PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26429914-3 2015 In tumor cells, which frequently are characterized by constitutively high GSTP1 expression, GSTP1 undergoes phosphorylation by epidermal growth factor receptor (EGFR) at tyrosine residues 3, 7, and 198. Tyrosine 170-178 glutathione S-transferase pi 1 Homo sapiens 74-79 27113843-0 2016 A tyrosine-reactive irreversible inhibitor for glutathione S-transferase Pi (GSTP1). Tyrosine 2-10 glutathione S-transferase pi 1 Homo sapiens 77-82 26429914-3 2015 In tumor cells, which frequently are characterized by constitutively high GSTP1 expression, GSTP1 undergoes phosphorylation by epidermal growth factor receptor (EGFR) at tyrosine residues 3, 7, and 198. Tyrosine 170-178 glutathione S-transferase pi 1 Homo sapiens 92-97 26429914-4 2015 Here we report on the effect of this EGFR-dependent GSTP1 tyrosine phosphorylation on the interaction of GSTP1 with JNK, on the regulation of JNK downstream signaling by GSTP1, and on tumor cell survival. Tyrosine 58-66 glutathione S-transferase pi 1 Homo sapiens 52-57 26429914-4 2015 Here we report on the effect of this EGFR-dependent GSTP1 tyrosine phosphorylation on the interaction of GSTP1 with JNK, on the regulation of JNK downstream signaling by GSTP1, and on tumor cell survival. Tyrosine 58-66 glutathione S-transferase pi 1 Homo sapiens 105-110 26429914-4 2015 Here we report on the effect of this EGFR-dependent GSTP1 tyrosine phosphorylation on the interaction of GSTP1 with JNK, on the regulation of JNK downstream signaling by GSTP1, and on tumor cell survival. Tyrosine 58-66 glutathione S-transferase pi 1 Homo sapiens 105-110 26429914-5 2015 Using in vitro and in vivo growing human brain tumors, we show that tyrosine phosphorylation shifts the GSTP1 dimer-monomer equilibrium to the monomeric state and facilitates the formation of the GSTP1-JNK complex, in which JNK is functionally inhibited. Tyrosine 68-76 glutathione S-transferase pi 1 Homo sapiens 104-109 26429914-5 2015 Using in vitro and in vivo growing human brain tumors, we show that tyrosine phosphorylation shifts the GSTP1 dimer-monomer equilibrium to the monomeric state and facilitates the formation of the GSTP1-JNK complex, in which JNK is functionally inhibited. Tyrosine 68-76 glutathione S-transferase pi 1 Homo sapiens 196-201 26429914-6 2015 Targeted mutagenesis and functional analysis demonstrated that the increased GSTP1 binding to JNK results from phosphorylation of the GSTP1 C-terminal Tyr-198 by EGFR and is associated with a >2.5-fold decrease in JNK downstream signaling and a significant suppression of both spontaneous and drug-induced apoptosis in the tumor cells. Tyrosine 151-154 glutathione S-transferase pi 1 Homo sapiens 77-82 26429914-6 2015 Targeted mutagenesis and functional analysis demonstrated that the increased GSTP1 binding to JNK results from phosphorylation of the GSTP1 C-terminal Tyr-198 by EGFR and is associated with a >2.5-fold decrease in JNK downstream signaling and a significant suppression of both spontaneous and drug-induced apoptosis in the tumor cells. Tyrosine 151-154 glutathione S-transferase pi 1 Homo sapiens 134-139 14676193-4 2004 The key residue, which is either Phe or Tyr (Tyr(50) in human GSTP1-1) in one subunit, is wedged into a hydrophobic pocket of the other subunit. Tyrosine 40-43 glutathione S-transferase pi 1 Homo sapiens 62-69 19254954-6 2009 In human glioma and breast cancer cells, epidermal growth factor stimulation rapidly increased GSTP1 tyrosine phosphorylation and decreased cisplatin sensitivity. Tyrosine 101-109 glutathione S-transferase pi 1 Homo sapiens 95-100 23426146-9 2013 The transient