PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
22370559-4	2012	Our fluorescence quenching and sedimentation velocity experiments with Alexa488-labeled apoC-II indicated a time-dependent subunit interchange for both linear and closed-loop fibrils, while dilution experiments using mature fibrils indicated a shift to smaller size distributions consistent with a reversible assembly pathway.	alexa488	71-79	apolipoprotein C2	Homo sapiens	88-95
23470567-4	2013	METHODS: We performed detailed biochemical/genetic analyses of our new case of hypoapoC-II, manifesting severe hypertriglyceridemia (plasma triglycerides, 3235 mg dL(-1)) with markedly reduced levels of plasma apoC-II (0.6 mg dL(-1)).	Triglycerides	140-153	apolipoprotein C2	Homo sapiens	83-90
22623394-4	2012	Interestingly, the rs2304672 SNP interacted with plasma total SFA concentrations to affect fasting plasma TG, TG-rich lipoprotein (TRL-TG), total cholesterol, apoC-II, apoB, and apoB-48 concentrations (P-interaction < 0.001-0.046).	suppressive factor of allergy	62-65	apolipoprotein C2	Homo sapiens	159-166
22262056-7	2012	In liver and small intestine, CREB-H induces LPL coactivators, Apoa4, Apoa5, and Apoc2 that facilitate triglyceride clearance from plasma.	Triglycerides	103-115	apolipoprotein C2	Homo sapiens	81-86
22304839-8	2012	Furthermore, excess apoC-II has been associated with increased triglyceride-rich particles and alterations in HDL particle distribution, factors that may increase the risk of CVD.	Triglycerides	63-75	apolipoprotein C2	Homo sapiens	20-27
22304839-10	2012	A number of pharmaceutical interventions, including statins, fibrates, ezetimibe, nicotinic acid, and orlistat, have been shown to reduce the increased apoC-II concentrations.	Ezetimibe	71-80	apolipoprotein C2	Homo sapiens	152-159
22304839-10	2012	A number of pharmaceutical interventions, including statins, fibrates, ezetimibe, nicotinic acid, and orlistat, have been shown to reduce the increased apoC-II concentrations.	Niacin	82-96	apolipoprotein C2	Homo sapiens	152-159
22304839-10	2012	A number of pharmaceutical interventions, including statins, fibrates, ezetimibe, nicotinic acid, and orlistat, have been shown to reduce the increased apoC-II concentrations.	Orlistat	102-110	apolipoprotein C2	Homo sapiens	152-159
22304839-11	2012	An excess of apoC-II is associated with increased triglyceride-rich particles and alterations in HDL particle distribution.	Triglycerides	50-62	apolipoprotein C2	Homo sapiens	13-20
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
23119086-8	2012	Suggestive associations with fenofibrate response were observed for markers in or near PDE3A, MOSC1, FLJ36070, CETP, the APOE-APOC1-APOC4-APOC2, and CILP2.	Fenofibrate	29-40	apolipoprotein C2	Homo sapiens	138-143
23119086-9	2012	Finally, we present strong evidence for epistasis (P-value for interaction =  0.0006 in GOLDN, 0.05 in HyperTG) between rs10401969 near CILP2 and rs4420638 in the APOE-APOC1-APOC4-APOC2 cluster with total cholesterol response to fenofibrate.	Cholesterol	205-216	apolipoprotein C2	Homo sapiens	180-185
21146539-5	2011	Cross-linking results using single-cysteine substitution mutants are consistent with a parallel in-register structural model for apoC-II fibrils.	Cysteine	35-43	apolipoprotein C2	Homo sapiens	129-136
23119086-9	2012	Finally, we present strong evidence for epistasis (P-value for interaction =  0.0006 in GOLDN, 0.05 in HyperTG) between rs10401969 near CILP2 and rs4420638 in the APOE-APOC1-APOC4-APOC2 cluster with total cholesterol response to fenofibrate.	Fenofibrate	229-240	apolipoprotein C2	Homo sapiens	180-185
22808166-1	2012	Apolipoprotein CII (apoCII) is a specific activator of lipoprotein lipase and plays an important role in triglyceride metabolism.	Triglycerides	105-117	apolipoprotein C2	Homo sapiens	0-18
22808166-1	2012	Apolipoprotein CII (apoCII) is a specific activator of lipoprotein lipase and plays an important role in triglyceride metabolism.	Triglycerides	105-117	apolipoprotein C2	Homo sapiens	20-26
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
21985034-5	2011	Addition of submicellar NBD-lyso-12-PC increased the rate of fibril formation by apoC-II approximately 2-fold.	-12-pc	32-38	apolipoprotein C2	Homo sapiens	81-88
21985034-6	2011	Stopped flow kinetic analysis using fluorescence detection and low, non-fibril-forming concentrations of apoC-II indicated NBD-lyso-12-PC binds rapidly, on the millisecond time scale, followed by the slower formation of discrete apoC-II tetramers.	lyso-12-pc	127-137	apolipoprotein C2	Homo sapiens	105-112
21985034-6	2011	Stopped flow kinetic analysis using fluorescence detection and low, non-fibril-forming concentrations of apoC-II indicated NBD-lyso-12-PC binds rapidly, on the millisecond time scale, followed by the slower formation of discrete apoC-II tetramers.	lyso-12-pc	127-137	apolipoprotein C2	Homo sapiens	229-236
21985034-7	2011	Sedimentation velocity analysis showed NBD-lyso-12-PC binds to both apoC-II monomers and tetramers at approximately five sites per monomer with an average dissociation constant of approximately 10 muM.	nbd	39-42	apolipoprotein C2	Homo sapiens	68-75
21985034-7	2011	Sedimentation velocity analysis showed NBD-lyso-12-PC binds to both apoC-II monomers and tetramers at approximately five sites per monomer with an average dissociation constant of approximately 10 muM.	lyso-12-pc	43-53	apolipoprotein C2	Homo sapiens	68-75
21985034-8	2011	Mature apoC-II fibrils formed in the presence of NBD-lyso-12-PC were devoid of lipid, indicating a purely catalytic role for submicellar lipids in the activation of apoC-II fibril formation.	nbd-lyso-12-pc	49-63	apolipoprotein C2	Homo sapiens	7-14
21985034-8	2011	Mature apoC-II fibrils formed in the presence of NBD-lyso-12-PC were devoid of lipid, indicating a purely catalytic role for submicellar lipids in the activation of apoC-II fibril formation.	nbd-lyso-12-pc	49-63	apolipoprotein C2	Homo sapiens	165-172
21476595-6	2011	Circular dichroism and tryptophan fluorescence indicated that shear induced an irreversible change in apoC-II secondary structure.	Tryptophan	23-33	apolipoprotein C2	Homo sapiens	102-109
21476595-7	2011	Fluorescence resonance energy transfer experiments using the single tryptophan residue in apoC-II as the donor and covalently attached acceptors showed that shear flow increased the distance between the donor and acceptor molecules.	Tryptophan	68-78	apolipoprotein C2	Homo sapiens	90-97
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
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
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).	1,2-hexanoylphosphatidylcholine	186-216	apolipoprotein C2	Homo sapiens	129-136
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).	1,2-hexanoylphosphatidylcholine	218-222	apolipoprotein C2	Homo sapiens	129-136
20433849-7	2010	Global fitting of the concentration dependence of apoC-II fibril formation showed that DHPC increased the overall tetramerisation constant from 7.5 x 10(-13) to 1.2 x 10(-6) microM(-3) without significantly affecting the rate of fibril elongation, breaking, or joining.	1,2-hexanoylphosphatidylcholine	87-91	apolipoprotein C2	Homo sapiens	50-57
20433849-8	2010	Studies on the effect of DHPC on the free pool of apoC-II monomer and on fibril formation by cross-linked apoC-II dimers further demonstrate that DHPC affects nucleation but not elongation.	1,2-hexanoylphosphatidylcholine	146-150	apolipoprotein C2	Homo sapiens	50-57
20496878-9	2010	This finding complements our recent ThT fluorescence results, which revealed that the 4:1 lipid to peptide ratio is sufficient to cause fibril inhibition in apoC-II(60-70).	tetrahydrothiophene	36-39	apolipoprotein C2	Homo sapiens	157-164
20061429-9	2010	Fenofibrate significantly reduced plasma triglyceride, apolipoprotein (apo) CII, apo CIII, and apo E (all P < 0.01), with a modest increase in high-density lipoprotein-cholesterol (+12%; P = 0.06).	Fenofibrate	0-11	apolipoprotein C2	Homo sapiens	55-79
19729871-6	2009	CONCLUSION: The particle size of HDL become smaller with the increase of apoCII levels, implying that the efficiency of reverse cholesterol transport (RCT) was impaired and blocked the maturation of HDL.	Cholesterol	128-139	apolipoprotein C2	Homo sapiens	73-79
19780547-2	2009	For human apolipoprotein (apo) C-II the oxidation of methionine at position 60 inhibits fibril formation by the mature protein and by the core peptides apoC-II(56-76) and apoC-II(60-70).	Methionine	53-63	apolipoprotein C2	Homo sapiens	10-35
19780547-2	2009	For human apolipoprotein (apo) C-II the oxidation of methionine at position 60 inhibits fibril formation by the mature protein and by the core peptides apoC-II(56-76) and apoC-II(60-70).	Methionine	53-63	apolipoprotein C2	Homo sapiens	152-159
19780547-2	2009	For human apolipoprotein (apo) C-II the oxidation of methionine at position 60 inhibits fibril formation by the mature protein and by the core peptides apoC-II(56-76) and apoC-II(60-70).	Methionine	53-63	apolipoprotein C2	Homo sapiens	171-178
19780547-3	2009	To investigate the molecular nature of these effects, we carried out fully solvated, all-atom molecular dynamics simulations of the structural changes in apoC-II(56-76) associated with substitutions of oxidized methionine (Met ox) at position 60.	Methionine	211-221	apolipoprotein C2	Homo sapiens	154-161
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
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
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
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)).	dipentanoylphosphatidylcholine	99-129	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)).	dipentanoylphosphatidylcholine	99-129	apolipoprotein C2	Homo sapiens	274-281
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)).	1,2-hexanoylphosphatidylcholine	134-163	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)).	1,2-hexanoylphosphatidylcholine	134-163	apolipoprotein C2	Homo sapiens	274-281
18852267-2	2008	We have examined the effect of the short-chain phospholipids, dihexanoylphosphatidylcholine (DHPC) and dihexanoylphosphatidylserine (DHPS), on amyloid fibril formation by human apolipoprotein C-II (apoC-II).	dihexanoylphosphatidylserine	103-131	apolipoprotein C2	Homo sapiens	177-196
19302807-13	2009	Furthermore, LPL and ApoC-II secretion induced by fucoidan may be involved in regulating plasma triglyceride lowering clearance.	Triglycerides	96-108	apolipoprotein C2	Homo sapiens	21-28
19261998-7	2009	RESULTS: Additional to a marked reduction of LDL-C (-43%), atorvastatin treatment significantly decreased TG, RLP-C, apoC-II, apoC-III, and apoE by 27%, 49%, 25%, 15%, and 28%, respectively.	Atorvastatin	59-71	apolipoprotein C2	Homo sapiens	117-124
19252740-4	2009	Furthermore, cyclosporine treatment of the insulinoma-1E cell line resulted in remarkable reduction in HNF4alpha protein and INS1 as well as INS2 gene expression, while transcript expression of HNF4alpha, apolipoprotein C2, glycerolkinase, pyruvatekinase and aldolase B was repressed in treated Caco-2 cells.	Cyclosporine	13-25	apolipoprotein C2	Homo sapiens	205-222
18852267-2	2008	We have examined the effect of the short-chain phospholipids, dihexanoylphosphatidylcholine (DHPC) and dihexanoylphosphatidylserine (DHPS), on amyloid fibril formation by human apolipoprotein C-II (apoC-II).	1,2-hexanoylphosphatidylcholine	62-91	apolipoprotein C2	Homo sapiens	177-196
18852267-3	2008	Micellar DHPC and DHPS strongly inhibited apoC-II fibril formation, whereas submicellar levels of these lipids accelerated apoC-II fibril formation to a similar degree.	1,2-hexanoylphosphatidylcholine	9-13	apolipoprotein C2	Homo sapiens	42-49
18852267-3	2008	Micellar DHPC and DHPS strongly inhibited apoC-II fibril formation, whereas submicellar levels of these lipids accelerated apoC-II fibril formation to a similar degree.	dhps	18-22	apolipoprotein C2	Homo sapiens	42-49
