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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-26 Sentence denotes Cloning of human PEX cDNA.
T1 0-26 Sentence denotes Cloning of human PEX cDNA.
TextSentencer_T2 27-92 Sentence denotes Expression, subcellular localization, and endopeptidase activity.
T2 27-92 Sentence denotes Expression, subcellular localization, and endopeptidase activity.
TextSentencer_T3 93-173 Sentence denotes Mutations in the PEX gene are responsible for X-linked hypophosphatemic rickets.
T3 93-173 Sentence denotes Mutations in the PEX gene are responsible for X-linked hypophosphatemic rickets.
TextSentencer_T4 174-358 Sentence denotes To gain insight into the role of PEX in normal physiology we have cloned the human full-length cDNA and studied its tissue expression, subcellular localization, and peptidase activity.
T4 174-358 Sentence denotes To gain insight into the role of PEX in normal physiology we have cloned the human full-length cDNA and studied its tissue expression, subcellular localization, and peptidase activity.
TextSentencer_T5 359-510 Sentence denotes We show that the cDNA encodes a 749-amino acid protein structurally related to a family of neutral endopeptidases that include neprilysin as prototype.
T5 359-510 Sentence denotes We show that the cDNA encodes a 749-amino acid protein structurally related to a family of neutral endopeptidases that include neprilysin as prototype.
TextSentencer_T6 511-598 Sentence denotes By Northern blot analysis, the size of the full-length PEX transcript is 6.5 kilobases.
T6 511-598 Sentence denotes By Northern blot analysis, the size of the full-length PEX transcript is 6.5 kilobases.
TextSentencer_T7 599-784 Sentence denotes PEX expression, as determined by semi-quantitative polymerase chain reaction, is high in bone and in tumor tissue associated with the paraneoplastic syndrome of renal phosphate wasting.
T7 599-784 Sentence denotes PEX expression, as determined by semi-quantitative polymerase chain reaction, is high in bone and in tumor tissue associated with the paraneoplastic syndrome of renal phosphate wasting.
TextSentencer_T8 785-969 Sentence denotes PEX is glycosylated in the presence of canine microsomal membranes and partitions exclusively in the detergent phase from Triton X-114 extractions of transiently transfected COS cells.
T8 785-969 Sentence denotes PEX is glycosylated in the presence of canine microsomal membranes and partitions exclusively in the detergent phase from Triton X-114 extractions of transiently transfected COS cells.
TextSentencer_T9 970-1315 Sentence denotes Immunofluorescence studies in A293 cells expressing PEX tagged with a c-myc epitope show a predominant cell-surface location for the protein with its COOH-terminal domain in the extracellular compartment, substantiating the assumption that PEX, like other members of the neutral endopeptidase family, is a type II integral membrane glycoprotein.
T9 970-1315 Sentence denotes Immunofluorescence studies in A293 cells expressing PEX tagged with a c-myc epitope show a predominant cell-surface location for the protein with its COOH-terminal domain in the extracellular compartment, substantiating the assumption that PEX, like other members of the neutral endopeptidase family, is a type II integral membrane glycoprotein.
TextSentencer_T10 1316-1545 Sentence denotes Cell membranes from cultured COS cells transiently expressing PEX efficiently degrade exogenously added parathyroid hormone-derived peptides, demonstrating for the first time that recombinant PEX can function as an endopeptidase.
T10 1316-1545 Sentence denotes Cell membranes from cultured COS cells transiently expressing PEX efficiently degrade exogenously added parathyroid hormone-derived peptides, demonstrating for the first time that recombinant PEX can function as an endopeptidase.
TextSentencer_T11 1546-1708 Sentence denotes PEX peptidase activity may provide a convenient target for pharmacological intervention in states of altered phosphate homeostasis and in metabolic bone diseases.
T11 1546-1708 Sentence denotes PEX peptidase activity may provide a convenient target for pharmacological intervention in states of altered phosphate homeostasis and in metabolic bone diseases.