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Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-134 Sentence denotes N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
T1 0-134 Sentence denotes N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
T1 0-134 Sentence denotes N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
TextSentencer_T2 135-359 Sentence denotes Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
T2 135-359 Sentence denotes Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
T2 135-359 Sentence denotes Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
TextSentencer_T3 360-538 Sentence denotes We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
T3 360-538 Sentence denotes We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
T3 360-538 Sentence denotes We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
TextSentencer_T4 539-705 Sentence denotes To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
T4 539-705 Sentence denotes To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
T4 539-705 Sentence denotes To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
TextSentencer_T5 706-859 Sentence denotes N382Q/N393Q and N289Q/N382Q/N393Q were sequestered in the endoplasmic reticulum, resulting in a severe reduction in the cellular incorporation of Ac-LDL.
T5 706-859 Sentence denotes N382Q/N393Q and N289Q/N382Q/N393Q were sequestered in the endoplasmic reticulum, resulting in a severe reduction in the cellular incorporation of Ac-LDL.
T5 706-859 Sentence denotes N382Q/N393Q and N289Q/N382Q/N393Q were sequestered in the endoplasmic reticulum, resulting in a severe reduction in the cellular incorporation of Ac-LDL.
TextSentencer_T6 860-997 Sentence denotes N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
T6 860-997 Sentence denotes N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
T6 860-997 Sentence denotes N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
TextSentencer_T7 998-1164 Sentence denotes These results indicate that the N-glycan of Asn(393) regulates the intracellular sorting of SREC-I and that the N-glycan of Asn(382) controls ligand-binding affinity.
T7 998-1164 Sentence denotes These results indicate that the N-glycan of Asn(393) regulates the intracellular sorting of SREC-I and that the N-glycan of Asn(382) controls ligand-binding affinity.
T7 998-1164 Sentence denotes These results indicate that the N-glycan of Asn(393) regulates the intracellular sorting of SREC-I and that the N-glycan of Asn(382) controls ligand-binding affinity.
TextSentencer_T8 1165-1235 Sentence denotes Furthermore, we detected an enhanced trypsin sensitivity of the N289Q.
T8 1165-1235 Sentence denotes Furthermore, we detected an enhanced trypsin sensitivity of the N289Q.
T8 1165-1235 Sentence denotes Furthermore, we detected an enhanced trypsin sensitivity of the N289Q.
TextSentencer_T9 1236-1367 Sentence denotes Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
T9 1236-1367 Sentence denotes Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
T9 1236-1367 Sentence denotes Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
TextSentencer_T10 1368-1454 Sentence denotes In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
T10 1368-1454 Sentence denotes In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
T10 1368-1454 Sentence denotes In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
TextSentencer_T11 1455-1517 Sentence denotes A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
T11 1455-1517 Sentence denotes A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
T11 1455-1517 Sentence denotes A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
TextSentencer_T12 1518-1714 Sentence denotes Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
T12 1518-1714 Sentence denotes Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
T12 1518-1984 Sentence denotes Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I. These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
TextSentencer_T13 1715-1984 Sentence denotes These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
T13 1715-1984 Sentence denotes These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.