Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms
Constitutive Btk signaling drives several B-cell cancers. Here the authors demonstrate key allosteric intramolecular interactions between the SH2 domain and the kinase domain of Btk, and propose an alternative approach for inhibition of both wild-type and tyrosine kinase inhibitor-resistant Btk.
Autor*in: |
Daniel P. Duarte [verfasserIn] Allan J. Lamontanara [verfasserIn] Giuseppina La Sala [verfasserIn] Sukyo Jeong [verfasserIn] Yoo-Kyoung Sohn [verfasserIn] Alejandro Panjkovich [verfasserIn] Sandrine Georgeon [verfasserIn] Tim Kükenshöner [verfasserIn] Maria J. Marcaida [verfasserIn] Florence Pojer [verfasserIn] Marco De Vivo [verfasserIn] Dmitri Svergun [verfasserIn] Hak-Sung Kim [verfasserIn] Matteo Dal Peraro [verfasserIn] Oliver Hantschel [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2020 |
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Übergeordnetes Werk: |
In: Nature Communications - Nature Portfolio, 2016, 11(2020), 1, Seite 15 |
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Übergeordnetes Werk: |
volume:11 ; year:2020 ; number:1 ; pages:15 |
Links: |
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DOI / URN: |
10.1038/s41467-020-16128-5 |
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Katalog-ID: |
DOAJ066569354 |
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Daniel P. Duarte @@aut@@ Allan J. Lamontanara @@aut@@ Giuseppina La Sala @@aut@@ Sukyo Jeong @@aut@@ Yoo-Kyoung Sohn @@aut@@ Alejandro Panjkovich @@aut@@ Sandrine Georgeon @@aut@@ Tim Kükenshöner @@aut@@ Maria J. Marcaida @@aut@@ Florence Pojer @@aut@@ Marco De Vivo @@aut@@ Dmitri Svergun @@aut@@ Hak-Sung Kim @@aut@@ Matteo Dal Peraro @@aut@@ Oliver Hantschel @@aut@@ |
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Daniel P. Duarte misc Science misc Q Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
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Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
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Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
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Constitutive Btk signaling drives several B-cell cancers. Here the authors demonstrate key allosteric intramolecular interactions between the SH2 domain and the kinase domain of Btk, and propose an alternative approach for inhibition of both wild-type and tyrosine kinase inhibitor-resistant Btk. |
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Constitutive Btk signaling drives several B-cell cancers. Here the authors demonstrate key allosteric intramolecular interactions between the SH2 domain and the kinase domain of Btk, and propose an alternative approach for inhibition of both wild-type and tyrosine kinase inhibitor-resistant Btk. |
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Constitutive Btk signaling drives several B-cell cancers. Here the authors demonstrate key allosteric intramolecular interactions between the SH2 domain and the kinase domain of Btk, and propose an alternative approach for inhibition of both wild-type and tyrosine kinase inhibitor-resistant Btk. |
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Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms |
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