Identification of protein tyrosine phosphatase 1B and casein as substrates for 124-v-Mos
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1471-2091
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Identification of protein tyrosine phosphatase 1B and casein as substrates for 124-v-Mos ; volume:3 ; number:1 ; day:04 ; month:4 ; year:2002 ; pages:1-7 ; date:12.2002
BMC biochemistry ; 3, Heft 1 (04.4.2002), 1-7, 12.2002
- Creator
- Contributor
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Stabel, Silvia
Riethmacher, Dieter
SpringerLink (Online service)
- DOI
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10.1186/1471-2091-3-6
- URN
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urn:nbn:de:1111-201603026486
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:31 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Proikas-Cezanne, Tassula
- Stabel, Silvia
- Riethmacher, Dieter
- SpringerLink (Online service)
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Multipartite Fluorogenic Sensors for Monitoring Tyrosine Phosphatase Activity
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Identification of a variant form of tyrosine phosphatase LYP
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Regulation of autoimmune arthritis by the SHP-1 tyrosine phosphatase
Tyrosine phosphatase activity is restricted by basic charge substituting mutation of substrates
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
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
Phosphoprotein phosphatase substrates - selectivity from peptides to proteins
Identification of a variant form of tyrosine phosphatase LYP
Interaction of the disordered Gab1 with tyrosine phosphatase Shp2