PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11570867-4 2001 Surprisingly, mutagenesis of the histidine ligand, His249, to glutamine in the N-lobe half-molecule of human Tf (hTf/2N) shows that iron binding is destabilized and suggests that Gln249 does not bind to iron. Histidine 33-42 transferrin Homo sapiens 109-111 15924420-1 2005 Each homologous lobe of human serum transferrin (hTF) has one Fe(3+) ion bound by an aspartic acid, a histidine, two tyrosine residues, and two oxygens from the synergistic anion, carbonate. Histidine 102-111 transferrin Homo sapiens 36-47 11897357-0 2002 Histidine pK(a) values for the N-lobe of human transferrin: effect of substitution of binding site Asp by Ser (D63S). Histidine 0-9 transferrin Homo sapiens 47-58 19947643-5 2010 There are two ways in which the undissociated form of a bis-chelated complex can interact with transferrin, one "specific" when the carrier possesses a carboxylate group and behaves like a synergistic anion, and another "non-specific" when an imidazole nitrogen of a histidine residue from hTf replaces an equatorially coordinated water molecule giving rise to a ternary species with cis-octahedral geometry and cis-VO(carrier)(2)(hTf) stoichiometry. Histidine 267-276 transferrin Homo sapiens 95-106 12135367-0 2002 Differential effect of a his tag at the N- and C-termini: functional studies with recombinant human serum transferrin. Histidine 25-28 transferrin Homo sapiens 106-117 7947682-4 1994 While evolutionarily divergent, iron binding by all described transferrin lobes is accomplished by a remarkably similar repertoire of residues, including two Tyr, one His, and one Asp, as well as a synergestic bicarbonate anion. Histidine 167-170 transferrin Homo sapiens 62-73 9398207-1 1997 Human serum transferrin N-lobe (hTF/2N) has four iron-binding ligands, including one histidine, one aspartate, and two tyrosines. Histidine 85-94 transferrin Homo sapiens 12-23 10684597-0 2000 Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe. Histidine 17-26 transferrin Homo sapiens 111-122 10684598-3 2000 Possible explanations for the release of iron from transferrin at low pH include protonation of a histidine ligand and the existence of a pH-sensitive "trigger" involving a hydrogen-bonded pair of lysines in the N-lobe of transferrin. Histidine 98-107 transferrin Homo sapiens 51-62 1998724-1 1991 Diferric transferrin was modified using aquopentaammine ruthenium(II), a reagent for surface-accessible uncoordinated histidines. Histidine 118-128 transferrin Homo sapiens 9-20 2065098-1 1991 Sensitive Raman difference spectroscopy was used to monitor the protonation and deprotonation of histidine residues in apo-transferrin. Histidine 97-106 transferrin Homo sapiens 123-134 2065098-6 1991 Using this method, we have measured the Raman difference spectra of human transferrin at different pH values with respect to pH 8.9, titrating its various histidine residues. Histidine 155-164 transferrin Homo sapiens 74-85 1998724-7 1991 His-207 and His-242 in the N-terminal lobe of transferrin and His-535 and His-577 in the C-terminal lobe are within this distance, based on information from the lactoferrin crystal structure. Histidine 0-3 transferrin Homo sapiens 46-57 1998724-7 1991 His-207 and His-242 in the N-terminal lobe of transferrin and His-535 and His-577 in the C-terminal lobe are within this distance, based on information from the lactoferrin crystal structure. Histidine 12-15 transferrin Homo sapiens 46-57 1998724-7 1991 His-207 and His-242 in the N-terminal lobe of transferrin and His-535 and His-577 in the C-terminal lobe are within this distance, based on information from the lactoferrin crystal structure. Histidine 12-15 transferrin Homo sapiens 46-57 1998724-7 1991 His-207 and His-242 in the N-terminal lobe of transferrin and His-535 and His-577 in the C-terminal lobe are within this distance, based on information from the lactoferrin crystal structure. Histidine 12-15 transferrin Homo sapiens 46-57 1197263-5 1975 But under histidine treatment a significant rise of transferrin levels occurred in RDT patients, so that histidine must be considered as a limiting factor in protein metabolism in these cases. Histidine 10-19 transferrin Homo sapiens 52-63 2065098-8 1991 The pH difference spectrum of transferrin obtained is very similar to that of histidine in solution, but with clear differences in the 1200-1400 cm-1 region. Histidine 78-87 