PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25609257-9 2015 ApoC-II D69K fibrils exhibited reduced thioflavin T binding capacity compared to that of fibrils formed by WT apoC-II and apoC-II KDDK. thioflavin T 39-51 apolipoprotein C2 Homo sapiens 0-7 17217959-6 2007 Synthetic apoC-II(56-76) readily formed fibrils, albeit with a different morphology and thioflavinT fluorescence yield compared to full-length apoC-II. thioflavin T 88-99 apolipoprotein C2 Homo sapiens 10-17 10889036-1 2000 Human apolipoprotein C-II (apoC-II) self-associates in solution to form aggregates with the characteristics of amyloid including red-green birefringence in the presence of Congo Red under cross-polarized light, increased fluorescence in the presence of thioflavin T, and a fibrous structure when examined by electron microscopy. thioflavin T 253-265 apolipoprotein C2 Homo sapiens 6-25 10889036-1 2000 Human apolipoprotein C-II (apoC-II) self-associates in solution to form aggregates with the characteristics of amyloid including red-green birefringence in the presence of Congo Red under cross-polarized light, increased fluorescence in the presence of thioflavin T, and a fibrous structure when examined by electron microscopy. thioflavin T 253-265 apolipoprotein C2 Homo sapiens 27-34 12668464-7 2003 The kinetics of aggregation (1 mg/mL apoC-II) as assessed using thioflavin T and preparative pelleting assays reveal that monomeric apoC-II is depleted after approximately 12 h incubation at room temperature. thioflavin T 64-76 apolipoprotein C2 Homo sapiens 37-44 12668464-7 2003 The kinetics of aggregation (1 mg/mL apoC-II) as assessed using thioflavin T and preparative pelleting assays reveal that monomeric apoC-II is depleted after approximately 12 h incubation at room temperature. thioflavin T 64-76 apolipoprotein C2 Homo sapiens 132-139 19537801-2 2009 Thioflavin T fluorescence studies showed that submicellar levels of the short-chain phospholipids, dipentanoylphosphatidylcholine and dihexanoylphosphatidylcholine, strongly inhibited amyloid fibril formation by an 11-residue peptide derived from human apolipoprotein C-II (apoC-II(60-70)). thioflavin T 0-12 apolipoprotein C2 Homo sapiens 253-272 19537801-2 2009 Thioflavin T fluorescence studies showed that submicellar levels of the short-chain phospholipids, dipentanoylphosphatidylcholine and dihexanoylphosphatidylcholine, strongly inhibited amyloid fibril formation by an 11-residue peptide derived from human apolipoprotein C-II (apoC-II(60-70)). thioflavin T 0-12 apolipoprotein C2 Homo sapiens 274-281