PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30797067-6 2019 The amino terminal proline residue (P2) and invariant lysine residue (K33) which are critical active sites of tautomerase activity in mammalian MIF were also detected. Proline 19-26 macrophage migration inhibitory factor Homo sapiens 144-147 29440696-5 2018 Identification of the most abundant TRITC-modified protein in lymph nodes by tandem mass spectrometry revealed TRITC-modification of the N-terminal proline of macrophage migration inhibitory factor (MIF) - an evolutionary well-conserved protein involved in cell-mediated immunity and inflammation. Proline 148-155 macrophage migration inhibitory factor Homo sapiens 159-197 29247897-4 2018 Several studies have shown that MIF is subject to post-translational modification, particularly redox-dependent modification of the catalytic proline and cysteine residues. Proline 142-149 macrophage migration inhibitory factor Homo sapiens 32-35 29440696-5 2018 Identification of the most abundant TRITC-modified protein in lymph nodes by tandem mass spectrometry revealed TRITC-modification of the N-terminal proline of macrophage migration inhibitory factor (MIF) - an evolutionary well-conserved protein involved in cell-mediated immunity and inflammation. Proline 148-155 macrophage migration inhibitory factor Homo sapiens 199-202 29440696-7 2018 Most haptens are electrophiles and can therefore modify the N-terminal proline of MIF, which has an unusually reactive amino group under physiological conditions; thus, modification of MIF by haptens may have an immunomodulating role in contact allergy as well as in other immunotoxicity reactions. Proline 71-78 macrophage migration inhibitory factor Homo sapiens 82-85 29440696-7 2018 Most haptens are electrophiles and can therefore modify the N-terminal proline of MIF, which has an unusually reactive amino group under physiological conditions; thus, modification of MIF by haptens may have an immunomodulating role in contact allergy as well as in other immunotoxicity reactions. Proline 71-78 macrophage migration inhibitory factor Homo sapiens 185-188 27159346-3 2016 The WRK-derived probes show unique reactivity towards the catalytic N-terminal proline in the macrophage migration inhibitory factor (MIF) and can be used to label and, if equipped with a fluorophore, to image MIF activities in living cells. Proline 79-86 macrophage migration inhibitory factor Homo sapiens 94-132 27159346-3 2016 The WRK-derived probes show unique reactivity towards the catalytic N-terminal proline in the macrophage migration inhibitory factor (MIF) and can be used to label and, if equipped with a fluorophore, to image MIF activities in living cells. Proline 79-86 macrophage migration inhibitory factor Homo sapiens 134-137 27159346-3 2016 The WRK-derived probes show unique reactivity towards the catalytic N-terminal proline in the macrophage migration inhibitory factor (MIF) and can be used to label and, if equipped with a fluorophore, to image MIF activities in living cells. Proline 79-86 macrophage migration inhibitory factor Homo sapiens 210-213 26453918-4 2015 MIF has an unusual nucleophilic N-terminal proline with catalytic tautomerase activity. Proline 43-50 macrophage migration inhibitory factor Homo sapiens 0-3 26453918-7 2015 We hypothesized that MPO-derived oxidants would oxidize the N-terminal proline of MIF and alter its biological activity. Proline 71-78 macrophage migration inhibitory factor Homo sapiens 82-85 25743213-4 2015 Isothiocyanates inhibit MIF tautomerase activity via covalent modification of the N-terminal proline. Proline 93-100 macrophage migration inhibitory factor Homo sapiens 24-27 22782901-4 2012 Known small molecule MIF inhibitors typically bind in the tautomerase site of the MIF trimer, often covalently modifying the catalytic proline. Proline 135-142 macrophage migration inhibitory factor Homo sapiens 21-24 24916123-3 2014 MIF has an unusual N-terminal proline with catalytic activity, and targeting of this residue by small-molecule inhibitors has been shown to interfere with the biological activity of MIF. Proline 30-37 macrophage migration inhibitory factor Homo sapiens 0-3 24916123-3 2014 MIF has an unusual N-terminal proline with catalytic activity, and targeting of this residue by small-molecule inhibitors has been shown to interfere with the biological activity of MIF. Proline 30-37 macrophage migration inhibitory factor Homo sapiens 182-185 24916123-8 2014 We have characterized the modification introduced by oxidized (-)-epicatechin on MIF by LC-MS (liquid chromatography MS) and found it to occur at the N-terminal proline. Proline 161-168 macrophage migration inhibitory factor Homo sapiens 81-84 22782901-4 2012 Known small molecule MIF inhibitors typically bind in the tautomerase site of the MIF trimer, often covalently modifying the catalytic proline. Proline 135-142 macrophage migration inhibitory factor Homo sapiens 82-85 19723024-4 2009 ITCs covalently modify the N-terminal proline residue of MIF and extinguish its catalytic tautomerase activity. Proline 