18852267-6	2008	Emission data for fluorescently labeled apoC-II indicated that DHPC and DHPS stimulate the early formation and accumulation of oligomeric species.	1,2-hexanoylphosphatidylcholine	63-67	apolipoprotein C2	Homo sapiens	40-47
18852267-6	2008	Emission data for fluorescently labeled apoC-II indicated that DHPC and DHPS stimulate the early formation and accumulation of oligomeric species.	dhps	72-76	apolipoprotein C2	Homo sapiens	40-47
18450649-6	2008	In youths, evidence of association between rs9322331 and rs9340799 and apoC-II was stronger in males (P = 0.0036 and P = 0.0124) than in females (P > 0.05), whereas evidence of association with TG was stronger in females (P = 0.0030 and P = 0.0024) than in males (P > 0.05).	Triglycerides	197-199	apolipoprotein C2	Homo sapiens	71-78
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
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.	Methionine	105-115	apolipoprotein C2	Homo sapiens	200-219
18729385-5	2008	Upon oxidation of the methionine residues of apoC-II with hydrogen peroxide, fibril formation was inhibited.	Methionine	22-32	apolipoprotein C2	Homo sapiens	45-52
18729385-5	2008	Upon oxidation of the methionine residues of apoC-II with hydrogen peroxide, fibril formation was inhibited.	Hydrogen Peroxide	58-75	apolipoprotein C2	Homo sapiens	45-52
18729385-9	2008	The oxidation of preformed apoC-II fibrils caused their dissociation; however, mutants in which the Met-60 was substituted with a valine were protected from this peroxide-induced dissociation.	Peroxides	162-170	apolipoprotein C2	Homo sapiens	27-34
21291744-7	2008	Fenofibrate administration significantly reduced concentrations of ApoC-II and ApoC-III, whereas the combination of orlistat and fenofibrate had an additive effect on these apolipoproteins.	Fenofibrate	0-11	apolipoprotein C2	Homo sapiens	67-74
21291744-9	2008	Multivariate analysis showed that in O group"s baseline TG levels were independently positively correlated, whereas the baseline ApoC-II levels were negatively correlated with TG-lowering.	Triglycerides	176-178	apolipoprotein C2	Homo sapiens	129-136
21291744-12	2008	CONCLUSIONS: Orlistat-mediated TG-lowering is independently associated with baseline TG and ApoC-II levels.	Triglycerides	31-33	apolipoprotein C2	Homo sapiens	92-99
18344410-10	2008	Lipase activity detected in a 1.6 M NaCl-eluted fraction from a heparin-Sepharose column was enhanced by adding purified apoC-II in a dose-dependent manner, whereas that eluted by 0.8 M NaCl was not.	Sodium Chloride	36-40	apolipoprotein C2	Homo sapiens	121-128
18344410-10	2008	Lipase activity detected in a 1.6 M NaCl-eluted fraction from a heparin-Sepharose column was enhanced by adding purified apoC-II in a dose-dependent manner, whereas that eluted by 0.8 M NaCl was not.	Heparin	64-71	apolipoprotein C2	Homo sapiens	121-128
18344410-10	2008	Lipase activity detected in a 1.6 M NaCl-eluted fraction from a heparin-Sepharose column was enhanced by adding purified apoC-II in a dose-dependent manner, whereas that eluted by 0.8 M NaCl was not.	Sepharose	72-81	apolipoprotein C2	Homo sapiens	121-128
17217959-4	2007	Hydrogen-deuterium exchange and NMR spectroscopy of apoC-II fibrils revealed core regions between residues 19-37 and 57-74 with reduced amide proton exchange rates compared to monomeric apoC-II.	Amides	136-141	apolipoprotein C2	Homo sapiens	52-59
18453574-5	2008	In this study, we show that mature human macrophages differentiated in the presence of IL-4, and dexamethasone (M2(IL-4/GC)) but not M2(IL-4) responds to TGF-beta1 which induced a gene expression program comprising 111 genes including transcriptional/signaling regulators (ID3 and RGS1), immune modulators (ALOX5AP and IL-17 receptor B) and atherosclerosis-related genes (ALOX5AP, ORL1, APOC1, APOC2, and APOE).	Dexamethasone	97-110	apolipoprotein C2	Homo sapiens	394-399
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
17630380-5	2007	In vitro studies showed that SAP accelerated the formation of amyloid fibrils by purified apoC-II.	BENSULIDE	29-32	apolipoprotein C2	Homo sapiens	90-97
17630380-6	2007	Furthermore, SAP strongly inhibited the phagocytosis of apoC-II amyloid fibrils by primary macrophages and macrophage cell lines and blocked the resultant production of reactive oxygen species.	BENSULIDE	13-16	apolipoprotein C2	Homo sapiens	56-63
17630380-7	2007	The ability of SAP to accelerate apoC-II amyloid fibril formation and inhibit macrophage recognition of apoC-II fibrils suggests that SAP may modulate the inflammatory response to amyloid fibrils in atherosclerosis.	BENSULIDE	15-18	apolipoprotein C2	Homo sapiens	33-40
17630380-7	2007	The ability of SAP to accelerate apoC-II amyloid fibril formation and inhibit macrophage recognition of apoC-II fibrils suggests that SAP may modulate the inflammatory response to amyloid fibrils in atherosclerosis.	BENSULIDE	15-18	apolipoprotein C2	Homo sapiens	104-111
17429947-4	2007	High-performance liquid chromatography, mass spectrometry, and proteolysis of KA-modified apoC-II revealed that KA randomly modified six different lysine residues, with primarily one KA attached per apoC-II molecule.	Lysine	147-153	apolipoprotein C2	Homo sapiens	90-97
17429947-5	2007	Competition experiments showed that an aldehyde scavenging compound partially inhibited the ability of KA to hasten apoC-II fibril formation.	Aldehydes	39-47	apolipoprotein C2	Homo sapiens	116-123
17429947-9	2007	KA-mediated fibril formation by apoC-II was inhibited by the addition of the amine-containing compound hydralazine and the lipid-binding protein apoA-I.	Amines	77-82	apolipoprotein C2	Homo sapiens	32-39
17429947-9	2007	KA-mediated fibril formation by apoC-II was inhibited by the addition of the amine-containing compound hydralazine and the lipid-binding protein apoA-I.	Hydralazine	103-114	apolipoprotein C2	Homo sapiens	32-39
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
15533211-7	2004	But in 9 families with left and bilateral CL/P, two-point Zmax for APOC2[AC1/AC2] was 1.701 and multi-point Zmax at APOC2 locus was 1.909.	Phosphorus	45-46	apolipoprotein C2	Homo sapiens	67-72
16153625-7	2006	Substitution of residue 72 from a helix former leucine to a helix breaker, proline, is predicted to change the secondary structure of the C-terminal helix and subsequently alter the interaction between apo C-II and LPL.	Leucine	47-54	apolipoprotein C2	Homo sapiens	202-210
16153625-7	2006	Substitution of residue 72 from a helix former leucine to a helix breaker, proline, is predicted to change the secondary structure of the C-terminal helix and subsequently alter the interaction between apo C-II and LPL.	Proline	75-82	apolipoprotein C2	Homo sapiens	202-210
16782082-1	2006	BACKGROUND: Apolipoprotein C-II and apolipoprotein C-III play an important and complex role in plasma triglycerides metabolism, respectively, as inhibitor and activator of lipoprotein lipase.	Triglycerides	102-115	apolipoprotein C2	Homo sapiens	12-56
16314153-5	2006	Cleavage of apoC-II by MMP-14 markedly decreased LPL activity and would thus impair hydrolysis of triglycerides in plasma and transfer of fatty acids to tissues.	Triglycerides	98-111	apolipoprotein C2	Homo sapiens	12-19
16314153-5	2006	Cleavage of apoC-II by MMP-14 markedly decreased LPL activity and would thus impair hydrolysis of triglycerides in plasma and transfer of fatty acids to tissues.	Fatty Acids	138-149	apolipoprotein C2	Homo sapiens	12-19
15878877-8	2005	ApoA-V enrichment enhanced binding of apoC-II-deficient chylomicrons and VLDL to heparin-coated chips.	Heparin	81-88	apolipoprotein C2	Homo sapiens	38-45
15209504-0	2004	The structure and interactions of human apolipoprotein C-II in dodecyl phosphocholine.	dodecylphosphocholine	63-85	apolipoprotein C2	Homo sapiens	40-59
15559550-7	2004	Finally, the fact that hypertriglyceridaemia is more frequently observed after certain immunosuppressive treatments may be partly caused by changes in the synthesis and elimination of triglycerides involving lipoprotein lipase or some apolipoproteins which serve as its cofactors (apoCII or apoCIII).	Triglycerides	184-197	apolipoprotein C2	Homo sapiens	281-287
15222761-6	2004	Circular dichroism studies show that residues within the inner core of apoC-II, which compose a four-alpha-helix bundle when this apolipoprotein is associated with VLDL, are directly affected upon binding TCDD.	Polychlorinated Dibenzodioxins	205-209	apolipoprotein C2	Homo sapiens	71-78
15222761-7	2004	Fluorescence also indicates the specific interaction of Trp-48 within apoC-II upon TCDD binding.	Tryptophan	56-59	apolipoprotein C2	Homo sapiens	70-77
15222761-7	2004	Fluorescence also indicates the specific interaction of Trp-48 within apoC-II upon TCDD binding.	Polychlorinated Dibenzodioxins	83-87	apolipoprotein C2	Homo sapiens	70-77
15222761-8	2004	We found that the TCDD/apoC-II complex suffers a 5-fold reduction in its ability to bind lipoprotein lipase compared to untreated apoC-II.	Polychlorinated Dibenzodioxins	18-22	apolipoprotein C2	Homo sapiens	23-30
15222761-8	2004	We found that the TCDD/apoC-II complex suffers a 5-fold reduction in its ability to bind lipoprotein lipase compared to untreated apoC-II.	Polychlorinated Dibenzodioxins	18-22	apolipoprotein C2	Homo sapiens	130-137
15209504-1	2004	The structure of human apolipoprotein C-II (apoC-II) in the presence of dodecyl phosphocholine (DPC) micelles has been investigated by NMR spectroscopy.	dodecylphosphocholine	72-94	apolipoprotein C2	Homo sapiens	23-42
15209504-1	2004	The structure of human apolipoprotein C-II (apoC-II) in the presence of dodecyl phosphocholine (DPC) micelles has been investigated by NMR spectroscopy.	dodecylphosphocholine	72-94	apolipoprotein C2	Homo sapiens	44-51
15209504-1	2004	The structure of human apolipoprotein C-II (apoC-II) in the presence of dodecyl phosphocholine (DPC) micelles has been investigated by NMR spectroscopy.	dodecylphosphocholine	96-99	apolipoprotein C2	Homo sapiens	23-42
15209504-1	2004	The structure of human apolipoprotein C-II (apoC-II) in the presence of dodecyl phosphocholine (DPC) micelles has been investigated by NMR spectroscopy.	dodecylphosphocholine	96-99	apolipoprotein C2	Homo sapiens	44-51
15209504-2	2004	The resulting structural information is compared to that available for apoC-II in the presence of sodium dodecyl sulfate, revealing a high level of overall similarity but several significant differences.	Sodium Dodecyl Sulfate	98-120	apolipoprotein C2	Homo sapiens	71-78
15209504-6	2004	Furthermore, we observe specific contacts between lysine residues of apoC-II and protons near the phosphate group of DPC, consistent with the predictions of the so-called "snorkel hypothesis" of the structural basis for the apolipoprotein/lipid interaction (Segrest, J. P., Jackson, R. L., Morrisett, J. D., and Gotto, A. M., Jr. (1974) A molecular theory of lipid-protein interactions in the plasma lipoproteins, FEBS Lett 38, 247-258.).	Lysine	50-56	apolipoprotein C2	Homo sapiens	69-76
15209504-6	2004	Furthermore, we observe specific contacts between lysine residues of apoC-II and protons near the phosphate group of DPC, consistent with the predictions of the so-called "snorkel hypothesis" of the structural basis for the apolipoprotein/lipid interaction (Segrest, J. P., Jackson, R. L., Morrisett, J. D., and Gotto, A. M., Jr. (1974) A molecular theory of lipid-protein interactions in the plasma lipoproteins, FEBS Lett 38, 247-258.).	Phosphates	98-107	apolipoprotein C2	Homo sapiens	69-76
12855707-0	2003	1,1"-bis(anilino)-4-,4"-bis(naphtalene)-8,8"-disulfonate acts as an inhibitor of lipoprotein lipase and competes for binding with apolipoprotein CII.	1,1"-bis(anilino)-4-,4"-bis(naphtalene)-8,8"-disulfonate	0-56	apolipoprotein C2	Homo sapiens	130-148
