(PDF) Insufficient Deactivation of the Protein Tyrosine

Insufficient Deactivation of the Protein Tyrosine Kinase LCK Amplifies T-Cell Responsiveness in Acute Coronary Syndrome

Circulation Research - United States

doi 10.1161/circresaha.109.206052

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March 5, 2010

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Ovid Technologies (Wolters Kluwer Health)

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Amanote Research

Insufficient Deactivation of the Protein Tyrosine Kinase LCK Amplifies T-Cell Responsiveness in Acute Coronary Syndrome

Circulation Research - United States

doi 10.1161/circresaha.109.206052

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Interaction of SAP-1, a Transmembrane-Type Protein-Tyrosine Phosphatase, With the Tyrosine Kinase LCK

LCK-Dependent Tyrosine Phosphorylation of Diacylglycerol Kinase Α Regulates Its Membrane Association in T Cells

Rapid T-Cell Receptor-Mediated Tyrosine Phosphorylation of P120, an Fyn/LCK SRC Homology 3 Domain-Binding Protein.

LCK Regulates the Tyrosine Phosphorylation of the T Cell Receptor Subunits and ZAP-70 in Murine Thymocytes

Identification of Rlk, a Novel Protein Tyrosine Kinase With Predominant Expression in the T Cell Lineage

Overexpression of Syk Tyrosine Kinase in Peripheral T-Cell Lymphomas

Interaction Between Sam68 and SRC Family Tyrosine Kinases, Fyn and Lck, in T Cell Receptor Signaling

T Cell Specific Adaptor Protein (TSAd) Promotes Interaction of NCK With LCK and SLP-76 in T Cells

Differential Effects of Expression of the CD45 Tyrosine Protein Phosphatase on the Tyrosine Phosphorylation of the Lck, Fyn, and C-SRC Tyrosine Protein Kinases.