PubMed:9546397 JSONTXT

{"project":"NCBI-Disease-Corpus-GPT5-withguidelines","denotations":[{"id":"T1","span":{"begin":25,"end":40},"obj":"Modifier"},{"id":"T2","span":{"begin":173,"end":194},"obj":"DiseaseClass"},{"id":"T3","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T4","span":{"begin":413,"end":428},"obj":"Modifier"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-GPT5-noguidelines","denotations":[{"id":"T1","span":{"begin":173,"end":194},"obj":"DiseaseClass"},{"id":"T2","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T3","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-GPT5-guidelineprompt","denotations":[{"id":"T1","span":{"begin":25,"end":40},"obj":"Modifier"},{"id":"T2","span":{"begin":173,"end":194},"obj":"Modifier"},{"id":"T3","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T4","span":{"begin":413,"end":428},"obj":"Modifier"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-Moderated1","denotations":[{"id":"T1","span":{"begin":25,"end":40},"obj":"Modifier"},{"id":"T2","span":{"begin":173,"end":194},"obj":"DiseaseClass"},{"id":"T3","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T4","span":{"begin":413,"end":428},"obj":"Modifier"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"9546397-1#0#3#gene3077","span":{"begin":120,"end":123},"obj":"gene3077"},{"id":"9546397-1#10#13#gene3107","span":{"begin":130,"end":133},"obj":"gene3107"},{"id":"9546397-1#75#101#diseaseC0392514","span":{"begin":195,"end":221},"obj":"diseaseC0392514"},{"id":"9546397-1#53#74#diseaseC0018995","span":{"begin":173,"end":194},"obj":"diseaseC0018995"},{"id":"9546397-1#75#101#diseaseC0392514","span":{"begin":195,"end":221},"obj":"diseaseC0392514"}],"relations":[{"id":"0#3#gene307775#101#diseaseC0392514","pred":"associated_with","subj":"9546397-1#0#3#gene3077","obj":"9546397-1#75#101#diseaseC0392514"},{"id":"0#3#gene307753#74#diseaseC0018995","pred":"associated_with","subj":"9546397-1#0#3#gene3077","obj":"9546397-1#53#74#diseaseC0018995"},{"id":"0#3#gene307775#101#diseaseC0392514","pred":"associated_with","subj":"9546397-1#0#3#gene3077","obj":"9546397-1#75#101#diseaseC0392514"},{"id":"10#13#gene310775#101#diseaseC0392514","pred":"associated_with","subj":"9546397-1#10#13#gene3107","obj":"9546397-1#75#101#diseaseC0392514"},{"id":"10#13#gene310753#74#diseaseC0018995","pred":"associated_with","subj":"9546397-1#10#13#gene3107","obj":"9546397-1#53#74#diseaseC0018995"},{"id":"10#13#gene310775#101#diseaseC0392514","pred":"associated_with","subj":"9546397-1#10#13#gene3107","obj":"9546397-1#75#101#diseaseC0392514"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBIDiseaseCorpus","denotations":[{"id":"T1","span":{"begin":25,"end":40},"obj":"Modifier:D006432"},{"id":"T2","span":{"begin":173,"end":194},"obj":"SpecificDisease:D019190"},{"id":"T3","span":{"begin":195,"end":221},"obj":"SpecificDisease:D006432"},{"id":"T4","span":{"begin":413,"end":428},"obj":"Modifier:D006432"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":25,"end":40},"obj":"Disease"},{"id":"T2","span":{"begin":195,"end":221},"obj":"Disease"},{"id":"T3","span":{"begin":413,"end":428},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0006507"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0006507"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0006507"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Test","denotations":[{"id":"T171","span":{"begin":25,"end":40},"obj":"Modifier"},{"id":"T172","span":{"begin":173,"end":194},"obj":"SpecificDisease"},{"id":"T173","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T174","span":{"begin":413,"end":428},"obj":"Modifier"}],"attributes":[{"id":"A171","pred":"database_id","subj":"T171","obj":"D006432"},{"id":"A172","pred":"database_id","subj":"T172","obj":"D019190"},{"id":"A173","pred":"database_id","subj":"T173","obj":"D006432"},{"id":"A174","pred":"database_id","subj":"T174","obj":"D006432"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Test-Assistant-Knowledge","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Test-4o-NoGuidelineInPrompt","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-o3-2","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-high-o3-1","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-high-o3-2","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Test-4o-GuidelineInPrompt","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-UpdatedGuideline","denotations":[{"id":"T1","span":{"begin":173,"end":186},"obj":"Modifier"},{"id":"T2","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T3","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-humanintheloop","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-rezarta1","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-All","denotations":[{"id":"T171","span":{"begin":25,"end":40},"obj":"Modifier"},{"id":"T172","span":{"begin":173,"end":194},"obj":"SpecificDisease"},{"id":"T173","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T174","span":{"begin":413,"end":428},"obj":"Modifier"}],"attributes":[{"id":"A171","pred":"database_id","subj":"T171","obj":"D006432"},{"id":"A172","pred":"database_id","subj":"T172","obj":"D019190"},{"id":"A173","pred":"database_id","subj":"T173","obj":"D006432"},{"id":"A174","pred":"database_id","subj":"T174","obj":"D006432"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-2stage-All","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-rezarta-All","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"Modifier"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-4oGuideline-All","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"NCBI-Disease-Corpus-Simple-All","denotations":[{"id":"T1","span":{"begin":173,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":438},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":641,"end":663},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0097708"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"123456","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"SpecificDisease"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}

{"project":"12345","denotations":[{"id":"T1","span":{"begin":195,"end":221},"obj":"SpecificDisease"},{"id":"T2","span":{"begin":413,"end":428},"obj":"Modifier"}],"text":"Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.\nHFE is an MHC-related protein that is mutated in the iron-overload disease hereditary hemochromatosis. HFE binds to transferrin receptor (TfR) and reduces its affinity for iron-loaded transferrin, implicating HFE in iron metabolism. The 2.6 A crystal structure of HFE reveals the locations of hemochromatosis mutations and a patch of histidines that could be involved in pH-dependent interactions. We also demonstrate that soluble TfR and HFE bind tightly at the basic pH of the cell surface, but not at the acidic pH of intracellular vesicles. TfR:HFE stoichiometry (2:1) differs from TfR:transferrin stoichiometry (2:2), implying a different mode of binding for HFE and transferrin to TfR, consistent with our demonstration that HFE, transferrin, and TfR form a ternary complex."}