15126543-5	2004	The women in the methyltestosterone plus esterified estrogen group had significant decreases in total triglycerides, apoCI, apoCII, apoCIII, apoE, and high density lipoprotein (HDL) cholesterol compared with those in the esterified estrogen group.	Methyltestosterone	17-35	apolipoprotein C2	Homo sapiens	124-130
14645070-0	2003	Phospholipid complexation and association with apolipoprotein C-II: insights from mass spectrometry.	Phospholipids	0-12	apolipoprotein C2	Homo sapiens	47-66
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
12855707-3	2003	ApoCII prevented the inhibition by bis-ANS, and was also able to restore the activity of inhibited LPL in a competitive manner, but only with triacylglycerols with acyl chains longer than three carbons.	5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)	35-42	apolipoprotein C2	Homo sapiens	0-6
12855707-3	2003	ApoCII prevented the inhibition by bis-ANS, and was also able to restore the activity of inhibited LPL in a competitive manner, but only with triacylglycerols with acyl chains longer than three carbons.	Triglycerides	142-158	apolipoprotein C2	Homo sapiens	0-6
12855707-3	2003	ApoCII prevented the inhibition by bis-ANS, and was also able to restore the activity of inhibited LPL in a competitive manner, but only with triacylglycerols with acyl chains longer than three carbons.	Carbon	194-201	apolipoprotein C2	Homo sapiens	0-6
24944394-11	2003	In group A, serum TG (P<0.001) and apolipoprotein (apo) C2, C3, and E (all P<0.01) concentrations decreased significantly with fenofibrate, and HDL-C and apo A1 and A2 increased significantly (all P<0.001).	Fenofibrate	133-144	apolipoprotein C2	Homo sapiens	38-61
12646232-5	2003	The apoCII/CIII ratio was higher in the DAG group than in the TAG group (p<0.01).	dag	40-43	apolipoprotein C2	Homo sapiens	4-10
12799125-2	2003	Several indices related to apolipoproteins (apo) CII and CIII blood concentration have been proposed to reflect TG metabolism more accurately than the blood level of TG.	Triglycerides	112-114	apolipoprotein C2	Homo sapiens	27-52
12585964-0	2003	Synergism between nuclear receptors bound to specific hormone response elements of the hepatic control region-1 and the proximal apolipoprotein C-II promoter mediate apolipoprotein C-II gene regulation by bile acids and retinoids.	Bile Acids and Salts	205-215	apolipoprotein C2	Homo sapiens	129-148
12585964-0	2003	Synergism between nuclear receptors bound to specific hormone response elements of the hepatic control region-1 and the proximal apolipoprotein C-II promoter mediate apolipoprotein C-II gene regulation by bile acids and retinoids.	Bile Acids and Salts	205-215	apolipoprotein C2	Homo sapiens	166-185
12585964-0	2003	Synergism between nuclear receptors bound to specific hormone response elements of the hepatic control region-1 and the proximal apolipoprotein C-II promoter mediate apolipoprotein C-II gene regulation by bile acids and retinoids.	Retinoids	220-229	apolipoprotein C2	Homo sapiens	129-148
12585964-0	2003	Synergism between nuclear receptors bound to specific hormone response elements of the hepatic control region-1 and the proximal apolipoprotein C-II promoter mediate apolipoprotein C-II gene regulation by bile acids and retinoids.	Retinoids	220-229	apolipoprotein C2	Homo sapiens	166-185
12585964-2	2003	In the present paper, we report that the HCR-1 selectively mediates the transactivation of the apoC-II promoter by chenodeoxycholic acid (CDCA) and 9- cis -retinoic acid.	Chenodeoxycholic Acid	115-136	apolipoprotein C2	Homo sapiens	95-102
12585964-2	2003	In the present paper, we report that the HCR-1 selectively mediates the transactivation of the apoC-II promoter by chenodeoxycholic acid (CDCA) and 9- cis -retinoic acid.	Chenodeoxycholic Acid	138-142	apolipoprotein C2	Homo sapiens	95-102
12585964-2	2003	In the present paper, we report that the HCR-1 selectively mediates the transactivation of the apoC-II promoter by chenodeoxycholic acid (CDCA) and 9- cis -retinoic acid.	Alitretinoin	148-169	apolipoprotein C2	Homo sapiens	95-102
12585964-3	2003	CDCA, which is a natural ligand of farnesoid X receptor alpha (FXRalpha), increases the steady-state apoC-II mRNA levels in HepG2 cells.	Chenodeoxycholic Acid	0-4	apolipoprotein C2	Homo sapiens	101-108
12585964-6	2003	Transactivation of the HCR-1/apoC-II promoter cluster by RXRalpha-FXRalpha heterodimers in the presence of CDCA was abolished by mutations either in the IR-1 HRE of the HCR-1 or in the thyroid HRE of the proximal apoC-II promoter, which binds RXRalpha-thyroid hormone receptor beta (T3Rbeta) heterodimers.	Chenodeoxycholic Acid	107-111	apolipoprotein C2	Homo sapiens	29-36
12585964-6	2003	Transactivation of the HCR-1/apoC-II promoter cluster by RXRalpha-FXRalpha heterodimers in the presence of CDCA was abolished by mutations either in the IR-1 HRE of the HCR-1 or in the thyroid HRE of the proximal apoC-II promoter, which binds RXRalpha-thyroid hormone receptor beta (T3Rbeta) heterodimers.	Chenodeoxycholic Acid	107-111	apolipoprotein C2	Homo sapiens	213-220
12585964-7	2003	The same mutations also abolished transactivation of the HCR-1/apoC-II promoter cluster by RXRalpha-T3Rbeta heterodimers in the presence of tri-iodothyronine.	Triiodothyronine	140-157	apolipoprotein C2	Homo sapiens	63-70
12585964-8	2003	The findings establish synergism between nuclear receptors bound to specific HREs of the proximal apoC-II promoter and the HCR-1, and suggest that this synergism mediates the induction of the HCR-1/apoC-II promoter cluster by bile acids and retinoids.	Bile Acids and Salts	226-236	apolipoprotein C2	Homo sapiens	98-105
12585964-8	2003	The findings establish synergism between nuclear receptors bound to specific HREs of the proximal apoC-II promoter and the HCR-1, and suggest that this synergism mediates the induction of the HCR-1/apoC-II promoter cluster by bile acids and retinoids.	Bile Acids and Salts	226-236	apolipoprotein C2	Homo sapiens	198-205
12585964-8	2003	The findings establish synergism between nuclear receptors bound to specific HREs of the proximal apoC-II promoter and the HCR-1, and suggest that this synergism mediates the induction of the HCR-1/apoC-II promoter cluster by bile acids and retinoids.	Retinoids	241-250	apolipoprotein C2	Homo sapiens	98-105
12585964-8	2003	The findings establish synergism between nuclear receptors bound to specific HREs of the proximal apoC-II promoter and the HCR-1, and suggest that this synergism mediates the induction of the HCR-1/apoC-II promoter cluster by bile acids and retinoids.	Retinoids	241-250	apolipoprotein C2	Homo sapiens	198-205
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
12079439-8	2002	The risk factor-adjusted odds ratio (OR) for CHD was 1.60 (95% CI: 1.31-1.94) per 1 mg/dl increment in Apo C(II), compared with a risk factor-adjusted OR of 1.05 (95% CI: 0.85-1.32) per 40 mg/dl increment in triglyceride concentration.	Triglycerides	208-220	apolipoprotein C2	Homo sapiens	103-112
12590574-2	2003	The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported.	Carbon	39-40	apolipoprotein C2	Homo sapiens	76-82
12590574-2	2003	The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported.	Nitrogen	47-48	apolipoprotein C2	Homo sapiens	76-82
12590574-2	2003	The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported.	Sodium Dodecyl Sulfate	99-121	apolipoprotein C2	Homo sapiens	76-82
12590574-2	2003	The three-dimensional structure of (13)C-, (15)N-enriched human full-length apoCII in complex with sodium dodecyl sulfate (SDS) micelles is reported.	Sodium Dodecyl Sulfate	123-126	apolipoprotein C2	Homo sapiens	76-82
12590574-6	2003	In addition, global constraints were derived from the fact that apoCII helices are attached to the surface of the SDS micelle and that the hydrophobic moments of each helix faces the interior of the micelle.	Sodium Dodecyl Sulfate	114-117	apolipoprotein C2	Homo sapiens	64-70
12590574-7	2003	These three categories of global constraints, together with the local classical NMR constraints, were sufficient to define the 3D structure of the apoCII-SDS micelle complex.	Sodium Dodecyl Sulfate	154-157	apolipoprotein C2	Homo sapiens	147-153
12678662-9	2003	APOCI I/I homozygotes have the highest level of triglycerides (p<0.003).	Triglycerides	48-61	apolipoprotein C2	Homo sapiens	0-7
12450397-0	2002	Cross-linking and amyloid formation by N- and C-terminal cysteine derivatives of human apolipoprotein C-II.	Cysteine	57-65	apolipoprotein C2	Homo sapiens	87-106
12450397-2	2002	Three derivatives of apoC-II were generated by inserting a cysteine residue on either the N-terminus (C(N)-apoC-II), C-terminus (C(C)-apoC-II), or both termini (C(N)C(C)-apoC-II).	Cysteine	59-67	apolipoprotein C2	Homo sapiens	21-28
12450397-4	2002	Under oxidizing conditions, C(N)- and C(N)C(C)-apoC-II formed a highly tangled network of fibrils, suggesting that the addition of an N-terminal cysteine to apoC-II promotes interfibril disulfide cross-links.	Cysteine	145-153	apolipoprotein C2	Homo sapiens	47-54
12450397-4	2002	Under oxidizing conditions, C(N)- and C(N)C(C)-apoC-II formed a highly tangled network of fibrils, suggesting that the addition of an N-terminal cysteine to apoC-II promotes interfibril disulfide cross-links.	Cysteine	145-153	apolipoprotein C2	Homo sapiens	157-164
12450397-4	2002	Under oxidizing conditions, C(N)- and C(N)C(C)-apoC-II formed a highly tangled network of fibrils, suggesting that the addition of an N-terminal cysteine to apoC-II promotes interfibril disulfide cross-links.	Disulfides	186-195	apolipoprotein C2	Homo sapiens	47-54
12450397-4	2002	Under oxidizing conditions, C(N)- and C(N)C(C)-apoC-II formed a highly tangled network of fibrils, suggesting that the addition of an N-terminal cysteine to apoC-II promotes interfibril disulfide cross-links.	Disulfides	186-195	apolipoprotein C2	Homo sapiens	157-164
11751863-1	2002	Human apolipoprotein C-II (apoC-II) slowly forms amyloid fibers in lipid-free solutions at physiological pH and salt concentrations (Hatters, D. M., MacPhee, C. E., Lawrence, L. J., Sawyer, W. H., and Howlett, G. J.	Salts	112-116	apolipoprotein C2	Homo sapiens	6-25
11751863-1	2002	Human apolipoprotein C-II (apoC-II) slowly forms amyloid fibers in lipid-free solutions at physiological pH and salt concentrations (Hatters, D. M., MacPhee, C. E., Lawrence, L. J., Sawyer, W. H., and Howlett, G. J.	Salts	112-116	apolipoprotein C2	Homo sapiens	27-34
12517327-12	2002	In both groups, triglycerides levels were positively correlated with Apo E (p=0.0429), Apo C2 (p=0.0045) and Apo C3 (p=0.0004) concentrations, but not with Apo E/Apo C2 ratio (p=0.760).	Triglycerides	16-29	apolipoprotein C2	Homo sapiens	87-93
11812765-7	2002	However, we found the strongest evidence for linkage of triglyceride levels to chromosome 19q13.2, very close to the ApoC2/ApoE/ApoC1/ApoC4 gene cluster (LOD 2.56) in the screening study; the LOD increased to 3.16 in the extended study.	Triglycerides	56-68	apolipoprotein C2	Homo sapiens	117-122
11719505-5	2002	Replacement of Tyr(63), Ile(66), Asp(69), or Gln(70) by alanine lowered the affinity for LPL and the catalytic activity of the LPL-apoCII complex.	Tyrosine	15-18	apolipoprotein C2	Homo sapiens	131-137
11719505-5	2002	Replacement of Tyr(63), Ile(66), Asp(69), or Gln(70) by alanine lowered the affinity for LPL and the catalytic activity of the LPL-apoCII complex.	Isoleucine	24-27	apolipoprotein C2	Homo sapiens	131-137
12517327-12	2002	In both groups, triglycerides levels were positively correlated with Apo E (p=0.0429), Apo C2 (p=0.0045) and Apo C3 (p=0.0004) concentrations, but not with Apo E/Apo C2 ratio (p=0.760).	Triglycerides	16-29	apolipoprotein C2	Homo sapiens	162-168
11311244-0	2001	Sub-micellar phospholipid accelerates amyloid formation by apolipoprotein C-II.	Phospholipids	13-25	apolipoprotein C2	Homo sapiens	59-78
