Tyrosine phosphatase activity is restricted by basic charge substituting mutation of substrates
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2045-2322
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
-
Tyrosine phosphatase activity is restricted by basic charge substituting mutation of substrates ; volume:12 ; number:1 ; day:5 ; month:9 ; year:2022 ; pages:1-9 ; date:12.2022
Scientific reports ; 12, Heft 1 (5.9.2022), 1-9, 12.2022
- Creator
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Huang, Che-Fan
Gottardi, Cara J.
Mrksich, Milan
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41598-022-19133-4
- URN
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urn:nbn:de:101:1-2022112221114112198906
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:37 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Huang, Che-Fan
- Gottardi, Cara J.
- Mrksich, Milan
- SpringerLink (Online service)
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Identification of a variant form of tyrosine phosphatase LYP
Interaction of the disordered Gab1 with tyrosine phosphatase Shp2
Regulation of autoimmune arthritis by the SHP-1 tyrosine phosphatase
Synthesis, characterization and application of stabilized natural substrates as protein tyrosine phosphatase inhibitors
Synthesis, Characterization and Application of Stabilized Natural Substrates as Protein Tyrosine Phosphatase Inhibitors
Identification of protein tyrosine phosphatase 1B and casein as substrates for 124-v-Mos
Investigations of Protein Tyrosine Phosphatase Functions
Small Molecule Degraders of Protein Tyrosine Phosphatase 1B and T‐Cell Protein Tyrosine Phosphatase for Cancer Immunotherapy
Small Molecule Degraders of Protein Tyrosine Phosphatase 1B and T‐Cell Protein Tyrosine Phosphatase for Cancer Immunotherapy
Protein tyrosine phosphatase PTP-RR regulates corticosteroid sensitivity
Multipartite Fluorogenic Sensors for Monitoring Tyrosine Phosphatase Activity
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Identification of a variant form of tyrosine phosphatase LYP
Interaction of the disordered Gab1 with tyrosine phosphatase Shp2