PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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)). Phospholipids 84-97 apolipoprotein C2 Homo sapiens 253-272 20889492-2 2011 Previously, the effects of phospholipids on amyloid fibril formation by apolipoprotein (apo) C-II have been examined, where low concentrations of micellar phospholipids and lipid bilayers induce a new, straight rod-like morphology for apoC-II fibrils. Phospholipids 155-168 apolipoprotein C2 Homo sapiens 235-242 20433849-5 2010 We used fluorescence techniques and stopped-flow analysis to identify the individual kinetic steps involved in the activation of apoC-II fibril formation by the short-chain phospholipid dihexanoyl phosphatidylcholine (DHPC). Phospholipids 173-185 apolipoprotein C2 Homo sapiens 129-136 20496878-1 2010 Molecular dynamics simulations were implemented to investigate the effects of phospholipid concentration on the conformation and dynamics of the amyloidogenic peptide apoC-II(60-70). Phospholipids 78-90 apolipoprotein C2 Homo sapiens 167-174 21985034-3 2011 ApoC-II fibril formation is activated by submicellar phospholipids but inhibited by micellar lipids. Phospholipids 53-66 apolipoprotein C2 Homo sapiens 0-7 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)). Phospholipids 84-97 apolipoprotein C2 Homo sapiens 274-281 18769912-1 2008 We have performed experimental and computational studies to investigate the influences of phospholipids, methionine oxidation and acidic pH on amyloid fibril formation by a peptide derived from human apolipoprotein C-II (apoC-II), a known component of proteinaceous atherosclerotic plaques. Phospholipids 90-103 apolipoprotein C2 Homo sapiens 221-228 18769912-1 2008 We have performed experimental and computational studies to investigate the influences of phospholipids, methionine oxidation and acidic pH on amyloid fibril formation by a peptide derived from human apolipoprotein C-II (apoC-II), a known component of proteinaceous atherosclerotic plaques. Phospholipids 90-103 apolipoprotein C2 Homo sapiens 200-219 14645070-0 2003 Phospholipid complexation and association with apolipoprotein C-II: insights from mass spectrometry. Phospholipids 0-12 apolipoprotein C2 Homo sapiens 47-66 18005990-0 2008 Phospholipid interaction induces molecular-level polymorphism in apolipoprotein C-II amyloid fibrils via alternative assembly pathways. Phospholipids 0-12 apolipoprotein C2 Homo sapiens 65-84 18005990-4 2008 Submicellar concentrations of short-chain phospholipids increase the rate of apoC-II fibril formation in an acyl-chain-length- and concentration-dependent fashion, while high micellar concentrations of phospholipids completely inhibited amyloid formation. Phospholipids 42-55 apolipoprotein C2 Homo sapiens 77-84 18005990-5 2008 At lower concentrations of soluble phospholipid complexes, fibril formation by apoC-II was only partially inhibited, and under these conditions, aggregation followed a two-phase process. Phospholipids 35-47 apolipoprotein C2 Homo sapiens 79-86 14645070-5 2003 The mass spectra of heterogeneous suspensions and their complexes with apolipoprotein C-II demonstrate that the protein binds simultaneously to two different phospholipids. Phospholipids 158-171 apolipoprotein C2 Homo sapiens 71-90 14645070-7 2003 These observations demonstrate a capacity for apolipoprotein C-II to change the topology of the phospholipid surface. Phospholipids 96-108 apolipoprotein C2 Homo sapiens 46-65 3994718-2 1985 Rates of phospholipid hydrolysis were dependent on apolipoprotein C-II (the activator protein for LpL) phospholipid fatty acyl composition, and lipid-packing density. Phospholipids 9-21 apolipoprotein C2 Homo sapiens 51-70 10972686-12 2000 Multivariate analysis suggested that the relative lack of apoCII and apoCIII on patients VLDL1 was related to smaller particle size and increased free cholesterol:phospholipid (FC:PL) ratio. Phospholipids 163-175 apolipoprotein C2 Homo sapiens 