The DOI matches its Crossref record; 78 of the 78 references it cites were found in a registry or an index.
Allosteric Disulfide Bonds
Abstract
Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when it breaks and/or forms. These bonds can be thought of as allosteric disulfides. To better define the properties of allosteric disulfides, we have analyzed the geometry and dihedral strain of 6874 unique disulfide bonds in 2776 X-ray structures. A total of 20 types of disulfide bonds were identified in the dataset based on the sign of the five chi angles that make up the bond. The known allosteric disulfides were all contained in 1 of the 20 groups, the -RHStaple bonds. This bond group has a high mean potential energy and narrow energy distribution, which is consistent with a functional role. We suggest that the -RHStaple configuration is a hallmark of allosteric disulfides. About 1 in 15 of all structurally determined disulfides is a potential allosteric bond.
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Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
The rapid generation of mutation data matrices from protein sequences
Jones, D. T., Taylor, W. R., & Thornton, J. M. (1992) · Bioinformatics · doi:10.1093/bioinformatics/8.3.275 · Cited by 6,947
Murzin, A. G., Brenner, S. E., Hubbard, T., & Chothia, C. (1995) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80134-2 · Cited by 6,445
A Production of Amino Acids Under Possible Primitive Earth Conditions
Miller, S. L. (1953) · Science · doi:10.1126/science.117.3046.528 · Cited by 3,522
Thioredoxin and Glutaredoxin Systems
Holmgren, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71625-6 · Cited by 1,796
TimeTree: A public knowledge-base of divergence times among organisms
Hedges, S. B., Dudley, J., & Kumar, S. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl505 · Cited by 1,234
Transglutaminases: Nature’s biological glues
GRIFFIN, M., CASADIO, R., & BERGAMINI, C. M. (2002) · Biochemical Journal · doi:10.1042/bj20021234 · Cited by 1,042
Broad tumor-associated expression and recognition by tumor-derived γδ T cells of MICA and MICB
Groh, V., Rhinehart, R., Secrist, H., Bauer, S., Grabstein, K. H., & Spies, T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6879 · Cited by 1,028
Groh, V, Bahram, S., Bauer, S., Herman, A., Beauchamp, M., & Spies, T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12445 · Cited by 1,017
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Furie, B., & Furie, B. C. (2008) · New England Journal of Medicine · doi:10.1056/nejmra0801082 · Cited by 1,926
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Filipovic, M. R., Zivanovic, J., Alvarez, B., & Banerjee, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00205 · Cited by 1,046
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Meyer, A. J., & Dick, T. P. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2948 · Cited by 527
Structural and Functional Characterization of Disulfide Isoforms of the Human IgG2 Subclass
Dillon, T. M., Ricci, M. S., Vezina, C., Flynn, G. C., Liu, Y. D., Rehder, D. S., Plant, M., Henkle, B., Li, Y., Deechongkit, S., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709988200 · Cited by 291
Gould, N. S., Evans, P., Martínez-Acedo, P., Marino, S. M., Gladyshev, V. N., Carroll, K. S., & Ischiropoulos, H. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.06.010 · Cited by 128
Metadata
- Authors
- Schmidt, B., Ho, L., & Hogg, P. J.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-05-24
- Volume
- 45
- Issue
- 24
- Pages
- 7429-7433
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2033972039
- Cited by
- 332
- References
- 78
- FWCI
- 5.89
- Type
- journal article
- Language
- en
- Open access
- closed
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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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