11930616-2	2001	METHODS: The apoCII microsatellite DNA (TG) n(AG)m genotypes of 108 patients with CHD and 231 healthy persons were detected by using polymerase chain reaction (PCR) and high voltage denatured polyacrylamid gels electrophoresis.	polyacrylamide	192-205	apolipoprotein C2	Homo sapiens	13-19
11286640-4	2001	Although rare mutations in lipoprotein lipase (LPL), the major TG-hydrolyzing enzyme, and apo CII (APOC2), its essential activator, result in extremely high plasma TG levels, their low frequency means they have little impact upon TG levels in the general population.	Triglycerides	164-166	apolipoprotein C2	Homo sapiens	90-97
11286640-4	2001	Although rare mutations in lipoprotein lipase (LPL), the major TG-hydrolyzing enzyme, and apo CII (APOC2), its essential activator, result in extremely high plasma TG levels, their low frequency means they have little impact upon TG levels in the general population.	Triglycerides	164-166	apolipoprotein C2	Homo sapiens	99-104
11331005-0	2001	NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.	Sodium Dodecyl Sulfate	62-84	apolipoprotein C2	Homo sapiens	23-42
11331005-1	2001	The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein.	Sodium Dodecyl Sulfate	101-104	apolipoprotein C2	Homo sapiens	52-71
11331005-1	2001	The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein.	Sodium Dodecyl Sulfate	101-104	apolipoprotein C2	Homo sapiens	73-80
11331005-2	2001	Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism.	Sodium Dodecyl Sulfate	9-12	apolipoprotein C2	Homo sapiens	94-101
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
11311244-3	2001	We have investigated the effect of the short-chain phospholipid, dihexanoylphosphatidylcholine (DHPC) on amyloid formation by apoC-II.	1,2-hexanoylphosphatidylcholine	65-94	apolipoprotein C2	Homo sapiens	126-133
11311244-3	2001	We have investigated the effect of the short-chain phospholipid, dihexanoylphosphatidylcholine (DHPC) on amyloid formation by apoC-II.	1,2-hexanoylphosphatidylcholine	96-100	apolipoprotein C2	Homo sapiens	126-133
11311244-4	2001	The alpha-helical content of apoC-II increases in the presence of micellar DHPC (16 mM) and amyloid formation is inhibited.	1,2-hexanoylphosphatidylcholine	75-79	apolipoprotein C2	Homo sapiens	29-36
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.	Cholesterol	160-171	apolipoprotein C2	Homo sapiens	91-98
11310852-1	2001	Apolipoprotein C-II (apoC-II), which is known to activate lipoprotein lipase (LPL), was identified by ordered differential display (ODD)-polymerase chain reaction (PCR) as a cDNA fragment exhibiting a distinct increase in expression during 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced differentiation of promonocytic U937 cells into monocytes and macrophages.	Tetradecanoylphorbol Acetate	240-276	apolipoprotein C2	Homo sapiens	0-19
11310852-1	2001	Apolipoprotein C-II (apoC-II), which is known to activate lipoprotein lipase (LPL), was identified by ordered differential display (ODD)-polymerase chain reaction (PCR) as a cDNA fragment exhibiting a distinct increase in expression during 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced differentiation of promonocytic U937 cells into monocytes and macrophages.	Tetradecanoylphorbol Acetate	240-276	apolipoprotein C2	Homo sapiens	21-28
11310852-1	2001	Apolipoprotein C-II (apoC-II), which is known to activate lipoprotein lipase (LPL), was identified by ordered differential display (ODD)-polymerase chain reaction (PCR) as a cDNA fragment exhibiting a distinct increase in expression during 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced differentiation of promonocytic U937 cells into monocytes and macrophages.	Tetradecanoylphorbol Acetate	278-281	apolipoprotein C2	Homo sapiens	0-19
11310852-1	2001	Apolipoprotein C-II (apoC-II), which is known to activate lipoprotein lipase (LPL), was identified by ordered differential display (ODD)-polymerase chain reaction (PCR) as a cDNA fragment exhibiting a distinct increase in expression during 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced differentiation of promonocytic U937 cells into monocytes and macrophages.	Tetradecanoylphorbol Acetate	278-281	apolipoprotein C2	Homo sapiens	21-28
11310852-2	2001	The amount of apoC-II mRNA expression detectable in U937 cells significantly increased and reached a maximum 24-48 h after treatment with 32 nM TPA.	Tetradecanoylphorbol Acetate	144-147	apolipoprotein C2	Homo sapiens	14-21
11310852-5	2001	Although apoC-II mRNA expression was markedly up-regulated during the induced differentiation of HL-60 cells into monocytes and macrophages with 32 nM TPA, such expression was not induced during the differentiation of HL-60 cells into granulocytes with 1.25% dimethyl sulfoxide.	Tetradecanoylphorbol Acetate	151-154	apolipoprotein C2	Homo sapiens	9-16
11310852-5	2001	Although apoC-II mRNA expression was markedly up-regulated during the induced differentiation of HL-60 cells into monocytes and macrophages with 32 nM TPA, such expression was not induced during the differentiation of HL-60 cells into granulocytes with 1.25% dimethyl sulfoxide.	Dimethyl Sulfoxide	259-277	apolipoprotein C2	Homo sapiens	9-16
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
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.	Cholesterol	151-162	apolipoprotein C2	Homo sapiens	58-64
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
10903476-0	2000	Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine.	Sodium Dodecyl Sulfate	98-120	apolipoprotein C2	Homo sapiens	59-78
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.	Congo Red	172-181	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.	Congo Red	172-181	apolipoprotein C2	Homo sapiens	27-34
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
10889036-2	2000	ApoC-II was expressed and purified from Escherichia coli and rapidly exchanged from 5 M guanidine hydrochloride into 100 mM sodium phosphate, pH 7.4, to a final concentration of 0.3 mg/mL.	Guanidine	88-111	apolipoprotein C2	Homo sapiens	0-7
10889036-2	2000	ApoC-II was expressed and purified from Escherichia coli and rapidly exchanged from 5 M guanidine hydrochloride into 100 mM sodium phosphate, pH 7.4, to a final concentration of 0.3 mg/mL.	sodium phosphate	124-140	apolipoprotein C2	Homo sapiens	0-7
10889036-3	2000	This apoC-II was initially soluble, eluting as low molecular weight species in gel filtration experiments using Sephadex G-50.	sephadex	112-125	apolipoprotein C2	Homo sapiens	5-12
10889036-5	2000	Upon incubation for 24 h, apoC-II self-associated into high molecular weight aggregates as indicated by elution in the void volume of a Sephadex G-50 column, by rapid sedimentation in an analytical ultracentrifuge, and by increased light scattering.	sephadex	136-146	apolipoprotein C2	Homo sapiens	26-33
10903476-0	2000	Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine.	dodecylphosphocholine	125-146	apolipoprotein C2	Homo sapiens	59-78
10903476-3	2000	A comparison of alpha-proton secondary shifts and CD spectroscopic data indicates that the structure of apoC-II(44-79) is similar in the presence of dodecylphosphocholine and sodium dodecyl sulfate.	dodecylphosphocholine	149-170	apolipoprotein C2	Homo sapiens	104-111
10903476-3	2000	A comparison of alpha-proton secondary shifts and CD spectroscopic data indicates that the structure of apoC-II(44-79) is similar in the presence of dodecylphosphocholine and sodium dodecyl sulfate.	Sodium Dodecyl Sulfate	175-197	apolipoprotein C2	Homo sapiens	104-111
10903476-4	2000	The three-dimensional structure of apoC-II(44-79) in the presence of sodium dodecyl sulfate, determined by relaxation matrix calculations, contains two amphipathic helical domains formed by residues 50-58 and 67-75, separated by a non-helical linker centered at Tyr63.	Sodium Dodecyl Sulfate	69-91	apolipoprotein C2	Homo sapiens	35-42
10225669-0	1999	A thymidine to cytosine substitution for codon 26 of exon 3 of apolipoprotein C-II gene in a patient with apolipoprotein C-II deficiency.	Thymidine	2-11	apolipoprotein C2	Homo sapiens	63-82
10542105-3	1999	ApoC-II(19-39) forms approximately 60% alpha-helix upon binding to model egg yolk phosphatidylcholine small unilamellar vesicles.	Phosphatidylcholines	82-101	apolipoprotein C2	Homo sapiens	0-7
10225669-0	1999	A thymidine to cytosine substitution for codon 26 of exon 3 of apolipoprotein C-II gene in a patient with apolipoprotein C-II deficiency.	Cytosine	15-23	apolipoprotein C2	Homo sapiens	63-82
9714127-3	1998	We have identified several new heterozygotes for the catalytically inactive, nonsecreted HL variant S267F in the kindred that was originally ascertained because of hypertriglyceridemia due to the mutant, secreted, circulating apolipoprotein (apo) CII variant apo CII-T. Pairwise comparisons with family controls showed that only the plasma low density lipoprotein triglycerides (LDL TGs) were higher in 11 simple heterozygotes for HL S267F (P=0.002).	density lipoprotein triglycerides	344-377	apolipoprotein C2	Homo sapiens	226-250
9469593-6	1998	Interestingly, Chol did not affect the lipolysis rates even though it decreased TG solubility and apoC-II binding.	Cholesterol	15-19	apolipoprotein C2	Homo sapiens	98-105
9651383-8	1998	Transient cotransfection experiments showed that in the presence of T3, RXRalpha/T3Rbeta heterodimers transactivated the -205/+18 apoCII promoter 1.6- and 11-fold in HepG2 and COS-1 respectively.	carbonyl sulfide	176-179	apolipoprotein C2	Homo sapiens	130-136
10684052-4	1997	The results of the linear correlation showed that there was a positive correlation of apoC II, C III, E with TG, TC, LDL-C; of apoC II, C III with BMI; and of apoE with ages.	Thioguanine	109-111	apolipoprotein C2	Homo sapiens	86-93
9373166-3	1997	In contrast, the TFE-induced alpha-helical formation of two peptides derived from human apolipoproteins C-II and E was accompanied by the formation of discrete dimers and trimers, respectively.	Trifluoroethanol	17-20	apolipoprotein C2	Homo sapiens	88-114
10684052-4	1997	The results of the linear correlation showed that there was a positive correlation of apoC II, C III, E with TG, TC, LDL-C; of apoC II, C III with BMI; and of apoE with ages.	Technetium	113-115	apolipoprotein C2	Homo sapiens	86-93
10684052-4	1997	The results of the linear correlation showed that there was a positive correlation of apoC II, C III, E with TG, TC, LDL-C; of apoC II, C III with BMI; and of apoE with ages.	ldl-c	117-122	apolipoprotein C2	Homo sapiens	86-93
8765143-5	1996	Sequencing and mass spectrometric analyses indicated that the isolated recombinant ApoC-II contained predominantly (64%) the native form with threonine as the N-terminus, but also contained a minor (36%) molecular form of ApoC-II with an additional methionine at the N-terminus (Met-ApoC-II).	Threonine	142-151	apolipoprotein C2	Homo sapiens	83-90
9162750-6	1997	Large and small VLDL isolated from the NTG group were enriched with apoE and C-I, and cholesterol, but depleted of apoC-II in the postprandial state, whereas the apoC-III, triglyceride, and phospholipid contents were essentially unchanged.	Nitroglycerin	39-42	apolipoprotein C2	Homo sapiens	115-122
8879439-4	1996	Gemfibrozil significantly affected VLDL composition: protein increased 26%, molar ratio of apoE to apoB reduced 48%, apoC-II increased 19%, and apoC-III decreased 9%.	Gemfibrozil	0-11	apolipoprotein C2	Homo sapiens	117-124
8765143-5	1996	Sequencing and mass spectrometric analyses indicated that the isolated recombinant ApoC-II contained predominantly (64%) the native form with threonine as the N-terminus, but also contained a minor (36%) molecular form of ApoC-II with an additional methionine at the N-terminus (Met-ApoC-II).	Methionine	249-259	apolipoprotein C2	Homo sapiens	83-90
8767460-6	1996	Apo CII mRNA level increases after incubation of HepG2 cells with 10 microM forskolin within 2 hours as measured by northern blot analyses.	Colforsin	76-85	apolipoprotein C2	Homo sapiens	0-7
