A novel approach of recombinant laterosporulin production using the N-SH2 domain of SHP-2
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1472-6750
- 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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A novel approach of recombinant laterosporulin production using the N-SH2 domain of SHP-2 ; volume:21 ; number:1 ; day:21 ; month:10 ; year:2021 ; pages:1-11 ; date:12.2021
BMC biotechnology ; 21, Heft 1 (21.10.2021), 1-11, 12.2021
- Creator
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Salehzadeh, Simin
Tabatabaei, Mohammad
Derakhshandeh, Abdollah
Karbalaei-Heidari, Hamidreza
Kazemipour, Nasrin
- Contributor
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SpringerLink (Online service)
- DOI
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10.1186/s12896-021-00721-7
- URN
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urn:nbn:de:101:1-2022011418530587098429
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:27 AM CEST
Data provider
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Salehzadeh, Simin
- Tabatabaei, Mohammad
- Derakhshandeh, Abdollah
- Karbalaei-Heidari, Hamidreza
- Kazemipour, Nasrin
- SpringerLink (Online service)
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Regulation der Enzymaktivität der Proteintyrosinphosphatase SHP-1 durch monophosphorylierte SH2-Domänen-Liganden
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Author Correction: Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
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Development of highly potent small-molecule inhibitors of the STAT5b SH2 domain
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Regulation der Enzymaktivität der Proteintyrosinphosphatase SHP-1 durch monophosphorylierte SH2-Domänen-Liganden
Regulation der Enzymaktivität der Proteintyrosinphosphatase SHP-1 durch monophosphorylierte SH2-Domänen-Liganden
Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft
Allosterische Inhibierung und Aktivierung der Proteintyrosinphosphatase SHP-1 durch Mono- und bivalente SH2-Phosphopeptidliganden
Allosterische Inhibierung und Aktivierung der Proteintyrosinphosphatase SHP-1 durch mono- und bivalente SH2-Phosphopeptidliganden
Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
Author Correction: Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
Synthese und biologische Wirksamkeit abbau-stabilisierter Liganden der SH2-Domäne der Protein-Tyrosin-Phosphatase SHP-1
Development of highly potent small-molecule inhibitors of the STAT5b SH2 domain
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Negative regulation of the SH2-homology-containing protein-tyrosine phosphatase-1 (Shp-1) P2 promoter by the HTLV-1 tax oncoprotein
Regulation der Enzymaktivität der Proteintyrosinphosphatase SHP-1 durch monophosphorylierte SH2-Domänen-Liganden
Regulation der Enzymaktivität der Proteintyrosinphosphatase SHP-1 durch monophosphorylierte SH2-Domänen-Liganden
Tyr66 acts as a conformational switch in the closed-to-open transition of the SHP-2 N-SH2-domain phosphotyrosine-peptide binding cleft
Allosterische Inhibierung und Aktivierung der Proteintyrosinphosphatase SHP-1 durch Mono- und bivalente SH2-Phosphopeptidliganden
Allosterische Inhibierung und Aktivierung der Proteintyrosinphosphatase SHP-1 durch mono- und bivalente SH2-Phosphopeptidliganden
Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
Author Correction: Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
Synthese und biologische Wirksamkeit abbau-stabilisierter Liganden der SH2-Domäne der Protein-Tyrosin-Phosphatase SHP-1
Development of highly potent small-molecule inhibitors of the STAT5b SH2 domain
SHP
SHP