PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22128160-5 2012 Furthermore, pharmacological and mutagenesis assays revealed that protein kinase C (PKC) and high K(+) depolarization increase RET surface levels through phosphorylation of the Thr(675) residue in the Box1 motif. Threonine 177-180 ret proto-oncogene Homo sapiens 127-130 3001107-4 1985 In an attempt to find a protein that might link the receptor tyrosine kinase to these serine/threonine phosphorylation reactions, we have studied the interaction of a partially purified preparation of insulin receptor with purified preparations of serine/threonine kinases known to phosphorylate glycogen synthase. Threonine 93-102 ret proto-oncogene Homo sapiens 52-76 24501868-6 2013 RESULTS: After HT along with the increase of Hb from 89, 7+/-10,0 to 119+/-13,3, there was significant decrease in Ret % from 2,4+/-1,1 to 1,4+/-0,5 7-10 day after HT There was also a reduction of Thr from 391,5+/-131,5 to 250, 7+/-57,2 and blood lactate in mmol/l from 2,5+/-1,1 to 1,5+/-0,7. Threonine 197-200 ret proto-oncogene Homo sapiens 115-118 22128160-6 2012 Finally, we found that the phosphorylation status of the Thr(675) residue influences RET mediated response to GDNF stimulation. Threonine 57-60 ret proto-oncogene Homo sapiens 85-88 16254257-0 2005 p-p70S6K (Thr 389) Expression in nodular sclerosing hodgkin"s disease as evidence for receptor tyrosine kinase signaling. Threonine 10-13 ret proto-oncogene Homo sapiens 86-110 17102091-8 2006 MEN 2A is primarily associated with substitutions at five extracellular cysteine residues, while 95% of MEN 2B is associated with a single methionine to threonine mutation in the kinase domain (M918T). Threonine 153-162 ret proto-oncogene Homo sapiens 104-110 17108110-2 2006 The disease is caused primarily by a methionine to threonine substitution of residue 918 in the kinase domain of the RET receptor (2B-RET); however, the molecular mechanisms that lead to the disease phenotype are unclear. Threonine 51-60 ret proto-oncogene Homo sapiens 117-120 17108110-2 2006 The disease is caused primarily by a methionine to threonine substitution of residue 918 in the kinase domain of the RET receptor (2B-RET); however, the molecular mechanisms that lead to the disease phenotype are unclear. Threonine 51-60 ret proto-oncogene Homo sapiens 134-137 16829704-13 2006 RET gene analysis showed a codon 918 mutation in exon 16 resulting in an ATG (methionine) to ACG (threonine) substitution, but analysis of the patient"s parents showed the wild type. Threonine 98-107 ret proto-oncogene Homo sapiens 0-3 16427628-2 2006 We showed that all RET-PTC-1 mutants in which the C in this motif (C376) was replaced with glycine, lysine, threonine or serine lost their activity in vitro. Threonine 108-117 ret proto-oncogene Homo sapiens 19-22 15531548-2 2004 We describe here a novel germline homozygous mutation in exon 15 of the RET gene that determines an amino acid substitution (Ala->Thr) at codon 883. Threonine 133-136 ret proto-oncogene Homo sapiens 72-75 15485908-1 2004 The receptor tyrosine kinases (RTKs) RET, MET, and RON all carry the Met(p+1loop)-->Thr point mutation (i.e., 2B mutation), leading to the formation of tumors with high metastatic potential. Threonine 87-90 ret proto-oncogene Homo sapiens 37-40 15379552-2 2004 In addition to RTK-specific tyrosine phosphorylation, these docking proteins also can be phosphorylated on serine/threonine residues affecting signal transduction. Threonine 114-123 ret proto-oncogene Homo sapiens 15-18 12757658-3 2003 RESULTS: We found the same mutation Met(ATG)-->Thr(ACG) at codon 918 in exon 16 of RET proto-oncogene in both the tumor (c)DNA and leukocyte DNA of the MEN-2B patient in the form of homozygous missense mutation, but there was no corresponding mutation in leukocytes DNA of his parents. Threonine 50-53 ret proto-oncogene Homo sapiens 86-89 12757658-3 2003 RESULTS: We found the same mutation Met(ATG)-->Thr(ACG) at codon 918 in exon 16 of RET proto-oncogene in both the tumor (c)DNA and leukocyte DNA of the MEN-2B patient in the form of homozygous missense mutation, but there was no corresponding