8647097-1	1996	The hydrolysis of triacylglycerols of chylomicrons and very low density lipoproteins by lipoprotein lipase (LPL) requires the presence of apolipoprotein (apo) CII as a cofactor.	Triglycerides	18-34	apolipoprotein C2	Homo sapiens	138-162
8647097-8	1996	A polyclonal antibody specific for apo CII impaired their ability to hydrolyse triacylglycerol emulsions.	Triglycerides	79-94	apolipoprotein C2	Homo sapiens	35-42
7815420-2	1994	ApoCII serves as cofactor for lipoprotein lipase (LPL) in triglyceride hydrolysis of chylomicrons and very low density lipoproteins.	Triglycerides	58-70	apolipoprotein C2	Homo sapiens	0-6
8847480-10	1995	Some of the fibrates, especially gemfibrozil also reduced plasma apoC-II levels, an effect that could contribute to the observed triglyceride-lowering effect.	Gemfibrozil	33-44	apolipoprotein C2	Homo sapiens	65-72
8847480-10	1995	Some of the fibrates, especially gemfibrozil also reduced plasma apoC-II levels, an effect that could contribute to the observed triglyceride-lowering effect.	Triglycerides	129-141	apolipoprotein C2	Homo sapiens	65-72
8847480-11	1995	In addition, the ratio of plasma apoE to plasma apoC-II plus apoC-III was strongly and inversely correlated with plasma triglyceride levels.	Triglycerides	120-132	apolipoprotein C2	Homo sapiens	48-55
8850383-6	1995	Simvastatin therapy further showed a significant decrease in apoC2 (p < 0.05), the apo C2/C3 ratio (p < 0.01), and apoE (p < 0.01), as well as a significant increase in Lp(a) plasma levels (p < 0.05).	Simvastatin	0-11	apolipoprotein C2	Homo sapiens	61-66
8350216-0	1993	Relationship between plasma triglycerides and apolipoprotein CII in infants during the first year of life.	Triglycerides	28-41	apolipoprotein C2	Homo sapiens	46-64
8020477-3	1994	Apolipoprotein CII increased the maximal inactivation rate constant by 1.8-fold in the presence of an emulsion of long-chain triacylglycerols, but had no effect in the presence of an emulsion of tributyrylglycerol.	Triglycerides	125-141	apolipoprotein C2	Homo sapiens	0-18
8301229-5	1993	Despite LPL acyl-chain specificity being obscured by the substrate binding effect of albumin, a systematic study of the lipolysis reaction under various assay conditions demonstrated that tributyroylglycerol represents the best substrate for LPL, and the preferential order of LPL catalysis for both the basal and apoC-II-activated activities is: C4 > C6 > C8 > C10 > C12 > C18:1.	tributyroylglycerol	188-207	apolipoprotein C2	Homo sapiens	314-321
8301229-7	1993	The synergistic effect of apoC-II and albumin resulted in the preferential activation of LPL for the hydrolysis of long-chain triacylglycerols.	Triglycerides	126-142	apolipoprotein C2	Homo sapiens	26-33
7923858-0	1994	The apolipoprotein C-II variant apoC-IILys19-->Thr is not associated with dyslipidemia in an affected kindred.	Threonine	50-53	apolipoprotein C2	Homo sapiens	4-23
7923858-1	1994	The rare apolipoprotein C-II (apoC-II) mutation, apoC-IILys19-->Thr, also known as apoC-II-v, has been found previously in association with hyperlipoproteinemia.	Threonine	67-70	apolipoprotein C2	Homo sapiens	9-28
7923858-1	1994	The rare apolipoprotein C-II (apoC-II) mutation, apoC-IILys19-->Thr, also known as apoC-II-v, has been found previously in association with hyperlipoproteinemia.	Threonine	67-70	apolipoprotein C2	Homo sapiens	30-37
7923858-1	1994	The rare apolipoprotein C-II (apoC-II) mutation, apoC-IILys19-->Thr, also known as apoC-II-v, has been found previously in association with hyperlipoproteinemia.	Threonine	67-70	apolipoprotein C2	Homo sapiens	49-56
8163669-2	1994	Human apoCII transgenic (HuCIITg) mice exhibited significant basal expression of the transgene (plasma apoCII level = 26.1 +/- 4 mg/dl) and showed further induction of transgene expression after treatment with beta-naphthoflavone.	beta-Naphthoflavone	210-229	apolipoprotein C2	Homo sapiens	6-12
8245727-2	1993	As the concentrations of acceptor triglycerides were increased, a greater fraction of both apoC-II and apoC-III shifted away from the native plasma lipoproteins to the artificial lipid emulsions.	Triglycerides	34-47	apolipoprotein C2	Homo sapiens	91-98
1555583-0	1992	Sequence specific 1H-NMR assignments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CII.	Hydrogen	18-20	apolipoprotein C2	Homo sapiens	106-124
8112221-1	1993	The three-dimensional structure of a synthetic fragment of human apolipoprotein CII (apo-CII) in 35%, 1,1,1,3,3,3-hexafluoro-2-propanol (HFP) has been determined on the basis of distance and intensity constraints derived from two-dimensional proton nuclear magnetic resonance measurements.	3-hexafluoro-2-propanol	112-135	apolipoprotein C2	Homo sapiens	65-83
8112221-1	1993	The three-dimensional structure of a synthetic fragment of human apolipoprotein CII (apo-CII) in 35%, 1,1,1,3,3,3-hexafluoro-2-propanol (HFP) has been determined on the basis of distance and intensity constraints derived from two-dimensional proton nuclear magnetic resonance measurements.	3-hexafluoro-2-propanol	112-135	apolipoprotein C2	Homo sapiens	85-92
1479292-9	1992	A nonsense mutation (Arg 19 Term) in the gene encoding apolipoprotein C-II (apoC-II), the cofactor of LPL, was found to underlie chylomicronemia in the sixth patient who had normal LPL but was apoC-II-deficient.	Arginine	21-24	apolipoprotein C2	Homo sapiens	55-74
1479292-9	1992	A nonsense mutation (Arg 19 Term) in the gene encoding apolipoprotein C-II (apoC-II), the cofactor of LPL, was found to underlie chylomicronemia in the sixth patient who had normal LPL but was apoC-II-deficient.	Arginine	21-24	apolipoprotein C2	Homo sapiens	76-83
1479292-9	1992	A nonsense mutation (Arg 19 Term) in the gene encoding apolipoprotein C-II (apoC-II), the cofactor of LPL, was found to underlie chylomicronemia in the sixth patient who had normal LPL but was apoC-II-deficient.	Arginine	21-24	apolipoprotein C2	Homo sapiens	193-200
1490289-6	1992	Allele-specific polymerase chain reaction (ASPCR) of the apoCII gene from the CII-S proband and her relatives showed unambiguous identification of heterozygous carriers of the CII-S protein.	cii-s	78-83	apolipoprotein C2	Homo sapiens	57-63
1490289-6	1992	Allele-specific polymerase chain reaction (ASPCR) of the apoCII gene from the CII-S proband and her relatives showed unambiguous identification of heterozygous carriers of the CII-S protein.	cii-s	176-181	apolipoprotein C2	Homo sapiens	57-63
1452137-7	1992	There was a significantly positive correlation between TC and apoAI, CII, CIII in HDL respectively, which indicated that apoCII and CIII were also associated with the alteration of HDL cholesterol.	Technetium	55-57	apolipoprotein C2	Homo sapiens	121-127
1452137-7	1992	There was a significantly positive correlation between TC and apoAI, CII, CIII in HDL respectively, which indicated that apoCII and CIII were also associated with the alteration of HDL cholesterol.	Cholesterol	185-196	apolipoprotein C2	Homo sapiens	121-127
1452137-8	1992	It is suggested that the elevated plasma VLDL-TG concentration in endogenous hypertriglyceridemia may induce abnormal redistribution of lipid and apolipoprotein among apoCII plasma lipoproteins, and and CIII may play an important role in these changes.	Triglycerides	46-48	apolipoprotein C2	Homo sapiens	167-173
1619390-8	1992	Characterization of these defects has provided new insights into the structure and function of apoC-II and LPL and established the important role that these two proteins play in normal triglyceride metabolism.	Triglycerides	185-197	apolipoprotein C2	Homo sapiens	95-102
1397477-8	1992	In BZF treated patients Apo CIII fell indicating a possible reduction of specific inhibition of lipoprotein lipase activity, while APX affected both Apo CII (+23%) and Apo CIII (-26%) and led to a 62% Apo CII/CIII ratio increase.	Bezafibrate	3-6	apolipoprotein C2	Homo sapiens	24-31
8405008-7	1993	The changes in TC, PL, LDL-C, apo B, apo CII and apo E were dependent upon the dose of pravastatin, as assessed by two-way analysis of variance.	Pravastatin	87-98	apolipoprotein C2	Homo sapiens	37-44
8327031-3	1993	It is furthermore characterized by a marked increase of apo CIII, which is disproportionate with respect to the increase of apo CII and the variation of apo E, in relation with an accumulation of Lp B-CIII (and also Lp B-E and Lp B-C-E for hemodialyzed patients) in the whole spectrum of low density lipoproteins.	leucylproline	196-198	apolipoprotein C2	Homo sapiens	56-63
1451339-6	1992	PTH and insulin showed a positive correlation with TG, the former being also inversely related to apo-CII/apo-CIII ratio.	Triglycerides	51-53	apolipoprotein C2	Homo sapiens	98-105
1804473-2	1991	This study was undertaken to investigate whether the capacity of high-density lipoprotein (HDL) for donating apoCII and apoCIII is influenced by the concentration of triglycerides (TGs) in plasma.	Triglycerides	166-179	apolipoprotein C2	Homo sapiens	109-115
1525253-11	1992	Furthermore, in male coronary heart disease patients a negative correlation was found between the concentrations of apolipoprotein CII/CIII-B and HDL-cholesterol.	Cholesterol	150-161	apolipoprotein C2	Homo sapiens	116-134
1569385-2	1992	Cleavage of heteroduplexes formed between normal and patient DNA strands with hydroxylamine and osmium tetroxide readily localized a mutation near base 2660 of the mutant apoC-II.	Hydroxylamine	78-91	apolipoprotein C2	Homo sapiens	171-178
1569385-2	1992	Cleavage of heteroduplexes formed between normal and patient DNA strands with hydroxylamine and osmium tetroxide readily localized a mutation near base 2660 of the mutant apoC-II.	Osmium Tetroxide	96-112	apolipoprotein C2	Homo sapiens	171-178
1782747-0	1991	An apolipoprotein CII mutation, CIILys19----Thr" identified in patients with hyperlipidemia.	Threonine	44-47	apolipoprotein C2	Homo sapiens	3-21
1753217-9	1991	ApoC-II and apoC-III isoforms differed by the oxidation of the two methionine residues in these proteins.	Methionine	67-77	apolipoprotein C2	Homo sapiens	0-7
1782747-2	1991	The structure of the apolipoprotein CII variant was determined to be the same as normal apolipoprotein CII except for replacement of the normal Lys at amino acid residue 19 by Thr (C2K19T).	Lysine	144-147	apolipoprotein C2	Homo sapiens	21-39
1782747-2	1991	The structure of the apolipoprotein CII variant was determined to be the same as normal apolipoprotein CII except for replacement of the normal Lys at amino acid residue 19 by Thr (C2K19T).	Threonine	176-179	apolipoprotein C2	Homo sapiens	21-39
1797121-6	1991	HDL cholesterol was not inversely correlated with triglycerides, and showed a highly positive correlation with apo E, apo CII and apo CIII, which did not correlate with HDL cholesterol in adults.	Cholesterol	4-15	apolipoprotein C2	Homo sapiens	118-125
2032722-5	1991	Two of the primer pairs (APOC2 and G6PD) detect CA dinucleotide repeat polymorphisms.	ca dinucleotide	48-63	apolipoprotein C2	Homo sapiens	25-30
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	Glutamine	44-47	apolipoprotein C2	Homo sapiens	169-176
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	Aspartic Acid	48-51	apolipoprotein C2	Homo sapiens	169-176
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	alanylhistidine	81-88	apolipoprotein C2	Homo sapiens	169-176
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	Valine	89-92	apolipoprotein C2	Homo sapiens	169-176
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	Proline	93-96	apolipoprotein C2	Homo sapiens	169-176
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	Glutamine	97-100	apolipoprotein C2	Homo sapiens	169-176
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	Glutamine	97-100	apolipoprotein C2	Homo sapiens	169-176
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	Aspartic Acid	105-108	apolipoprotein C2	Homo sapiens	169-176
