Discover open access scientific publications

Search, annotate, share and cite publications

Publications by K. Baltensperger

Phosphorylation of Tyrosyl Residues 350/354 of the -Adrenergic Receptor Is Obligatory for Counterregulatory Effects of Insulin

Journal of Biological Chemistry

English

Related publications

Prolactin Activates Tyrosyl Phosphorylation of Insulin Receptor Substrate 1 and Phosphatidylinositol-3-Oh Kinase

Journal of Biological Chemistry

English

Antitumor Effects of Β-Elemene via Targeting the Phosphorylation of Insulin Receptor

Endocrine-Related Cancer

English

Serine Residues 1177/78/82 of the Insulin Receptor Are Required for Substrate Phosphorylation but Not Autophosphorylation

English

Tyrosine Phosphorylation of Phosphoinositide-Dependent Kinase 1 by the Insulin Receptor Is Necessary for Insulin Metabolic Signaling

Molecular and Cellular Biology

Cell Biology

Molecular Biology

2005

English

Insulin Stimulates Sequestration of Β-Adrenergic Receptors and Enhanced Association of Β-Adrenergic Receptors With Grb2 via Tyrosine 350

Journal of Biological Chemistry

English

Trp64Arg Mutation of ?-Adrenergic Receptor in Essential Hypertension Insulin Resistance and the Adrenergic System

American Journal of Hypertension

Internal Medicine

1997

English

Role of Group-Conserved Residues in the Helical Core of Beta2-Adrenergic Receptor

Proceedings of the National Academy of Sciences of the United States of America

Multidisciplinary

2007

English

Insulin-Like Growth Factor Receptor-1 Stimulates Phosphorylation of the Β2-Adrenergic Receptorin Vivoon Sites Distinct From Those Phosphorylated in Response to Insulin

Journal of Biological Chemistry

English

Insulin Receptor-Mediated P62dokTyrosine Phosphorylation at Residues 362 and 398 Plays Distinct Roles for Binding GTPase-activating Protein and NCK and Is Essential for Inhibiting Insulin-Stimulated Activation of Ras and Akt

Journal of Biological Chemistry

English

Amanote Research

Discover open access scientific publications

Search, annotate, share and cite publications

Publications by K. Baltensperger

Phosphorylation of Tyrosyl Residues 350/354 of the -Adrenergic Receptor Is Obligatory for Counterregulatory Effects of Insulin

Related publications

Prolactin Activates Tyrosyl Phosphorylation of Insulin Receptor Substrate 1 and Phosphatidylinositol-3-Oh Kinase

Antitumor Effects of Β-Elemene via Targeting the Phosphorylation of Insulin Receptor

Serine Residues 1177/78/82 of the Insulin Receptor Are Required for Substrate Phosphorylation but Not Autophosphorylation

Tyrosine Phosphorylation of Phosphoinositide-Dependent Kinase 1 by the Insulin Receptor Is Necessary for Insulin Metabolic Signaling

Insulin Stimulates Sequestration of Β-Adrenergic Receptors and Enhanced Association of Β-Adrenergic Receptors With Grb2 via Tyrosine 350

Trp64Arg Mutation of ?-Adrenergic Receptor in Essential Hypertension Insulin Resistance and the Adrenergic System

Role of Group-Conserved Residues in the Helical Core of Beta2-Adrenergic Receptor

Insulin-Like Growth Factor Receptor-1 Stimulates Phosphorylation of the Β2-Adrenergic Receptorin Vivoon Sites Distinct From Those Phosphorylated in Response to Insulin

Insulin Receptor-Mediated P62dokTyrosine Phosphorylation at Residues 362 and 398 Plays Distinct Roles for Binding GTPase-activating Protein and NCK and Is Essential for Inhibiting Insulin-Stimulated Activation of Ras and Akt