expression of GSTP1 specifically downregulated epidermal growth factor (EGF)-mediated tyrosine phosphorylation of Stat3, and subsequently suppressed the transcriptional activity of Stat3. Tyrosine 100-108 glutathione S-transferase pi 1 Homo sapiens 28-33 21439344-11 2011 Stimulation with particulates phosphorylated and dephosphorylated several proteins in epithelial cells, and serine and tyrosine protein phosphorylation of GSTP1 decreased. Tyrosine 119-127 glutathione S-transferase pi 1 Homo sapiens 155-160 19254954-0 2009 Tyrosine phosphorylation of the human glutathione S-transferase P1 by epidermal growth factor receptor. Tyrosine 0-8 glutathione S-transferase pi 1 Homo sapiens 38-66 19254954-3 2009 Here, we provide evidence that GSTP1 is a downstream EGFR target and that EGFR binds to and phosphorylates tyrosine residues in the GSTP1 protein in vitro and in vivo. Tyrosine 107-115 glutathione S-transferase pi 1 Homo sapiens 132-137 19254954-4 2009 Mass spectrometry and mutagenesis analyses in a cell-free system and in gliomas cells identified Tyr-7 and Tyr-198 as major EGFR-specific phospho-acceptor residues in the GSTP1 protein. Tyrosine 97-100 glutathione S-transferase pi 1 Homo sapiens 171-176 19254954-4 2009 Mass spectrometry and mutagenesis analyses in a cell-free system and in gliomas cells identified Tyr-7 and Tyr-198 as major EGFR-specific phospho-acceptor residues in the GSTP1 protein. Tyrosine 107-110 glutathione S-transferase pi 1 Homo sapiens 171-176 14676193-4 2004 The key residue, which is either Phe or Tyr (Tyr(50) in human GSTP1-1) in one subunit, is wedged into a hydrophobic pocket of the other subunit. Tyrosine 45-48 glutathione S-transferase pi 1 Homo sapiens 62-69 14676193-9 2004 A network of hydrogen-bonded water molecules, found in crystal structures of GSTP1-1, connects the two active sites and the main chain carbonyl group of Tyr(50), thereby offering a mechanism for communication between the two active sites. Tyrosine 153-156 glutathione S-transferase pi 1 Homo sapiens 77-84 8343114-1 1993 Reaction of human GSH transferase P1-1 (GSTP1-1) with diethylpyrocarbonate (DEPC) at pH 7.0 and 4 degrees C resulted in covalent modification of an equivalent of one histidine and one tyrosine residue per subunit, with loss of activity. Tyrosine 184-192 glutathione S-transferase pi 1 Homo sapiens 40-47 10744731-7 2000 In P(i) class GSTs, Tyr(154) appears to be of particular structural importance, since it interacts with conserved residues Leu(21), Asp(24), and Gln(25) of the adjacent alpha1-helix which contributes to the active site. Tyrosine 20-23 glutathione S-transferase pi 1 Homo sapiens 14-18 8343114-6 1993 Kinetic analysis of the DEPC modification of Tyr-7 in GSTP1-1 gave a k2 approx. Tyrosine 45-48 glutathione S-transferase pi 1 Homo sapiens 54-61 8343114-8 1993 The reaction of Tyr-7 of GSTP1-1 with DEPC was poorly inhibited by 1 mM GSH (14%) or 10 microM S-hexylglutathione (18%). Tyrosine 16-19 glutathione S-transferase pi 1 Homo sapiens 25-32 34641326-5 2021 A crystal structure of a dinitrosyl-dithiol-iron complex with glutathione-S-transferase P1 has been solved that demonstrates that a tyrosine residue in glutathione-S-transferase P1 is responsible for binding dinitrosyl-dithiol-iron-complexes. Tyrosine 132-140 glutathione S-transferase pi 1 Homo sapiens 62-90 34641326-5 2021 A crystal structure of a dinitrosyl-dithiol-iron complex with glutathione-S-transferase P1 has been solved that demonstrates that a tyrosine residue in glutathione-S-transferase P1 is responsible for binding dinitrosyl-dithiol-iron-complexes. Tyrosine 132-140 glutathione S-transferase pi 1 Homo sapiens 152-180