2209608-6	1990	This was apparently due to cleavage of the -Gln-Asp- linkage in the sequence H2N-Ala-His-Val-Pro-Gln-Gln-Asp-Glu-, analogous to cleavages described for human apo AI and apo CII.	Glutamic Acid	109-112	apolipoprotein C2	Homo sapiens	169-176
2386483-1	1990	In this study we have prepared peptides of the C-terminal domain of apolipoprotein CII (ApoCII) by a solid-peptide-synthesis technique and demonstrated that the C-terminal tetrapeptide, Lys-Gly-Glu-Glu, represents an inhibitor of lipoprotein lipase.	lysylglycine	186-193	apolipoprotein C2	Homo sapiens	68-86
2094629-8	1990	Apo CII and CIII levels declined during the high CHO diet period but increased in normal subjects after intake of high fat died.	CAV protocol	49-52	apolipoprotein C2	Homo sapiens	0-7
2386483-1	1990	In this study we have prepared peptides of the C-terminal domain of apolipoprotein CII (ApoCII) by a solid-peptide-synthesis technique and demonstrated that the C-terminal tetrapeptide, Lys-Gly-Glu-Glu, represents an inhibitor of lipoprotein lipase.	Glutamic Acid	194-197	apolipoprotein C2	Homo sapiens	68-86
2386483-1	1990	In this study we have prepared peptides of the C-terminal domain of apolipoprotein CII (ApoCII) by a solid-peptide-synthesis technique and demonstrated that the C-terminal tetrapeptide, Lys-Gly-Glu-Glu, represents an inhibitor of lipoprotein lipase.	Glutamic Acid	194-197	apolipoprotein C2	Homo sapiens	88-94
2386483-1	1990	In this study we have prepared peptides of the C-terminal domain of apolipoprotein CII (ApoCII) by a solid-peptide-synthesis technique and demonstrated that the C-terminal tetrapeptide, Lys-Gly-Glu-Glu, represents an inhibitor of lipoprotein lipase.	lysylglycine	186-193	apolipoprotein C2	Homo sapiens	88-94
2386483-1	1990	In this study we have prepared peptides of the C-terminal domain of apolipoprotein CII (ApoCII) by a solid-peptide-synthesis technique and demonstrated that the C-terminal tetrapeptide, Lys-Gly-Glu-Glu, represents an inhibitor of lipoprotein lipase.	Glutamic Acid	198-201	apolipoprotein C2	Homo sapiens	68-86
2386483-1	1990	In this study we have prepared peptides of the C-terminal domain of apolipoprotein CII (ApoCII) by a solid-peptide-synthesis technique and demonstrated that the C-terminal tetrapeptide, Lys-Gly-Glu-Glu, represents an inhibitor of lipoprotein lipase.	Glutamic Acid	198-201	apolipoprotein C2	Homo sapiens	88-94
2592354-3	1989	Potential initiation of translation at the closest inframe methionine codon eliminates the entire signal peptide and the first 8 amino-terminal residues of apoC-II which would prevent apoC-II secretion into plasma.	Methionine	59-69	apolipoprotein C2	Homo sapiens	156-163
34458211-10	2021	Plasma levels of apoC-II and apoC-III were positively correlated with total cholesterol, triglyceride, and low-density lipoprotein (LDL) (all p < 0.001).	Cholesterol	76-87	apolipoprotein C2	Homo sapiens	17-24
34458211-10	2021	Plasma levels of apoC-II and apoC-III were positively correlated with total cholesterol, triglyceride, and low-density lipoprotein (LDL) (all p < 0.001).	Triglycerides	89-101	apolipoprotein C2	Homo sapiens	17-24
2307668-15	1990	We hypothesize that apoA-IV is required for efficient release of apoC-II from either HDL or VLDL, which then allows for LPL-mediated hydrolysis of TG in nascent chylomicrons.	Triglycerides	147-149	apolipoprotein C2	Homo sapiens	65-72
34462238-6	2021	RESULTS: After GH withdrawal, we found a reduction in fasting plasma TRL concentration (significant decrease in TRL-TG, TRL-cholesterol, TRL-apoB-100, TRL-apoC-III and TRL-apoC-II) but not in postprandial TRL response.	TRL	69-72	apolipoprotein C2	Homo sapiens	172-179
34459127-3	2021	As apolipoprotein C2 (APOC2) is a key activator of lipoprotein lipase for triglyceride metabolism, the exact mechanism of APOC2 remains largely unknown in GC.	Triglycerides	74-86	apolipoprotein C2	Homo sapiens	22-27
2592354-3	1989	Potential initiation of translation at the closest inframe methionine codon eliminates the entire signal peptide and the first 8 amino-terminal residues of apoC-II which would prevent apoC-II secretion into plasma.	Methionine	59-69	apolipoprotein C2	Homo sapiens	184-191
2592354-6	1989	We propose that in the apoC-IIParis gene, a mutation in the initiation methionine codon prevents the normal initiation of apolipoprotein synthesis and leads to a deficiency of apoC-II.	Methionine	71-81	apolipoprotein C2	Homo sapiens	23-30
3067732-2	1988	A full-length human apo CII cDNA clone has been constructed by completing the 5" end of an incomplete cDNA with a 44 bp long synthetic oligonucleotide.	Oligonucleotides	135-150	apolipoprotein C2	Homo sapiens	20-27
3198115-4	1988	This demonstrates that APOC2 and D19S19 are probably on the same side of DM.	dm	73-75	apolipoprotein C2	Homo sapiens	23-28
2600540-4	1989	In the present study, we have investigated the effect of the apoC-II polymorphism on quantitative serum levels of total cholesterol, total high density lipoprotein (HDL) cholesterol, cholesterol in high density lipoprotein subfractions, low density lipoprotein (LDL) cholesterol, and triglycerides (TG) in a sample of 368 unrelated Nigerian blacks.	Cholesterol	120-131	apolipoprotein C2	Homo sapiens	61-68
2600540-6	1989	In males, the effect of the APOC-II*2 allele was to lower the total serum cholesterol and LDL-cholesterol levels by 13.28 mg/dl and 10.55 mg/dl, respectively, relative to the common allele, APOC-II*1.	Cholesterol	74-85	apolipoprotein C2	Homo sapiens	28-35
2600540-6	1989	In males, the effect of the APOC-II*2 allele was to lower the total serum cholesterol and LDL-cholesterol levels by 13.28 mg/dl and 10.55 mg/dl, respectively, relative to the common allele, APOC-II*1.	Cholesterol	94-105	apolipoprotein C2	Homo sapiens	28-35
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
3411241-2	1988	We have determined concentrations of apoC-II and apoC-III in VLDL and HDL in subjects with a wide range of VLDL triglyceride and HDL cholesterol levels, and correlated these levels with fractional catabolic rates (FCR) of VLDL triglyceride and HDL apolipoprotein A-I (apoA-I).	Cholesterol	133-144	apolipoprotein C2	Homo sapiens	37-44
3411241-3	1988	Both apoC-II and apoC-III levels increased in VLDL as VLDL apolipoprotein B (apoB) and triglyceride levels rose.	Triglycerides	87-99	apolipoprotein C2	Homo sapiens	5-12
3411241-5	1988	Univariate analysis demonstrated that the FCR for VLDL triglyceride was inversely related to the ratio of apoC-III/apoC-II in VLDL (r = -0.58; P less than 0.05), although this relationship was not significant in a multivariate analysis.	Triglycerides	55-67	apolipoprotein C2	Homo sapiens	106-113
3131941-4	1988	In diabetic children serum selenium was significantly correlated with apolipoproteins A II and Apo C II, but not with any lipoprotein or lipid or any of their fractions.	Selenium	27-35	apolipoprotein C2	Homo sapiens	70-103
3680515-8	1987	Tryptic peptides of apoCIIs were identified that had retention times in reverse-phase high pressure liquid chromatography and amino acid compositions indistinguishable from that of residues 1 to 48 and 51 to 55 of normal apoCII.	Peptides	8-16	apolipoprotein C2	Homo sapiens	20-26
3680515-9	1987	The complete sequence of apoCIIs was deduced from a combination of the sequence analysis of tryptic peptides corresponding to residues 56 through 96 and the known sequence of the apoCII gene.	Peptides	100-108	apolipoprotein C2	Homo sapiens	25-31
3089635-0	1986	Substitution of Ser61----Gly61 in human apolipoprotein C-II does not alter its activation of lipoprotein lipase.	---gly61	22-30	apolipoprotein C2	Homo sapiens	40-59
3734708-4	1986	The apolipoprotein C-II concentrations in normolipaemic and hyperlipaemic plasma were not affected by delipidation, and increased only slightly after treatment with detergents or urea.	Urea	179-183	apolipoprotein C2	Homo sapiens	4-23
3474626-5	1987	Synthetic apoC-II was characterized by several complementary analytical techniques including amino acid composition, Edman phenylisothiocyanate degradation, polyacrylamide gel electrophoresis, and high-performance liquid chromatography.	edman phenylisothiocyanate	117-143	apolipoprotein C2	Homo sapiens	10-17
3474626-5	1987	Synthetic apoC-II was characterized by several complementary analytical techniques including amino acid composition, Edman phenylisothiocyanate degradation, polyacrylamide gel electrophoresis, and high-performance liquid chromatography.	polyacrylamide	157-171	apolipoprotein C2	Homo sapiens	10-17
3019390-3	1986	In contrast, apoC-II stimulates sphingomyelin hydrolysis by approximately 2.5-fold.	Sphingomyelins	32-45	apolipoprotein C2	Homo sapiens	13-20
3729948-1	1986	The effect of apolipoprotein C-II (apoC-II) and a synthetic fragment of apoC-II corresponding to residues 56-79 on the lipoprotein lipase (LpL) catalyzed hydrolysis of trioleoylglycerol in a monolayer of egg phosphatidylcholine and of dipalmitoylphosphatidylcholine vesicles was examined.	Triolein	168-185	apolipoprotein C2	Homo sapiens	14-33
3729948-1	1986	The effect of apolipoprotein C-II (apoC-II) and a synthetic fragment of apoC-II corresponding to residues 56-79 on the lipoprotein lipase (LpL) catalyzed hydrolysis of trioleoylglycerol in a monolayer of egg phosphatidylcholine and of dipalmitoylphosphatidylcholine vesicles was examined.	Triolein	168-185	apolipoprotein C2	Homo sapiens	35-42
3729948-1	1986	The effect of apolipoprotein C-II (apoC-II) and a synthetic fragment of apoC-II corresponding to residues 56-79 on the lipoprotein lipase (LpL) catalyzed hydrolysis of trioleoylglycerol in a monolayer of egg phosphatidylcholine and of dipalmitoylphosphatidylcholine vesicles was examined.	Triolein	168-185	apolipoprotein C2	Homo sapiens	72-79
3085084-7	1986	Testosterone alone has no effect on the rates of apolipoprotein secretion, but it does increase the concentration of estrogen required to maximally induce apoCII and apoAI by a mechanism that involves high-affinity androgen receptors.	Testosterone	0-12	apolipoprotein C2	Homo sapiens	155-161
3944267-11	1986	The reduction in plasma triglycerides after the injection of the synthetic apo C-II peptide persisted for 13-20 d. These results definitively established that the dyslipoproteinemia in this syndrome is due to a deficiency of normal apo C-II.	Triglycerides	24-37	apolipoprotein C2	Homo sapiens	75-83
3942763-1	1986	The effect of apolipoproteins C-II and C-III on the lipoprotein lipase-catalyzed hydrolysis of apolipoprotein C-II-deficient triacylglycerol-rich lipoproteins and particles of trioleoylglycerol stabilized with a phosphatidylcholine monolayer was investigated.	Phosphatidylcholines	212-231	apolipoprotein C2	Homo sapiens	95-114
3942763-3	1986	The effect of apolipoprotein C-II on lipoprotein lipase activity with apolipoprotein C-II-deficient lipoproteins as substrate was to decrease the apparent Michaelis constant (Kmapp) from 7.1 to 1.0 mM with minor changes on the apparent maximal velocity (Vmax) (22.2 mmol free fatty acid released/h per mg enzyme).	kmapp	175-180	apolipoprotein C2	Homo sapiens	14-33
3942763-3	1986	The effect of apolipoprotein C-II on lipoprotein lipase activity with apolipoprotein C-II-deficient lipoproteins as substrate was to decrease the apparent Michaelis constant (Kmapp) from 7.1 to 1.0 mM with minor changes on the apparent maximal velocity (Vmax) (22.2 mmol free fatty acid released/h per mg enzyme).	kmapp	175-180	apolipoprotein C2	Homo sapiens	70-89
3942763-3	1986	The effect of apolipoprotein C-II on lipoprotein lipase activity with apolipoprotein C-II-deficient lipoproteins as substrate was to decrease the apparent Michaelis constant (Kmapp) from 7.1 to 1.0 mM with minor changes on the apparent maximal velocity (Vmax) (22.2 mmol free fatty acid released/h per mg enzyme).	Fatty Acids, Nonesterified	271-286	apolipoprotein C2	Homo sapiens	14-33