38-45 macrophage migration inhibitory factor Homo sapiens 57-60 21370851-2 2011 The previously determined crystal structure of cis-CaaD and its promiscuous phenylpyruvate tautomerase (PPT) activity link this dehalogenase to the tautomerase superfamily, a group of homologous proteins that are characterized by a catalytic amino-terminal proline and a beta-alpha-beta structural fold. Proline 257-264 macrophage migration inhibitory factor Homo sapiens 76-102 20516071-7 2010 MIF inhibitors emerging from these studies could be divided into three categories based on their mechanism of action: 1) molecules that covalently modify the catalytic site at the N-terminal proline residue, Pro(1); 2) a novel class of catalytic site inhibitors; and finally 3) molecules that disrupt the trimeric structure of MIF. Proline 191-198 macrophage migration inhibitory factor Homo sapiens 0-3 19776019-6 2009 Site-directed mutagenesis and mass spectrometry showed that PEITC covalently modified the N-terminal proline residue of MIF. Proline 101-108 macrophage migration inhibitory factor Homo sapiens 120-123 16780921-5 2006 Mass spectral analysis established that the amino-terminal proline, previously implicated as a catalytic base in the PPT-catalyzed reaction, is the site of covalent modification. Proline 59-66 macrophage migration inhibitory factor Homo sapiens 117-120 19090677-9 2009 Crystallographic analysis reveals the formation of a stable, novel covalent bond for PMSF between the catalytic nitrogen of the N-terminal proline and the sulfur of PMSF with complete, well-defined electron density in all three active sites of the MIF homotrimer. Proline 139-146 macrophage migration inhibitory factor Homo sapiens 248-251 18794110-6 2008 Using a computational virtual screening strategy, we have identified a unique small molecule inhibitor that serves as a suicide substrate for MIF, resulting in the covalent modification of the catalytically active NH(2)-terminal proline. Proline 229-236 macrophage migration inhibitory factor Homo sapiens 142-145 11773615-2 2002 Although the biological activities of MIF are presumed to require a receptor-based mechanism of action, the protein is also a tautomerase and has a catalytically active N-terminal proline that is invariant in structurally homologous bacterial isomerases. Proline 180-187 macrophage migration inhibitory factor Homo sapiens 38-41 12382291-5 2002 Two hypotheses have been proposed to explain the catalytic inefficiency of MIF: the lower basicity of primary amines with regard to secondary ones and the increased flexibility resulting from the replacement of a proline by residues like glycine. Proline 213-220 macrophage migration inhibitory factor Homo sapiens 75-78 12221083-7 2002 The human and nematode MIF homologues share a tautomerase enzyme activity, which is in each case abolished by the mutation of the N-terminal proline residue. Proline 141-148 macrophage migration inhibitory factor Homo sapiens 23-26 11170644-5 2001 It showed that the hit compound is located in the active site of MIF containing the N-terminal proline which plays an important role in the tautomerase reaction and forms several hydrogen bonds and undergoes hydrophobic interactions. Proline 95-102 macrophage migration inhibitory factor Homo sapiens 65-68 11170644-6 2001 A crystallographic study also revealed that there is a hydrophobic surface which consists of Pro-33, Tyr-36, Trp-108, and Phe-113 at the rim of the active site of MIF, and molecular modeling studies indicated that several more potent hit compounds have the aromatic rings which can interact with this hydrophobic surface. Proline 93-96 macrophage migration inhibitory factor Homo sapiens 163-166 10504254-5 1999 MIF and these two enzymes have an invariant N-terminal proline that serves as a catalytic base. Proline 55-62 macrophage migration inhibitory factor Homo sapiens 0-3 9665726-0 1998 Characterization of the role of the amino-terminal proline in the enzymatic activity catalyzed by macrophage migration inhibitory factor. Proline 51-58 macrophage migration inhibitory factor Homo sapiens 109-136 9665726-4 1998 MIF also has an amino-terminal proline that has been implicated as a catalytic group in the MIF-catalyzed reaction. Proline 31-38 macrophage migration inhibitory factor Homo sapiens 0-3 9649424-3 1998 The three-dimensional structure of MIF is unlike that of any other cytokine, but bears striking resemblance to three microbial enzymes, two of which possess an N-terminal proline that serves as a catalytic base. Proline 171-178 macrophage migration inhibitory factor Homo sapiens 35-38 9649424-4 1998 Human MIF also possesses an N-terminal proline (Pro-1) that is invariant among all known homologues. Proline 39-46 macrophage migration inhibitory factor Homo sapiens 6-9 9649424-5 1998 Multiple sequence alignment of these MIF homologues reveals additional invariant residues that span the entire polypeptide but are in close proximity to the N-terminal proline in the folded protein. Proline 168-175 macrophage migration inhibitory factor Homo sapiens 37-40