Src family kinases interfere with dimerization of STAT5A through a phosphotyrosine-SH2 domain interaction

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Cell communication and signaling 13(1), Seiten/Artikel-Nr.:10

Classification: Biowissenschaften, Biologie

Event: Veröffentlichung

(where): Aachen

(who): Universitätsbibliothek der RWTH Aachen

(when): 2015

Creator: Fahrenkamp, Dirk
Schmitz-Van de Leur, Hildegard
Küster, Andrea
Chatain, Nicolas
Müller-Newen, Gerhard

DOI: 10.1186/s12964-014-0081-7

URN: urn:nbn:de:101:1-201804138870

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:55 AM CEST

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Associated

Fahrenkamp, Dirk
Schmitz-Van de Leur, Hildegard
Küster, Andrea
Chatain, Nicolas
Müller-Newen, Gerhard
Universitätsbibliothek der RWTH Aachen

Time of origin

2015

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Src family kinases interfere with dimerization of STAT5A through a phosphotyrosine-SH2 domain interaction

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Other Objects (12)

The Src family kinases: distinct functions of c-Src, Yes, and Fyn in the liver

Interaction of NO-sensitive guanylyl cyclase with Src-like kinases

Interaction of NO-sensitive guanylyl cyclase with Src-like kinases

Endocytosis and the Src family of non-receptor tyrosine kinases

Tyrosine Phosphorylation of Tau by the Src Family Kinases Lck and Fyn

Src kinases and Flt3 : phosphorylation, interference with receptor maturation and mechanism of association

Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases

FGF receptor kinase inhibitors exhibit broad antiviral activity by targeting Src family kinases

Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases

Single molecule fluorescence reveals dimerization of myristoylated Src N‐terminal region on supported lipid bilayers

Structural investigations of the Id helix-loop-helix dimerization domain

Phosphorylation-dependent pseudokinase domain dimerization drives full-length MLKL oligomerization

The Src family kinases: distinct functions of c-Src, Yes, and Fyn in the liver

Interaction of NO-sensitive guanylyl cyclase with Src-like kinases

Interaction of NO-sensitive guanylyl cyclase with Src-like kinases

Endocytosis and the Src family of non-receptor tyrosine kinases

Tyrosine Phosphorylation of Tau by the Src Family Kinases Lck and Fyn

Src kinases and Flt3 : phosphorylation, interference with receptor maturation and mechanism of association

Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases

FGF receptor kinase inhibitors exhibit broad antiviral activity by targeting Src family kinases

Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases

Single molecule fluorescence reveals dimerization of myristoylated Src N‐terminal region on supported lipid bilayers

Structural investigations of the Id helix-loop-helix dimerization domain

Phosphorylation-dependent pseudokinase domain dimerization drives full-length MLKL oligomerization

The Src family kinases: distinct functions of c-Src, Yes, and Fyn in the liver

Interaction of NO-sensitive guanylyl cyclase with Src-like kinases

Interaction of NO-sensitive guanylyl cyclase with Src-like kinases

Endocytosis and the Src family of non-receptor tyrosine kinases

Tyrosine Phosphorylation of Tau by the Src Family Kinases Lck and Fyn

Src kinases and Flt3 : phosphorylation, interference with receptor maturation and mechanism of association

Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases

FGF receptor kinase inhibitors exhibit broad antiviral activity by targeting Src family kinases

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Single molecule fluorescence reveals dimerization of myristoylated Src N‐terminal region on supported lipid bilayers

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