Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." ?g. }

• _7 value "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." provenance.
• _7 value "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." provenance.
• _7 value "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." provenance.
• _7 value "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." provenance.
• _7 value "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." provenance.
• _7 value "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." provenance.
• _7 value "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." provenance.
• _7 value "Depsipeptide Depsipeptide was originally isolated from a strain of Chromobacterium violaceum. Initial studies with this bicyclic peptide demonstrated a selective decrease in c-myc expression. However, growth inhibition of the Ha-rastransformed NIH-3T3 clonal cell line Ras-1 was also observed in the absence of altered Ha-ras mRNA expression [67]. Depsipeptide appears to regulate the cell cycle at several points, including cell cycle arrest at G0/G1 and inhibition of signal transduction through mitogen-activated protein kinase (MAPK) with resultant p53-independent G1 arrest. EPIDERMAL GROWTH FACTOR RECEPTOR TYROSINE KINASE INHIBITORS Epidermal Growth Factor Receptor Binding by any member of the EGF family of ligands results in receptor dimerization and activation of the intracytoplasmic tyrosine kinase domain. In addition to homodimers, members of this receptor family can also form heterodimers through a series of complex interactions that result in transphosphorylation and the concerted regulation of the involved receptors. Six EGF-like ligands are known to bind and activate EGFR: EGF, TGF?, amphiregulin (cripto-1; CR-1), heparin-binding EGF (HB-EGF), betacellulin (BTC), and epiregulin (EPR) [78, 79]. Ligand binding to EGFR at the cell membrane triggers a signal transduction cascade that leads to the activation of nuclear transcription factors that promote cell division." provenance.