transferrin Homo sapiens 30-41 2065098-9 1991 A titration curve with pKa of 6.08 +/- 0.01 fit the data of histidine in solution and a value of 6.56 +/- 0.02 was found for the average value of the 12 histidine residues inside transferrin. Histidine 153-162 transferrin Homo sapiens 179-190 3252892-4 1988 The most strongly associated interaction is the chelation of iron by transferrin, with an association constant of approximately 10(21); tyrosines, histidines, and sometimes aspartate are involved. Histidine 147-157 transferrin Homo sapiens 69-80 3759950-0 1986 The influence of uncoordinated histidines on iron release from transferrin. Histidine 31-41 transferrin Homo sapiens 63-74 3759950-2 1986 Histidine residues that influence the chelate-mediated removal of iron from transferrin have been investigated. Histidine 0-9 transferrin Homo sapiens 76-87 3759950-3 1986 Diferric human serum transferrin was chemically modified to various extents using ethoxyformic anhydride, a reagent for histidines. Histidine 120-130 transferrin Homo sapiens 21-32 3759950-5 1986 There are 18 histidine residues in transferrin. Histidine 13-22 transferrin Homo sapiens 35-46 558796-1 1977 The chemical reactivity of histidines in ovotransferrin and human serum transferrin was studied utilizing two different reactions. Histidine 27-37 transferrin Homo sapiens 44-55 558796-2 1977 Upon dye-sensitized photooxidation of ovotransferrin and ethoxyformylation of human serum transferrin and ovotransferrin, losses in histidine and iron-binding activity were observed. Histidine 132-141 transferrin Homo sapiens 41-52 558796-4 1977 The histidines of human serum transferrin showed a greater reactivity toward the reagent than did those of ovotransferrin. Histidine 4-14 transferrin Homo sapiens 30-41 34687221-7 2021 This affinity microfluidic chip has pre-fractioned four human plasma proteins (fibrinogen, immunoglobulin, transferrin and human serum albumin) based on their surface exposed histidine surface topography. Histidine 175-184 transferrin Homo sapiens 107-118 1157951-0 1975 Comparative study on histidine modification by diethylpyrocarbonate in human serotransferrin and lactotransferrin. Histidine 21-30 transferrin Homo sapiens 77-92 1197263-5 1975 But under histidine treatment a significant rise of transferrin levels occurred in RDT patients, so that histidine must be considered as a limiting factor in protein metabolism in these cases. Histidine 105-114 transferrin Homo sapiens 52-63 4444649-0 1974 [The influence of l-histidine substitution on protein metabolism (transferrin and complement system) and renal anaemia in endstage renal failure (author"s transl)]. Histidine 18-29 transferrin Homo sapiens 66-77 33625414-8 2021 The interaction of the complexes with human transferrin (hTf) proteins was studied through molecular docking calculations, suggesting favorable binding through histidine residues and possible internalization into cancer cells via TfR-mediated endocytosis. Histidine 160-169 transferrin Homo sapiens 44-55 15938304-0 1967 Influence of transferrin saturation on the effect of intraluminal fructose or histidine on iron absorption. Histidine 78-87 transferrin Homo sapiens 13-24 25617389-2 2015 The usefulness of the morpholinopropanesulfonic acid (MOPS)-histidine buffer in detecting beta2-transferrin, which is only found in the cerebrospinal fluid, was compared with the standard barbital buffer. Histidine 60-69 transferrin Homo sapiens 96-107 30270390-7 2018 All coordinating groups present in the Fe(iii) transferrin complex are also found for Cm(iii), i.e. Asp 63, Tyr 95, Tyr 188 and His 249. Histidine 128-131 transferrin Homo sapiens 47-58 30270390-10 2018 The results underline an involvement of Asp 63, Tyr 95, Tyr 188 and His 249 as well as carbonate in Cm(iii) coordination at the transferrin Fe(iii) binding site. Histidine 68-71 transferrin Homo sapiens 128-139 25617389-4 2015 RESULTS: The MOPS-histidine and barbital buffers revealed 5 transferrin bands and 2 transferrin bands with CSF, respectively. Histidine 18-27 transferrin Homo sapiens 60-71 25617389-4 2015 RESULTS: The MOPS-histidine and barbital buffers revealed 5 transferrin bands and 2 transferrin bands with CSF, respectively. Histidine 18-27 transferrin Homo sapiens 84-95 25617389-8 2015 CONCLUSION: Agarose electrophoresis with the MOPS-histidine buffer increases the resolution of transferrin isoforms. Histidine 50-59 transferrin Homo sapiens 95-106