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Targeting Receptor-Type Protein Tyrosine Phosphatases with Biotherapeutics: Is Outside-in Better than Inside-Out?
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- Molecules, 2018, v. 23, n. 3, p. 569, doi. 10.3390/molecules23030569
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- Article
The biochemical basis of disease.
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- Essays in Biochemistry, 2018, v. 62, n. 5, p. 619, doi. 10.1042/EBC20170054
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- Article
Analysis of Receptor-Type Protein Tyrosine Phosphatase Extracellular Regions with Insights from AlphaFold.
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- International Journal of Molecular Sciences, 2024, v. 25, n. 2, p. 820, doi. 10.3390/ijms25020820
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- Article
The crystal structure of human receptor protein tyrosine phosphatase κ phosphatase domain 1.
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- Protein Science: A Publication of the Protein Society, 2006, v. 15, n. 6, p. 1500, doi. 10.1110/ps.062128706
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- Article
HD-PTP Is a Catalytically Inactive Tyrosine Phosphatase Due to a Conserved Divergence in Its Phosphatase Domain.
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- PLoS ONE, 2009, v. 4, n. 4, p. 1, doi. 10.1371/journal.pone.0005105
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- Article
Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-Å resolution.
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- Proteins, 2006, v. 63, n. 4, p. 1132, doi. 10.1002/prot.20958
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- Article
Defining the molecular basis of interaction between R3 receptor-type protein tyrosine phosphatases and VE-cadherin.
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- PLoS ONE, 2017, v. 12, n. 9, p. 1, doi. 10.1371/journal.pone.0184574
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- Article