mutation in leukocytes DNA of his parents. Threonine 50-53 ret proto-oncogene Homo sapiens 155-161 9393871-2 1997 Germline mutation of a methionine to a threonine within the RET TK domain predisposes to the Multiple Endocrine Neoplasia type 2B (MEN 2B). Threonine 39-48 ret proto-oncogene Homo sapiens 60-63 10871866-2 2000 MEN 2B is associated with a germline point mutation in the RET proto-oncogene, leading to a Met-->Thr substitution at codon 918 in the kinase domain, which alters the substrate specificity of the protein. Threonine 101-104 ret proto-oncogene Homo sapiens 0-6 10871866-2 2000 MEN 2B is associated with a germline point mutation in the RET proto-oncogene, leading to a Met-->Thr substitution at codon 918 in the kinase domain, which alters the substrate specificity of the protein. Threonine 101-104 ret proto-oncogene Homo sapiens 59-62 10871866-3 2000 We used the human calcitonin gene (CALC-I) promoter to generate transgenic mice expressing either the human RET oncogene with the MEN2B-specific 918 Met-->Thr mutation (CALC-MEN2B-RET) or the human non-mutated RET proto-oncogene (CALC-WT-RET) in the C-cells. Threonine 158-161 ret proto-oncogene Homo sapiens 130-135 11839664-7 2002 More than 95% of MEN2B patients also had a predominant mutation type at codon 918 (Met-->Thr). Threonine 92-95 ret proto-oncogene Homo sapiens 17-22 11351254-3 2001 In sporadic MTCs the RET gene is mutated in codon 918, where a methionine is substituted to a threonine (M918T). Threonine 94-103 ret proto-oncogene Homo sapiens 21-24 9621513-5 1998 A mutation at codon 918, causing the substitution of threonine for methionine in the tyrosine kinase domain of the protein, was found in germline DNAs of all four patients with MEN2B and in two of the 22 patients with sporadic MTCs; codon 918 was mutated somatically in tumor DNAs from three other sporadic cases. Threonine 53-62 ret proto-oncogene Homo sapiens 177-182 9706252-8 1998 A unique mutation of codon 918 in exon 16, ATG --> ACG (methionine to threonine), was found in both MEN 2B affected patients. Threonine 73-82 ret proto-oncogene Homo sapiens 103-109 9398735-3 1997 In MEN 2B patients, a specific mutation at codon 918, substituting a threonine for a methionine, has been found in 95% of cases. Threonine 69-78 ret proto-oncogene Homo sapiens 3-9 9393871-2 1997 Germline mutation of a methionine to a threonine within the RET TK domain predisposes to the Multiple Endocrine Neoplasia type 2B (MEN 2B). Threonine 39-48 ret proto-oncogene Homo sapiens 93-129 9393871-2 1997 Germline mutation of a methionine to a threonine within the RET TK domain predisposes to the Multiple Endocrine Neoplasia type 2B (MEN 2B). Threonine 39-48 ret proto-oncogene Homo sapiens 131-137 9018112-4 1997 In this study, we have introduced a MEN 2A mutation (Cys634-->Arg) and the unique MEN 2B mutation (Met918-->Thr) in two RET isoforms of 1114 and 1072 amino acids which differ in the carboxy-terminus part. Threonine 114-117 ret proto-oncogene Homo sapiens 85-91 9075701-7 1997 However, only when a threonine residue is present in position 918, does RET efficiently couple with a transforming pathway. Threonine 21-30 ret proto-oncogene Homo sapiens 72-75 9018112-4 1997 In this study, we have introduced a MEN 2A mutation (Cys634-->Arg) and the unique MEN 2B mutation (Met918-->Thr) in two RET isoforms of 1114 and 1072 amino acids which differ in the carboxy-terminus part. Threonine 114-117 ret proto-oncogene Homo sapiens 126-129 8880581-4 1996 The mutational spectrum of MEN 2B is remarkably narrow, with over 95% of cases being caused by a single methionine to threonine substitution in the intracellular tyrosine kinase domain. Threonine 118-127 ret proto-oncogene Homo sapiens 27-33 8557249-8 1996 All MEN 2B probands carried a Met to Thr mutation in exon 16. Threonine 37-40 ret proto-oncogene Homo sapiens 4-10 8884827-5 1996 A codon 918 germ line mutation, which converts a highly conserved methionine to a threonine in the intracellular tyrosine kinase portion of this receptor of RET, has been identified in 95% of patients with MEN 2B. Threonine 82-91 ret proto-oncogene Homo sapiens 157-160 8884827-5 