The DOI matches its Crossref record; 142 of the 142 references it cites were found in a registry or an index.
Protein tyrosine phosphatase function: the substrate perspective
Open accessAbstract
It is now well established that the members of the PTP (protein tyrosine phosphatase) superfamily play critical roles in fundamental biological processes. Although there has been much progress in defining the function of PTPs, the task of identifying substrates for these enzymes still presents a challenge. Many PTPs have yet to have their physiological substrates identified. The focus of this review will be on the current state of knowledge of PTP substrates and the approaches used to identify them. We propose experimental criteria that should be satisfied in order to rigorously assign PTP substrates as bona fide. Finally, the progress that has been made in defining the biological roles of PTPs through the identification of their substrates will be discussed.
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2 retracted
Aoki, N., & Matsuda, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005615200 · Cited by 179
RetractedAoki, N., & Matsuda, T. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.1.0761 · Cited by 119
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Phosphorylation-Dephosphorylation of Enzymes
Krebs, E. G., & Beavo, J. A. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.004423 · Cited by 2,205
Protein Tyrosine Phosphatases in the Human Genome
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Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome
Tartaglia, M., Mehler, E. L., Goldberg, R., Zampino, G., Brunner, H. G., Kremer, H., van der Burgt, I., Crosby, A. H., Ion, A., Jeffery, S., et al. (2001) · Nature Genetics · doi:10.1038/ng772 · Cited by 1,733
Protein tyrosine phosphatases: from genes, to function, to disease
Tonks, N. K. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2039 · Cited by 1,677
The ‘Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling
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Klaman, L. D., Boss, O., Peroni, O. D., Kim, J. K., Martino, J. L., Zabolotny, J. M., Moghal, N., Lubkin, M., Kim, Y.-B., Sharpe, A. H., et al. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5479-5489.2000 · Cited by 1,235
SHP-2 Tyrosine Phosphatase as an Intracellular Target of Helicobacter pylori CagA Protein
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Obesity Drives STAT-1-Dependent NASH and STAT-3-Dependent HCC
Grohmann, M., Wiede, F., Dodd, G. T., Gurzov, E. N., Ooi, G. J., Butt, T., Rasmiena, A. A., Kaur, S., Gulati, T., Goh, P. K., et al. (2018) · Cell · doi:10.1016/j.cell.2018.09.053 · Cited by 373
Self-citationGarcia Fortanet, J., Chen, C. H.-T., Chen, Y.-N. P., Chen, Z., Deng, Z., Firestone, B., Fekkes, P., Fodor, M., Fortin, P. D., Fridrich, C., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00680 · Cited by 298
Reactive oxygen species and insulin resistance: the good, the bad and the ugly
Tiganis, T. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.11.006 · Cited by 256
Self-citationIdentification of TNO155, an Allosteric SHP2 Inhibitor for the Treatment of Cancer
LaMarche, M. J., Acker, M., Argintaru, A., Bauer, D., Boisclair, J., Chan, H., Chen, C. H.-T., Chen, Y.-N., Chen, Z., Deng, Z., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01170 · Cited by 231
Metadata
- Authors
- Tiganis, T., & Bennett, A. M.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2007-01-25
- Volume
- 402
- Issue
- 1
- Pages
- 1-15
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1982486689
- Cited by
- 297
- References
- 142
- FWCI
- 6.70
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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