
Formulation, Delivery and Stability of Bone Morphogenetic Proteins for Effective Bone Regeneration
El Bialy, I., Jiskoot, W., & Reza Nejadnik, M. (2017) · Pharmaceutical Research · doi:10.1007/s11095-017-2147-x · Cited by 257
Effects of PCSK9 Targeting: Alleviating Oxidation, Inflammation, and Atherosclerosis
Punch, E., Klein, J., Diaba‐Nuhoho, P., Morawietz, H., & Garelnabi, M. (2022) · Journal of the American Heart Association · doi:10.1161/jaha.121.023328 · Cited by 101
Clemente, A., Sonnante, G., & Domoney, C. (2011) · Current Protein & Peptide Science · doi:10.2174/138920311796391133 · Cited by 63
Butler, V. J., Gao, F., Corrales, C. I., Cortopassi, W. A., Caballero, B., Vohra, M., Ashrafi, K., Cuervo, A. M., Jacobson, M. P., Coppola, G., et al. (2019) · PLOS Genetics · doi:10.1371/journal.pgen.1008295 · Cited by 39
Metadata
- Authors
- Trivedi, M., Laurence, J., & Siahaan, T.
- Venue
- Current Protein & Peptide Science
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2009-12-01
- Volume
- 10
- Issue
- 6
- Pages
- 614-625
- ISSN
- 1389-2037 (ISSN-L)
- OpenAlex
- W2151737415
- Cited by
- 406
- References
- 59
- FWCI
- 3.12
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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