PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7696519-5 1995 In addition, from the proximal histidine resonances, we have observed a preference for the binding of oxygen to the alpha-chain (up to about 10%) of hemoglobin over the beta-chain in both the presence and absence of 2,3-diphosphoglycerate. Histidine 31-40 Fc gamma receptor and transporter Homo sapiens 116-127 1390944-0 1992 Hemoglobin Rouen (alpha-140 (HC2) Tyr-->His): alteration of the alpha-chain C-terminal region and moderate increase in oxygen affinity. Histidine 40-43 Fc gamma receptor and transporter Homo sapiens 64-75 7889418-4 1994 We find that alteration of a histidine pair within the alpha 3 domain of FcRn and of a nearby loop (the FcRn counterpart of the class I CD8-binding loop) affects the affinity for IgG. Histidine 29-38 Fc gamma receptor and transporter Homo sapiens 73-77 7889418-4 1994 We find that alteration of a histidine pair within the alpha 3 domain of FcRn and of a nearby loop (the FcRn counterpart of the class I CD8-binding loop) affects the affinity for IgG. Histidine 29-38 Fc gamma receptor and transporter Homo sapiens 104-108 7889418-7 1994 Three histidines present at the CH2-CH3 domain interface of Fc could be partially responsible for the pH-dependent interaction between FcRn and IgG. Histidine 6-16 Fc gamma receptor and transporter Homo sapiens 135-139 1511986-4 1992 Hb Zaire [alpha 116(GH4)-His-Leu-Pro-Ala-Glu-117 (GH5)] is the second example in which a short amino acid sequence is inserted within the alpha-chain. Histidine 25-28 Fc gamma receptor and transporter Homo sapiens 138-149 34447559-8 2021 In agreement with these results, careful mapping of all hydrolyzed Asp-X bonds on the protein structure revealed that the lower reactivity toward the alpha-chain was consistent with the presence of more redox-active amino acids (Tyr and His) in this subunit in comparison with the beta-chain. Histidine 237-240 Fc gamma receptor and transporter Homo sapiens 150-161 27433338-6 2016 Milling of the lyophilized IgG2 M428L FcRn-binding variant after formulation in 10 mmol/L histidine, pH 5.7, 8.5% sucrose, 0.04% PS80 did not alter the physicochemical properties nor the molecular integrity compared to the batch released in PBS. Histidine 90-99 Fc gamma receptor and transporter Homo sapiens 38-42 6155159-1 1980 In each of two families from Sardinia, Italy, we have found segregation for two alpha-chain hemoglobin variants, which we have identified as G Philadelphia [alpha 68 (E17) Asn leads to Lys] and J Sardinia [alpha 50 (CE8) His leads to Asp], respectively. Histidine 221-224 Fc gamma receptor and transporter Homo sapiens 80-91 1098653-11 1975 The utility of the method is demonstrated by repeating the determination of the substitution in haemoglobin Hopkins-2, a known alpha-chain core variant in which histidine-alpha112 (G19) is replaced by an aspartic acid residue. Histidine 161-170 Fc gamma receptor and transporter Homo sapiens 127-138 5355345-5 1969 The asparagine residue G10(108)beta lies in the internal cavity of the tetrameric molecule and its main chain carbonyl is thought to be hydrogen bonded to histidine G10(103)alpha at the region of contact between alpha- and beta-chains. Histidine 155-164 Fc gamma receptor and transporter Homo sapiens 212-234 14190977-0 1964 SUBSTITUTION OF TYROSINE FOR HISTIDINE (87 IN THE ALPHA-CHAIN OF HEMOGLOBIN M-IWATE). Histidine 29-38 Fc gamma receptor and transporter Homo sapiens 50-61 26627822-1 2016 Crystallographic evidence suggests that the pH-dependent affinity of IgG molecules for the neonatal Fc receptor (FcRn) receptor primarily arises from salt bridges involving IgG histidine residues, resulting in moderate affinity at mildly acidic conditions. Histidine 177-186 Fc gamma receptor and transporter Homo sapiens 91-111 26627822-1 2016 Crystallographic evidence suggests that the pH-dependent affinity of IgG molecules for the neonatal Fc receptor (FcRn) receptor primarily arises from salt bridges involving IgG histidine residues, resulting in moderate affinity at mildly acidic conditions. Histidine 177-186 Fc gamma receptor and transporter Homo sapiens 113-117 24469444-6 2014 At last, this study also allows an accurate structural definition of residues considered for decades as important to the human IgG/FcRn interaction and reveals Fc His(310) as a