The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Analysis and Functional Prediction of Reactive Cysteine Residues
Open accessAbstract
Cys is much different from other common amino acids in proteins. Being one of the least abundant residues, Cys is often observed in functional sites in proteins. This residue is reactive, polarizable, and redox-active; has high affinity for metals; and is particularly responsive to the local environment. A better understanding of the basic properties of Cys is essential for interpretation of high-throughput data sets and for prediction and classification of functional Cys residues. We provide an overview of approaches used to study Cys residues, from methods for investigation of their basic properties, such as exposure and pK(a), to algorithms for functional prediction of different types of Cys in proteins.
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Cites
The FoldX web server: an online force field
Schymkowitz, J., Borg, J., Stricher, F., Nys, R., Rousseau, F., & Serrano, L. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki387 · Cited by 2,759 · cited 3×
“After analyzing the typical arrangement of Cys ligands around zinc coordination sites, the method can recognize similar structural patterns in terms of both the nature of ligands clustered in space and their relative geometries and therefore predict new metal-binding sites (50).”
MethodInfluentialProtein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153
PROSITE: a documented database using patterns and profiles as motif descriptors
Sigrist, C. J. A. (2002) · Briefings in Bioinformatics · doi:10.1093/bib/3.3.265 · Cited by 913 · cited 1×
“The simplest approach is the use of curated sequence patterns and profiles, such as those found in the PROSITE database (38).”
MethodReactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799
A universal trend of amino acid gain and loss in protein evolution
Jordan, I. K., Kondrashov, F. A., Adzhubei, I. A., Wolf, Y. I., Koonin, E. V., Kondrashov, A. S., & Sunyaev, S. (2005) · Nature · doi:10.1038/nature03306 · Cited by 297
The Triplet Code From First Principles
Trifonov, E. N. (2004) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2004.10506975 · Cited by 246
Pyrrolysine and Selenocysteine Use Dissimilar Decoding Strategies
Zhang, Y., Baranov, P. V., Atkins, J. F., & Gladyshev, V. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501458200 · Cited by 135
Self-citationSalsbury, F. R., Knutson, S. T., Poole, L. B., & Fetrow, J. S. (2008) · Protein Science · doi:10.1110/ps.073096508 · Cited by 125
Cited by
H2S signalling through protein sulfhydration and beyond
Paul, B. D., & Snyder, S. H. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3391 · Cited by 853
Flanagan, M. E., Abramite, J. A., Anderson, D. P., Aulabaugh, A., Dahal, U. P., Gilbert, A. M., Li, C., Montgomery, J., Oppenheimer, S. R., Ryder, T., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501412a · Cited by 320
Cysteine Oxidative Posttranslational Modifications: Emerging Regulation in the Cardiovascular System
Chung, H. S., Wang, S.-B., Venkatraman, V., Murray, C. I., & Van Eyk, J. E. (2013) · Circulation Research · doi:10.1161/circresaha.112.268680 · Cited by 300
Regulation of protein function and signaling by reversible cysteine S-nitrosylation
Gould, N., Doulias, P.-T., Tenopoulou, M., Raju, K., & Ischiropoulos, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.460261 · Cited by 274
The Diverse Functions of Non-Essential Amino Acids in Cancer
Choi, B.-H., & Coloff, J. L. (2019) · Cancers · doi:10.3390/cancers11050675 · Cited by 213
Metadata
- Authors
- Marino, S. M., & Gladyshev, V. N.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 287
- Issue
- 7
- Pages
- 4419-4425
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2085094809
- Cited by
- 270
- References
- 8
- FWCI
- 5.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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