1996 A codon 918 germ line mutation, which converts a highly conserved methionine to a threonine in the intracellular tyrosine kinase portion of this receptor of RET, has been identified in 95% of patients with MEN 2B. Threonine 82-91 ret proto-oncogene Homo sapiens 206-212 8621456-2 1996 Multiple endocrine neoplasia type 2B (MEN 2B) is caused by the mutation of a conserved methionine to a threonine in the catalytic domain of the RET kinase. Threonine 103-112 ret proto-oncogene Homo sapiens 0-36 8621456-2 1996 Multiple endocrine neoplasia type 2B (MEN 2B) is caused by the mutation of a conserved methionine to a threonine in the catalytic domain of the RET kinase. Threonine 103-112 ret proto-oncogene Homo sapiens 38-44 8621456-2 1996 Multiple endocrine neoplasia type 2B (MEN 2B) is caused by the mutation of a conserved methionine to a threonine in the catalytic domain of the RET kinase. Threonine 103-112 ret proto-oncogene Homo sapiens 144-147 9074721-7 1996 A single point mutation leading to the replacement of a methionine by a threonine within the tyrosine kinase domain has been detected in almost all cases of MEN 2B. Threonine 72-81 ret proto-oncogene Homo sapiens 157-163 12114809-6 1995 A germline Met -* Thr point mutation at codon 918 of the RETtyrosine kinase domain encoded by exon 16 was identified in all MEN 2B patients. Threonine 18-21 ret proto-oncogene Homo sapiens 124-130 7495285-6 1995 Six MEN-2A-associated hyperplastic glands exhibited identical band shifts in the polymerase chain reaction single-strand conformation polymorphism analysis of exon 11, which corresponded to a Cys 634-->Arg substitution in the nucleotide sequence analysis (TGC-->CGC), whereas in the MEN 2B parathyroid specimen a point mutation was found at codon 918 of exon 16 (ATG-->ACG), causing a Met 918-->Thr substitution. Threonine 407-410 ret proto-oncogene Homo sapiens 4-10 7705835-4 1995 In MEN 2B patients, a single point mutation at codon 918 has recently been characterized, leading to the replacement of a methionine by a threonine within the RET tyrosine kinase domain. Threonine 138-147 ret proto-oncogene Homo sapiens 3-9 7705835-4 1995 In MEN 2B patients, a single point mutation at codon 918 has recently been characterized, leading to the replacement of a methionine by a threonine within the RET tyrosine kinase domain. Threonine 138-147 ret proto-oncogene Homo sapiens 159-162 7595167-5 1995 In contrast, a single point mutation that results in the substitution of threonine for methionine within the catalytic core of the tyrosine kinase domain (codon 918, exon 16) is responsible for all 66 reported cases of MEN 2B. Threonine 73-82 ret proto-oncogene Homo sapiens 219-225 8625130-9 1995 A germline Met-->Thr point mutation at codon 918 of the RET tyrosine kinase domain was identified in all three patients with MEN 2B. Threonine 20-23 ret proto-oncogene Homo sapiens 59-62 8625130-9 1995 A germline Met-->Thr point mutation at codon 918 of the RET tyrosine kinase domain was identified in all three patients with MEN 2B. Threonine 20-23 ret proto-oncogene Homo sapiens 128-134 7627271-2 1995 All tumors of 4 MEN 2B patients were confirmed to contain a heterozygous missense mutation at codon 918 (ATG-->ACG; Met-->Thr) of the RET proto-oncogene as well as their leukocytes. Threonine 128-131 ret proto-oncogene Homo sapiens 16-22 7627271-2 1995 All tumors of 4 MEN 2B patients were confirmed to contain a heterozygous missense mutation at codon 918 (ATG-->ACG; Met-->Thr) of the RET proto-oncogene as well as their leukocytes. Threonine 128-131 ret proto-oncogene Homo sapiens 140-143 7911697-3 1994 We now report a missense mutation, resulting in the substitution of a threonine for a methionine at codon 918 in the tyrosine kinase catalytic domain, in the germline of 26 of 28 apparently distinct families with MEN 2B. Threonine 70-79 ret proto-oncogene Homo sapiens 213-219 7906866-8 1994 A mutation in codon 664, causing the substitution of a threonine for a methionine in the tyrosine kinase domain of the protein, was found in all nine unrelated MEN 2B patients studied. Threonine 55-64 ret proto-oncogene Homo sapiens 160-166