PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31222087-6 2019 DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death. Histidine 161-170 eukaryotic translation elongation factor 2 Homo sapiens 52-94 6267047-2 1981 Diphtheria toxin inactivates protein synthesis elongation factor 2 by catalyzing the ADP-ribosylation of a novel derivative of histidine, diphthamide, in the protein (Van Ness, B. G., Howard, J. Histidine 127-136 eukaryotic translation elongation factor 2 Homo sapiens 47-66 33057331-1 2020 Diphthamide is a unique post-translationally modified histidine residue (His715 in all mammals) found only in eukaryotic elongation factor-2 (eEF-2). Histidine 54-63 eukaryotic translation elongation factor 2 Homo sapiens 110-140 33057331-1 2020 Diphthamide is a unique post-translationally modified histidine residue (His715 in all mammals) found only in eukaryotic elongation factor-2 (eEF-2). Histidine 54-63 eukaryotic translation elongation factor 2 Homo sapiens 142-147 2840927-3 1988 The 15 amino-acid-residue sequence comprising the histidine-715, supposed to be of importance for the biological function of EF-2, is preserved in human EF-2. Histidine 50-59 eukaryotic translation elongation factor 2 Homo sapiens 125-129 2840927-3 1988 The 15 amino-acid-residue sequence comprising the histidine-715, supposed to be of importance for the biological function of EF-2, is preserved in human EF-2. Histidine 50-59 eukaryotic translation elongation factor 2 Homo sapiens 153-157 31463593-1 2019 Diphthamide, the target of diphtheria toxin, is a post-translationally modified histidine residue found in archaeal and eukaryotic translation elongation factor 2 (EF2). Histidine 80-89 eukaryotic translation elongation factor 2 Homo sapiens 120-162 31463593-1 2019 Diphthamide, the target of diphtheria toxin, is a post-translationally modified histidine residue found in archaeal and eukaryotic translation elongation factor 2 (EF2). Histidine 80-89 eukaryotic translation elongation factor 2 Homo sapiens 164-167 31222087-6 2019 DTA exerts its toxic activity through inhibition of eukaryotic translation elongation factor 2 (eEF2) via adenosine diphosphate (ADP)-ribosylation of a modified histidine residue, diphthamide, at His715, which blocks protein translation and leads to cell death. Histidine 161-170 eukaryotic translation elongation factor 2 Homo sapiens 96-100 29590073-3 2018 In the presence of the substrate protein, elongation factor 2, this intermediate converts to an organic radical, formed by addition of the ACP radical to a histidine side chain. Histidine 156-165 eukaryotic translation elongation factor 2 Homo sapiens 42-61 29362492-2 2018 Diphthamide is the posttranslationally modified histidine residue on EEF2 that promotes protein chain elongation in the ribosome. Histidine 48-57 eukaryotic translation elongation factor 2 Homo sapiens 69-73 24422557-3 2014 The first step is the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-l-methionine (SAM) to the histidine residue of EF2, forming a C-C bond. Histidine 110-119 eukaryotic translation elongation factor 2 Homo sapiens 131-134 30097101-5 2018 Radical SAM enzymes in diphthamide biosynthesis cleave a different CS bond in SAM to generate a 3-amino-3-carboxypropyl radical and modify a histidine residue of substrate protein EF2. Histidine 141-150 eukaryotic translation elongation factor 2 Homo sapiens 180-183 27159451-8 2016 The structure explains how diphthamide, a eukaryotic and archaeal specific post-translational modification of a histidine residue of eEF2, is involved in translocation. Histidine 112-121 eukaryotic translation elongation factor 2 Homo sapiens 133-137 24140707-2 2014 A single histidine residue in eEF2 (H715) is modified to form diphthamide. Histidine 9-18 eukaryotic translation elongation factor 2 Homo sapiens 30-34 18460012-1 2008 Diphthamide is a post-translational derivative of histidine in protein synthesis elongation factor-2 (eEF-2) that is present in all eukaryotes with no known normal physiological role. Histidine 50-59 eukaryotic translation elongation factor 2 Homo sapiens 81-100 23971743-1 2013 Eukaryotic and archaeal elongation factor 2 contains a unique post-translationally modified histidine residue, named diphthamide. Histidine 92-101 eukaryotic translation elongation factor 2 Homo sapiens 24-43 16901746-4 2006 Using site-specific mutagenesis of the histidine precursor of diphthamide, the histidine residue of codon 715 in human EF-2 cDNA was substituted with one of four amino acid residue codons: leucine, methionine, asparagine or glutamine. Histidine 39-48 eukaryotic translation elongation factor 2 Homo sapiens 119-123 16901746-0 2006 Site-specific mutagenesis of the histidine precursor of diphthamide in the human elongation factor-2 gene confers resistance to diphtheria toxin. Histidine 33-42 eukaryotic translation elongation factor 2 Homo sapiens 81-100 16901746-1 2006 Protein synthesis elongation factor 2 (EF-2) from eukaryotes contains a conserved post-translationally modified histidine residue known as diphthamide. Histidine 112-121 eukaryotic translation elongation factor 2 Homo sapiens 18-37 16901746-1 2006 Protein synthesis elongation factor 2 (EF-2) from eukaryotes contains a conserved post-translationally modified histidine residue known as diphthamide. Histidine 112-121 eukaryotic translation elongation factor 2 Homo sapiens 39-43 16901746-4 2006 Using site-specific mutagenesis of the histidine precursor of diphthamide, the histidine residue of codon 715 in human EF-2 cDNA was substituted with one of four amino acid residue codons: leucine, methionine, asparagine or glutamine. Histidine 79-88 eukaryotic translation elongation factor 2 Homo sapiens 119-123 1353910-1 1992 The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide. Histidine 4-13 eukaryotic translation elongation factor 2 Homo sapiens 41-60 1353910-1 1992 The histidine residue at position 715 of elongation factor 2 (EF-2) is posttranslationally modified in a series of enzymatic reactions to 2-[3-carboxyamido-3-(trimethylammonio)-propyl]histidine, which has been given the trivial name diphthamide. Histidine 4-13 eukaryotic translation elongation factor 2 Homo sapiens 62-66 1353910-3 1992 EF-2 that has not been posttranslationally modified at histidine 715 is resistant to ADP ribosylation by these toxins. Histidine 55-64 eukaryotic translation elongation factor 2 Homo sapiens 0-4 1353910-4 1992 In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2. Histidine 206-215 eukaryotic translation elongation factor 2 Homo sapiens 90-94 1353910-4 1992 In this report we show that a G-to-A transition in the first position of codon 717 of the EF-2 gene results in substitution of arginine for glycine and prevents addition of the side chain of diphthamide to histidine 715 of EF-2. Histidine 206-215 eukaryotic translation elongation factor 2 Homo sapiens 223-227 1730643-9 1992 In addition, yeast and mammalian EF-2 share identical sequences at two critical functional sites: (i) the domain containing the histidine residue that is modified to diphthamide and (ii) the threonine residue that is specifically phosphorylated in vivo in mammalian cells by calmodulin-dependent protein kinase III, also known as EF-2 kinase. Histidine 128-137 eukaryotic translation elongation factor 2 Homo sapiens 33-37