Melissa Hector-Greene
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View article: Data from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma
Data from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma Open
Extracellular signal-regulated kinase (ERK)/mitogen-activated protein kinase pathway activity is regulated by the antagonist function of activating kinases and inactivating protein phosphatases. Sustained ERK pathway activity is commonly o…
View article: Data from Identification of PP2A Complexes and Pathways Involved in Cell Transformation
Data from Identification of PP2A Complexes and Pathways Involved in Cell Transformation Open
The simian virus 40 small t (SV40ST) oncoprotein interacts with protein phosphatase 2A (PP2A), an abundantly expressed family of serine–threonine phosphatases. This interaction is essential for the transformation of human cells by SV40, an…
View article: Data from Identification of PP2A Complexes and Pathways Involved in Cell Transformation
Data from Identification of PP2A Complexes and Pathways Involved in Cell Transformation Open
The simian virus 40 small t (SV40ST) oncoprotein interacts with protein phosphatase 2A (PP2A), an abundantly expressed family of serine–threonine phosphatases. This interaction is essential for the transformation of human cells by SV40, an…
View article: Supplementary Figures 1-8 from Identification of PP2A Complexes and Pathways Involved in Cell Transformation
Supplementary Figures 1-8 from Identification of PP2A Complexes and Pathways Involved in Cell Transformation Open
Supplementary Figures 1-8 from Identification of PP2A Complexes and Pathways Involved in Cell Transformation
View article: Supplementary Tables 1-3, Figures 1-6 from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma
Supplementary Tables 1-3, Figures 1-6 from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma Open
Supplementary Tables 1-3, Figures 1-6 from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma
View article: Supplementary Tables 1-3, Figures 1-6 from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma
Supplementary Tables 1-3, Figures 1-6 from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma Open
Supplementary Tables 1-3, Figures 1-6 from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma
View article: Data from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma
Data from PME-1 Protects Extracellular Signal-Regulated Kinase Pathway Activity from Protein Phosphatase 2A–Mediated Inactivation in Human Malignant Glioma Open
Extracellular signal-regulated kinase (ERK)/mitogen-activated protein kinase pathway activity is regulated by the antagonist function of activating kinases and inactivating protein phosphatases. Sustained ERK pathway activity is commonly o…
View article: Supplementary Figures 1-8 from Identification of PP2A Complexes and Pathways Involved in Cell Transformation
Supplementary Figures 1-8 from Identification of PP2A Complexes and Pathways Involved in Cell Transformation Open
Supplementary Figures 1-8 from Identification of PP2A Complexes and Pathways Involved in Cell Transformation
View article: ALK1 regulates the internalization of endoglin and the type III TGF-β receptor
ALK1 regulates the internalization of endoglin and the type III TGF-β receptor Open
The relation between complex formation among TGF-β receptors and their endocytosis remained unclear. We show that the complexes formed regulate their endocytosis and signaling, with a major effect by ALK1. Our results link TGF-β receptor o…
View article: TβRIII independently binds type I and type II TGF-β receptors to inhibit TGF-β signaling
TβRIII independently binds type I and type II TGF-β receptors to inhibit TGF-β signaling Open
Transforming growth factor-β (TGF-β) receptor oligomerization has important roles in signaling. Complex formation among type I and type II (TβRI and TβRII) TGF-β receptors is well characterized and is essential for signal transduction. How…
View article: Regulation of TGF-β receptor hetero-oligomerization and signaling by endoglin
Regulation of TGF-β receptor hetero-oligomerization and signaling by endoglin Open
Complex formation among transforming growth factor-β (TGF-β) receptors and its modulation by coreceptors represent an important level of regulation for TGF-β signaling. Oligomerization of ALK5 and the type II TGF-β receptor (TβRII) has bee…