significant contributor to pH-dependent binding. Histidine 163-166 Fc gamma receptor and transporter Homo sapiens 131-135 22215085-5 2012 These networks involve conserved histidines in both FcRn and albumin domain III. Histidine 33-43 Fc gamma receptor and transporter Homo sapiens 52-56 12568815-5 2003 When comparing with human Hb alpha-chain, alterations in important regions can be noted: alpha110 Ala-Gly, alpha114 Pro-Gly, alpha117 Phe-Tyr and alpha122 His-Gln. Histidine 155-158 Fc gamma receptor and transporter Homo sapiens 29-40 20592032-13 2010 Modeling of the peptide:FcRn structure as compared with available structural data on Fc and FcRn suggest that the His-6 and Phe-7 (peptide) partially mimic the interaction of His-310 and Ile-253 (Fc) in binding to FcRn, but using a different backbone topology. Histidine 114-117 Fc gamma receptor and transporter Homo sapiens 24-28 20592032-13 2010 Modeling of the peptide:FcRn structure as compared with available structural data on Fc and FcRn suggest that the His-6 and Phe-7 (peptide) partially mimic the interaction of His-310 and Ile-253 (Fc) in binding to FcRn, but using a different backbone topology. Histidine 114-117 Fc gamma receptor and transporter Homo sapiens 92-96 20592032-13 2010 Modeling of the peptide:FcRn structure as compared with available structural data on Fc and FcRn suggest that the His-6 and Phe-7 (peptide) partially mimic the interaction of His-310 and Ile-253 (Fc) in binding to FcRn, but using a different backbone topology. Histidine 114-117 Fc gamma receptor and transporter Homo sapiens 92-96 20592032-13 2010 Modeling of the peptide:FcRn structure as compared with available structural data on Fc and FcRn suggest that the His-6 and Phe-7 (peptide) partially mimic the interaction of His-310 and Ile-253 (Fc) in binding to FcRn, but using a different backbone topology. Histidine 175-178 Fc gamma receptor and transporter Homo sapiens 24-28 20592032-13 2010 Modeling of the peptide:FcRn structure as compared with available structural data on Fc and FcRn suggest that the His-6 and Phe-7 (peptide) partially mimic the interaction of His-310 and Ile-253 (Fc) in binding to FcRn, but using a different backbone topology. Histidine 175-178 Fc gamma receptor and transporter Homo sapiens 92-96 20592032-13 2010 Modeling of the peptide:FcRn structure as compared with available structural data on Fc and FcRn suggest that the His-6 and Phe-7 (peptide) partially mimic the interaction of His-310 and Ile-253 (Fc) in binding to FcRn, but using a different backbone topology. Histidine 175-178 Fc gamma receptor and transporter Homo sapiens 92-96 17048273-0 2006 The conserved histidine 166 residue of the human neonatal Fc receptor heavy chain is critical for the pH-dependent binding to albumin. Histidine 14-23 Fc gamma receptor and transporter Homo sapiens 49-69 17048273-3 2006 The FcRn-IgG interaction has been extensively characterized at the amino acid level and shown to depend on conserved histidine residues in the IgG-Fc part that interact with negatively charged residues in the alpha-2 domain of FcRn. Histidine 117-126 Fc gamma receptor and transporter Homo sapiens 4-8 17048273-3 2006 The FcRn-IgG interaction has been extensively characterized at the amino acid level and shown to depend on conserved histidine residues in the IgG-Fc part that interact with negatively charged residues in the alpha-2 domain of FcRn. Histidine 117-126 Fc gamma receptor and transporter Homo sapiens 227-231 9493268-11 1998 The pH dependence of IgG binding to FcRn can therefore primarily be attributed to titration of histidine residues on Fc that interact with anionic pockets on the receptor. Histidine 95-104 Fc gamma receptor and transporter Homo sapiens 36-40 12372819-6 2002 Using N-terminal sequencing they were identified as the normal cleavage site Arg(494)-Val(495) and the novel site Arg(424)-His(425) located in the K4 domain of the alpha-chain. Histidine 123-126 Fc gamma receptor and transporter Homo sapiens 164-175 9493268-12 1998 The FcRn dimer, which is required for high affinity binding of IgG, is itself stabilized at acidic pH by histidine-mediated salt bridges and a sidechain rearrangement that creates a more favorable interaction with an anionic pocket at pH 6.5 relative to pH 8. Histidine 105-114 Fc gamma receptor and transporter Homo sapiens 4-8