3942763-3	1986	The effect of apolipoprotein C-II on lipoprotein lipase activity with apolipoprotein C-II-deficient lipoproteins as substrate was to decrease the apparent Michaelis constant (Kmapp) from 7.1 to 1.0 mM with minor changes on the apparent maximal velocity (Vmax) (22.2 mmol free fatty acid released/h per mg enzyme).	Fatty Acids, Nonesterified	271-286	apolipoprotein C2	Homo sapiens	70-89
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).	Fatty Acids, Nonesterified	83-98	apolipoprotein C2	Homo sapiens	13-32
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).	Triolein	166-183	apolipoprotein C2	Homo sapiens	13-32
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
3942763-4	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).	kmapp	229-234	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.	Triolein	108-125	apolipoprotein C2	Homo sapiens	12-31
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.	Triolein	108-125	apolipoprotein C2	Homo sapiens	168-187
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
3944267-11	1986	The reduction in plasma triglycerides after the injection of the synthetic apo C-II peptide persisted for 13-20 d. These results definitively established that the dyslipoproteinemia in this syndrome is due to a deficiency of normal apo C-II.	Triglycerides	24-37	apolipoprotein C2	Homo sapiens	232-240
4052389-0	1985	Interaction of lipoprotein lipase and apolipoprotein C-II with sonicated vesicles of 1,2-ditetradecylphosphatidylcholine: comparison of binding constants.	1,2-ditetradecylphosphatidylcholine	85-120	apolipoprotein C2	Homo sapiens	38-57
4058312-7	1985	In both groups, TRL apoC-II and apoC-III levels were positively correlated with the triglyceride level as it increased following the corn oil meal.	Triglycerides	84-96	apolipoprotein C2	Homo sapiens	20-27
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Phosphatidylcholines	125-144	apolipoprotein C2	Homo sapiens	71-90
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Phosphatidylcholines	125-144	apolipoprotein C2	Homo sapiens	92-99
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	146-191	apolipoprotein C2	Homo sapiens	71-90
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	146-191	apolipoprotein C2	Homo sapiens	92-99
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	c14-ether-pc	193-205	apolipoprotein C2	Homo sapiens	71-90
4052389-1	1985	The interaction of lipoprotein lipase (LpL) and its activator protein, apolipoprotein C-II (apoC-II), with a nonhydrolyzable phosphatidylcholine, 1,2-ditetradecyl-rac-glycero-3-phosphocholine (C14-ether-PC), was studied by fluorescence spectroscopy.	c14-ether-pc	193-205	apolipoprotein C2	Homo sapiens	92-99
4052389-4	1985	Addition of C14-ether-PC vesicles to apoC-II caused a 2.5-fold increase in intrinsic tryptophan fluorescence and a shift in emission maximum from 340 to 317 nm.	Tryptophan	85-95	apolipoprotein C2	Homo sapiens	37-44
4052389-6	1985	The dissociation constant (Kd) of the complex is 4.3 X 10(-8) M. For apoC-II, the stoichiometry of the complex is 18 PC per apoprotein, and the Kd is 3.0 X 10(-6) M. These data suggest that LpL binds more strongly than apoC-II to phosphatidylcholine interfaces.	Phosphatidylcholines	230-249	apolipoprotein C2	Homo sapiens	69-76
4052389-6	1985	The dissociation constant (Kd) of the complex is 4.3 X 10(-8) M. For apoC-II, the stoichiometry of the complex is 18 PC per apoprotein, and the Kd is 3.0 X 10(-6) M. These data suggest that LpL binds more strongly than apoC-II to phosphatidylcholine interfaces.	Phosphatidylcholines	230-249	apolipoprotein C2	Homo sapiens	219-226
3998153-6	1985	Addition of both lipase and its activator, apolipoprotein CII, resulted in a further increase in the cellular tocopherol content, but apolipoprotein CII alone had no effect.	Tocopherols	110-120	apolipoprotein C2	Homo sapiens	43-61
4051756-0	1985	Reversible increase of the apo CII/apo CIII-1 ratio in the very low density lipoproteins after procetofen treatment in hypertriglyceridemic patients.	Fenofibrate	95-105	apolipoprotein C2	Homo sapiens	27-34
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
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
3988735-3	1985	Both apo-C-II and apo-E produced enhanced lipolysis in comparison to unsupplemented emulsions, at appropriate enzyme densities on the heparin-Sepharose.	Heparin	134-141	apolipoprotein C2	Homo sapiens	5-13
3988735-3	1985	Both apo-C-II and apo-E produced enhanced lipolysis in comparison to unsupplemented emulsions, at appropriate enzyme densities on the heparin-Sepharose.	Sepharose	142-151	apolipoprotein C2	Homo sapiens	5-13
3970943-6	1985	In these circumstances the lipoprotein lipase-apolipoprotein C-II interaction is much tighter (Kd = (7-10) X 10(-9) M) and is insensitive to salt and heparin.	Salts	141-145	apolipoprotein C2	Homo sapiens	46-65
3970943-6	1985	In these circumstances the lipoprotein lipase-apolipoprotein C-II interaction is much tighter (Kd = (7-10) X 10(-9) M) and is insensitive to salt and heparin.	Heparin	150-157	apolipoprotein C2	Homo sapiens	46-65
3970943-7	1985	The mechanism of activation of the enzyme at low concentrations of apolipoprotein C-II is described by a kinetic model in which apolipoprotein C-II binds preferentially to the form of the enzyme which is associated with the triacylglycerol substrate.	Triglycerides	224-239	apolipoprotein C2	Homo sapiens	67-86
3970943-7	1985	The mechanism of activation of the enzyme at low concentrations of apolipoprotein C-II is described by a kinetic model in which apolipoprotein C-II binds preferentially to the form of the enzyme which is associated with the triacylglycerol substrate.	Triglycerides	224-239	apolipoprotein C2	Homo sapiens	128-147
2981868-2	1985	We have demonstrated that physiological concentrations of 17 beta-estradiol increase nuclear estrogen-specific binding sites in the human hepatoma cell line HepG2 7- to 10-fold and the rate of accumulation of secreted apolipoprotein C-II (apo-C-II), 2.5-fold (Tam, S-P., Archer, T. K., and Deeley, R. G. (1985) J. Biol.	Estradiol	58-75	apolipoprotein C2	Homo sapiens	218-237
2981868-2	1985	We have demonstrated that physiological concentrations of 17 beta-estradiol increase nuclear estrogen-specific binding sites in the human hepatoma cell line HepG2 7- to 10-fold and the rate of accumulation of secreted apolipoprotein C-II (apo-C-II), 2.5-fold (Tam, S-P., Archer, T. K., and Deeley, R. G. (1985) J. Biol.	Estradiol	58-75	apolipoprotein C2	Homo sapiens	239-247
2981868-6	1985	In order to define more precisely the mechanism by which estrogen influences apo-C-II production, we have synthesized a triacontanucleotide DNA probe that is complementary to apo-C-II mRNA.	triacontanucleotide	120-139	apolipoprotein C2	Homo sapiens	77-85
2981868-6	1985	In order to define more precisely the mechanism by which estrogen influences apo-C-II production, we have synthesized a triacontanucleotide DNA probe that is complementary to apo-C-II mRNA.	triacontanucleotide	120-139	apolipoprotein C2	Homo sapiens	175-183
6093789-1	1984	Apolipoprotein C-II (apoC-II), a 79 amino acid protein, is a cofactor for lipoprotein lipase, the enzyme which catalyzes the lipolysis of triglycerides on plasma chylomicrons and VLDL.	Triglycerides	138-151	apolipoprotein C2	Homo sapiens	0-19
6093789-1	1984	Apolipoprotein C-II (apoC-II), a 79 amino acid protein, is a cofactor for lipoprotein lipase, the enzyme which catalyzes the lipolysis of triglycerides on plasma chylomicrons and VLDL.	Triglycerides	138-151	apolipoprotein C2	Homo sapiens	21-28
6593704-3	1984	A 17-base-long synthetic oligonucleotide based on amino acid residues 5-10 of apoC-II was utilized as a hybridization probe to select recombinant plasmids containing the apoC-II sequence.	17-base-long synthetic oligonucleotide	2-40	apolipoprotein C2	Homo sapiens	78-85
6593704-3	1984	A 17-base-long synthetic oligonucleotide based on amino acid residues 5-10 of apoC-II was utilized as a hybridization probe to select recombinant plasmids containing the apoC-II sequence.	17-base-long synthetic oligonucleotide	2-40	apolipoprotein C2	Homo sapiens	170-177
6433686-5	1984	Controlling for Apo C-II reduced the black-white differences in total cholesterol 87%, LDL cholesterol 44%, VLDL cholesterol 83%, and total triglyceride 83%.	Cholesterol	70-81	apolipoprotein C2	Homo sapiens	16-24
6087809-1	1984	Human apolipoprotein (apo) C-II, a 79 amino acid protein, functions as a cofactor for lipoprotein lipase, the enzyme which catalyzes the hydrolysis of plasma triglycerides.	Triglycerides	158-171	apolipoprotein C2	Homo sapiens	6-31
6746620-0	1984	Effect of apolipoprotein C-II on the temperature dependence of lipoprotein lipase-catalyzed hydrolysis of phosphatidylcholines.	Phosphatidylcholines	106-126	apolipoprotein C2	Homo sapiens	10-29
6746620-9	1984	We propose that the apo-C-II-mediated increase in the rate of the lipoprotein lipase-catalyzed hydrolysis of phosphatidylcholine is associated with transfer of a fatty acyl chain of the substrate or product to a more hydrophobic environment within the transition state complex.	Phosphatidylcholines	109-128	apolipoprotein C2	Homo sapiens	20-28
6433686-5	1984	Controlling for Apo C-II reduced the black-white differences in total cholesterol 87%, LDL cholesterol 44%, VLDL cholesterol 83%, and total triglyceride 83%.	Cholesterol	91-102	apolipoprotein C2	Homo sapiens	16-24
6433686-5	1984	Controlling for Apo C-II reduced the black-white differences in total cholesterol 87%, LDL cholesterol 44%, VLDL cholesterol 83%, and total triglyceride 83%.	Cholesterol	91-102	apolipoprotein C2	Homo sapiens	16-24
6433686-5	1984	Controlling for Apo C-II reduced the black-white differences in total cholesterol 87%, LDL cholesterol 44%, VLDL cholesterol 83%, and total triglyceride 83%.	Triglycerides	140-152	apolipoprotein C2	Homo sapiens	16-24
6328478-1	1984	cDNA clones encoding human apolipoprotein CII (apo CII) were identified by screening an adult human liver cDNA library with a mixed oligonucleotide probe corresponding to all possible codons for apo CII amino acid 6-10.	Oligonucleotides	132-147	apolipoprotein C2	Homo sapiens	27-45
6733134-4	1984	Apolipoprotein C-II, the activator protein for lipoprotein lipase, enhanced the rate of the lipoprotein lipase-catalyzed hydrolysis of dimyristoylphosphatidylcholine for each substrate tested.	Dimyristoylphosphatidylcholine	135-165	apolipoprotein C2	Homo sapiens	0-19
6328478-1	1984	cDNA clones encoding human apolipoprotein CII (apo CII) were identified by screening an adult human liver cDNA library with a mixed oligonucleotide probe corresponding to all possible codons for apo CII amino acid 6-10.	Oligonucleotides	132-147	apolipoprotein C2	Homo sapiens	47-54
6328478-1	1984	cDNA clones encoding human apolipoprotein CII (apo CII) were identified by screening an adult human liver cDNA library with a mixed oligonucleotide probe corresponding to all possible codons for apo CII amino acid 6-10.	cii amino acid	199-213	apolipoprotein C2	Homo sapiens	27-45
6328478-1	1984	cDNA clones encoding human apolipoprotein CII (apo CII) were identified by screening an adult human liver cDNA library with a mixed oligonucleotide probe corresponding to all possible codons for apo CII amino acid 6-10.	cii amino acid	199-213	apolipoprotein C2	Homo sapiens	47-54
6328478-5	1984	The pCII -711 clone contains a 36-bp DNA sequence upstream from that specifying the NH2-terminal threonine which, when read in frame, specifies the amino acid sequence Leu-Val-Leu-Leu-Val-Leu-Gly-Phe-Glu-Val-Gln-Gly and may be part of an apo CII signal peptide.	Threonine	97-106	apolipoprotein C2	Homo sapiens	238-245
6328478-5	1984	The pCII -711 clone contains a 36-bp DNA sequence upstream from that specifying the NH2-terminal threonine which, when read in frame, specifies the amino acid sequence Leu-Val-Leu-Leu-Val-Leu-Gly-Phe-Glu-Val-Gln-Gly and may be part of an apo CII signal peptide.	Leucine	168-171	apolipoprotein C2	Homo sapiens	238-245