58-64 3166993-9 1988 The dissociation constants, Kd, of apoC-I, apoC-II, and apoC-III bound to the surface monolayer of phospholipid-coated latex beads were 0.5, 1.4, and 0.5 microM, respectively. Phospholipids 99-111 apolipoprotein C2 Homo sapiens 43-50 11311244-0 2001 Sub-micellar phospholipid accelerates amyloid formation by apolipoprotein C-II. Phospholipids 13-25 apolipoprotein C2 Homo sapiens 59-78 11311244-3 2001 We have investigated the effect of the short-chain phospholipid, dihexanoylphosphatidylcholine (DHPC) on amyloid formation by apoC-II. Phospholipids 51-63 apolipoprotein C2 Homo sapiens 126-133 11162594-3 2001 ApoA-I and all of the other exchangeable apolipoproteins tested (apoA-II, apoA-IV, apoC-I, apoC-II, apoC-III, apoE) showed greater than a threefold increase in cholesterol and phospholipid efflux from ABCAI-GFP transfected cells compared to control cells. Phospholipids 176-188 apolipoprotein C2 Homo sapiens 91-98 3942763-4 1986 In contrast, apolipoprotein C-II increased the apparent Vmax from 2.4 to 20.0 mmol free fatty acid/h per mg enzyme for the lipoprotein lipase-catalyzed hydrolysis of trioleoylglycerol/phospholipid particles with little change in Kmapp (1.0 mM). Phospholipids 184-196 apolipoprotein C2 Homo sapiens 13-32 3942763-5 1986 Addition of apolipoprotein C-II-deficient triacylglycerol-rich lipoproteins or high-density lipoproteins to trioleoylglycerol/phospholipid particles in the presence of apolipoprotein C-II inhibited lipoprotein lipase activity. Phospholipids 126-138 apolipoprotein C2 Homo sapiens 168-187 3994718-2 1985 Rates of phospholipid hydrolysis were dependent on apolipoprotein C-II (the activator protein for LpL) phospholipid fatty acyl composition, and lipid-packing density. Phospholipids 103-115 apolipoprotein C2 Homo sapiens 51-70 6895327-6 1981 With limited phospholipid (40 micrograms), the amount of enzyme which associated with lipid decreased in the presence of apolipoprotein C-II (20 micrograms). Phospholipids 13-25 apolipoprotein C2 Homo sapiens 121-140 29791776-2 2018 Lipid-free apoC-II readily self-assembles into twisted-ribbon amyloid fibrils but forms straight, rod-like amyloid fibrils in the presence of low concentrations of micellar phospholipids. Phospholipids 173-186 apolipoprotein C2 Homo sapiens 11-18 26149930-7 2015 Short-chain phospholipids at submicellar concentrations significantly accelerate amyloid formation by inducing a tetrameric form of apoC-II that can nucleate fibril aggregation. Phospholipids 12-25 apolipoprotein C2 Homo sapiens 132-139 26149930-8 2015 Conversely, phospholipid micelles and bilayers inhibit the formation of apoC-II ribbon-type fibrils, but induce slow formation of amyloid with a distinct straight fibril morphology. Phospholipids 12-24 apolipoprotein C2 Homo sapiens 72-79 226140-4 1979 With apolipoprotein C-II and apolipoprotein C-III there was a decrease in surface radioactivity indicating that the apoproteins were removing phospholipid from the interface; the removal of phospholipid was specific for apolipoprotein C-II and apolipoprotein C-III. Phospholipids 142-154 apolipoprotein C2 Homo sapiens 5-49 226140-4 1979 With apolipoprotein C-II and apolipoprotein C-III there was a decrease in surface radioactivity indicating that the apoproteins were removing phospholipid from the interface; the removal of phospholipid was specific for apolipoprotein C-II and apolipoprotein C-III. Phospholipids 190-202 apolipoprotein C2 Homo sapiens 220-264 26026161-8 2015 We characterized apoC-II at phospholipid/triacylglycerol/water interfaces, which more closely mimic lipoprotein surfaces. Phospholipids 28-40 apolipoprotein C2 Homo sapiens 17-24 26026161-13 2015 This indicates that apoC-II removed phospholipid from the interface upon desorption. Phospholipids 36-48 apolipoprotein C2 Homo sapiens 20-27 26026161-16 2015 Above its retention pressure, apoC-II desorbs and removes phospholipid. Phospholipids 58-70 apolipoprotein C2 Homo sapiens 30-37