6328478-5	1984	The pCII -711 clone contains a 36-bp DNA sequence upstream from that specifying the NH2-terminal threonine which, when read in frame, specifies the amino acid sequence Leu-Val-Leu-Leu-Val-Leu-Gly-Phe-Glu-Val-Gln-Gly and may be part of an apo CII signal peptide.	Valine	172-175	apolipoprotein C2	Homo sapiens	238-245
6328478-5	1984	The pCII -711 clone contains a 36-bp DNA sequence upstream from that specifying the NH2-terminal threonine which, when read in frame, specifies the amino acid sequence Leu-Val-Leu-Leu-Val-Leu-Gly-Phe-Glu-Val-Gln-Gly and may be part of an apo CII signal peptide.	Leucine	176-179	apolipoprotein C2	Homo sapiens	238-245
6328478-5	1984	The pCII -711 clone contains a 36-bp DNA sequence upstream from that specifying the NH2-terminal threonine which, when read in frame, specifies the amino acid sequence Leu-Val-Leu-Leu-Val-Leu-Gly-Phe-Glu-Val-Gln-Gly and may be part of an apo CII signal peptide.	Valine	184-187	apolipoprotein C2	Homo sapiens	238-245
6706938-2	1984	Apo-C-II contains 79 amino acids with the following amino acid composition: Asp4, Asn1, Thr9, Ser9, Glu7, Gln7, Pro4, Gly2, Ala6, Val4, Met2, Ile1, Leu8, Tyr5, Phe2, Lys6, Arg1, Trp1.	Glycylglycine	118-122	apolipoprotein C2	Homo sapiens	0-8
6706938-3	1984	Cleavage of apo-C-II by cyanogen bromide produced three peptides designated as CB-1 (9 residues), CB-2 (51 residues), and CB-3 (19 residues).	Cyanogen Bromide	24-40	apolipoprotein C2	Homo sapiens	12-20
6706938-5	1984	The amino acid sequence of apo-C-II was obtained by the automated phenyl isothiocyanate degradation of intact apo-C-II and the peptides produced by cleavage of apo-C-II by cyanogen bromide and trypsin.	phenylisothiocyanate	66-87	apolipoprotein C2	Homo sapiens	27-35
6706938-5	1984	The amino acid sequence of apo-C-II was obtained by the automated phenyl isothiocyanate degradation of intact apo-C-II and the peptides produced by cleavage of apo-C-II by cyanogen bromide and trypsin.	Cyanogen Bromide	172-188	apolipoprotein C2	Homo sapiens	27-35
6847745-6	1983	Compared to the low Carb diet, the high Carb diet was associated with an increase in the size of HDL2 (116.0 +/- 1.8 vs. 109.1 +/- 1.8 A) and in the content (mean weight % +/- SEM) of apoE (2.81 +/- 0.71 vs. 1.79 +/- 0.49, P less than 0.01) and of apoC-II (1.73 +/- 0.09 vs. 1.11 +/- 0.12, P less than 0.01).	Carbohydrates	40-44	apolipoprotein C2	Homo sapiens	248-255
6872264-6	1983	These data suggest that in vivo a precursor-product relationship exists between triglyceride rich lipoproteins and LDL and HDL, and further stress the role of the lipoprotein lipase-apo C-II system in modulating these metabolic interconversions.	Triglycerides	80-92	apolipoprotein C2	Homo sapiens	182-190
7138621-14	1982	In heterozygotes, the partial deficiency of Apo C-II appears to result in a minor disturbance of the clearance of the triglycerides and Apo C-III rich particles but no marked changes in the concentrations of total lipids, lipoproteins and apolipoproteins in fasting plasma.	Triglycerides	118-131	apolipoprotein C2	Homo sapiens	44-52
6184366-2	1982	Polyacrylamide gel electrophoresis, isoelectric focusing and immunodiffusion tests of elastase-treated plasma lipoproteins revealed that apolipoprotein C-II and C-III polypeptides were more susceptible to elastase in free form than plasma <protein-id="114548">apolipoproteins (A-I, A-II, B, and E).	polyacrylamide	0-14	apolipoprotein C2	Homo sapiens	137-166
7130856-6	1982	Isocaloric changes in dietary carbohydrate and fat cause significant alterations in plasma levels of VLDL and HDL 2, the two major lipoproteins that transport apoC-III and apoC-II.	Carbohydrates	30-42	apolipoprotein C2	Homo sapiens	159-166
7104374-6	1982	The presence of apolipoprotein C-II, the apolipoprotein activator of lipoprotein lipase, partly reverses the inhibition of lipoprotein lipase by benzene boronic acid.	Benzene	145-152	apolipoprotein C2	Homo sapiens	16-87
7104374-6	1982	The presence of apolipoprotein C-II, the apolipoprotein activator of lipoprotein lipase, partly reverses the inhibition of lipoprotein lipase by benzene boronic acid.	Boronic Acids	153-165	apolipoprotein C2	Homo sapiens	16-87
7076797-9	1982	Gel isoelectric focusing of VLDL before and after nicotinic acid in types IIb and IV hyperlipidemia produced a significant increase in the VLDL ApoC-II component with simultaneous decreases in the total VLDL ApoC-III subspecies.	Niacin	50-64	apolipoprotein C2	Homo sapiens	144-151
7110307-6	1982	After extention of fructose intake to 28 days a decrease of VLDL-TG with concomitant fall of the relative ratio apo CIII1/apo CII in VLDL was found.	Fructose	19-27	apolipoprotein C2	Homo sapiens	112-119
7158381-6	1982	A correlation was found between triglyceride concentration in the VLDL fraction and the relative amounts of Apo CII and Apo CIII1.	Triglycerides	32-44	apolipoprotein C2	Homo sapiens	108-115
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
6459128-5	1981	The free form of heparan sulfate was found to be the activator which stimulated the lipoprotein lipase reaction in vitro in the presence of apolipoprotein CII.	Heparitin Sulfate	17-32	apolipoprotein C2	Homo sapiens	140-158
7410358-4	1980	The reversible denaturation of apoC-II by guanidinium chloride (GdmCl) proceeded in a sequential fashion.	Guanidine	42-62	apolipoprotein C2	Homo sapiens	31-38
7276752-3	1981	VLDLp binds apoC-II, and apoC-II associated with VLDLp markedly increases the rate of lipoprotein lipase-catalyzed hydrolysis of VLDLp-triglycerides.	Triglycerides	135-148	apolipoprotein C2	Homo sapiens	12-19
7276752-3	1981	VLDLp binds apoC-II, and apoC-II associated with VLDLp markedly increases the rate of lipoprotein lipase-catalyzed hydrolysis of VLDLp-triglycerides.	Triglycerides	135-148	apolipoprotein C2	Homo sapiens	25-32
7276752-5	1981	ApoC-II causes pH-dependent changes in both apparent Km and VmaX of LpL-catalyzed hydrolysis of VLDLp-triglycerides.	Triglycerides	102-115	apolipoprotein C2	Homo sapiens	0-7
7276752-10	1981	Based on a simple kinetic model, the data suggest that apoC-II favors direct interaction between enzyme and triglyceride within the lipoprotein particle, as well as subsequent catalytic turnover.	Triglycerides	108-120	apolipoprotein C2	Homo sapiens	55-62
7276737-5	1981	During perfusion, a 50% hydrolysis of the VLDL triacylglycerols was associated with the appearance of 11% of the apoC-II, 30% of the apoC-III, and 20% of apoE of the VLDL in HDL-like particles as isolated by agarose gel filtration.	Triglycerides	47-63	apolipoprotein C2	Homo sapiens	113-120
7410358-4	1980	The reversible denaturation of apoC-II by guanidinium chloride (GdmCl) proceeded in a sequential fashion.	Guanidine	64-69	apolipoprotein C2	Homo sapiens	31-38
7410358-6	1980	Based on tryptophan fluorescence quenching unfolded apoC-II was more permeable to penetration by small molecules than the self-associated protein.	Tryptophan	9-19	apolipoprotein C2	Homo sapiens	52-59
7382829-0	1980	Effects of short-term high carbohydrate, fat-free diet on plasma levels of Apo C-II and Apo C-III and on the Apo C subspecies in human plasma lipoproteins.	Carbohydrates	27-39	apolipoprotein C2	Homo sapiens	75-97
227736-0	1979	Apolipoprotein CII enhances hydrolysis of monoglycerides by lipoprotein lipase, but the effect is abolished by fatty acids.	Monoglycerides	42-56	apolipoprotein C2	Homo sapiens	0-18
227736-0	1979	Apolipoprotein CII enhances hydrolysis of monoglycerides by lipoprotein lipase, but the effect is abolished by fatty acids.	Fatty Acids	111-122	apolipoprotein C2	Homo sapiens	0-18
220493-8	1979	The regions of apoC-I and apoC-II that are involved in the activation of these enzymes have been localized with synthetic peptides.	Peptides	122-130	apolipoprotein C2	Homo sapiens	26-33
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
449689-0	1979	Availability of apolipoprotein CII in relation to the maximal removal capacity for an infused triglyceride emulsion in man.	Triglycerides	94-106	apolipoprotein C2	Homo sapiens	16-34
270715-4	1977	Cyanogen bromide fragments of apoC-II corresponding to residues 1--9 and 10--59 had little ability to activate LPL.	Cyanogen Bromide	0-16	apolipoprotein C2	Homo sapiens	30-37
213088-0	1978	Relative increase in apolipoprotein CII content of VLDL and chylomicrons in a case with massive type V hyperlipoproteinaemia by nicotinic acid treatment.	Niacin	128-142	apolipoprotein C2	Homo sapiens	21-39
271957-3	1977	ApoC-II contains a single arginine residue, permitting tryptic cleavage into two peptides after succinylation of the native protein.	Arginine	26-34	apolipoprotein C2	Homo sapiens	0-7
270715-5	1977	However, the COOH-terminal cyanogen bromide fragment corresponding to residues 60--78 increased hydrolysis 4-fold compared to an average of 9-fold activation for the same concentration of apoC-II.	Carbonic Acid	13-17	apolipoprotein C2	Homo sapiens	188-195
270715-5	1977	However, the COOH-terminal cyanogen bromide fragment corresponding to residues 60--78 increased hydrolysis 4-fold compared to an average of 9-fold activation for the same concentration of apoC-II.	Cyanogen Bromide	27-43	apolipoprotein C2	Homo sapiens	188-195
270715-7	1977	Addition of five residues produced a synthetic fragment 55--78 that enhanced the release of fatty acid 12-fold compared to 13-fold for intact apoC-II.	Fatty Acids	92-102	apolipoprotein C2	Homo sapiens	142-149
194919-3	1977	ApoCII was labeled with (125)I (chloramine-T) and monospecific antibody was raised in rabbits.	chloramine-T	32-44	apolipoprotein C2	Homo sapiens	0-6
194919-10	1977	Plasma triglycerides correlated inversely with the fraction of total apoCII in very low density lipoprotein (VLDL)-free plasma (r = -0.75, P &lt; 0.01).	Triglycerides	7-20	apolipoprotein C2	Homo sapiens	69-75
194919-14	1977	As plasma triglycerides and apoCII increase, apoCII is redistributed from high density lipoprotein to VLDL.	Triglycerides	10-23	apolipoprotein C2	Homo sapiens	45-51
189830-5	1977	Pig apoC-II had a molecular weight of approximately 10 000 as determined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate.	polyacrylamide	76-90	apolipoprotein C2	Homo sapiens	4-11
194244-3	1977	Chromatography on Bio-Gel P-30 in 25% formic acid of the cyanogen bromide digest of apoC-II yields three fragments designated as CNBr-I, -II, and -III.	formic acid	38-49	apolipoprotein C2	Homo sapiens	84-91
194244-3	1977	Chromatography on Bio-Gel P-30 in 25% formic acid of the cyanogen bromide digest of apoC-II yields three fragments designated as CNBr-I, -II, and -III.	Cyanogen Bromide	57-73	apolipoprotein C2	Homo sapiens	84-91
189830-5	1977	Pig apoC-II had a molecular weight of approximately 10 000 as determined by polyacrylamide gel electrophoresis in sodium dodecyl sulfate.	Sodium Dodecyl Sulfate	114-136	apolipoprotein C2	Homo sapiens	4-11
189830-7	1977	Treatment of pig apoC-II with carboxypeptidase indicated COOH-terminal serine.	Serine	71-77	apolipoprotein C2	Homo sapiens	17-24
8061-7	1976	The activity of the purified enzyme (i) had a pH optimum between 7.8 and 8.0; (ii) required serum for full enzymatic activity; apoC-II could be substituted for serum; (iii) was inhibited by by apoC-I in the presence of activated substrate; (iv) was markedly inhibited by NaCl; and (v) was stimulated by heparin.	Sodium Chloride	271-275	apolipoprotein C2	Homo sapiens	127-134
8061-7	1976	The activity of the purified enzyme (i) had a pH optimum between 7.8 and 8.0; (ii) required serum for full enzymatic activity; apoC-II could be substituted for serum; (iii) was inhibited by by apoC-I in the presence of activated substrate; (iv) was markedly inhibited by NaCl; and (v) was stimulated by heparin.	Heparin	303-310	apolipoprotein C2	Homo sapiens	127-134
33934596-1	2021	Triglyceride hydrolysis by lipoprotein lipase (LPL), regulated by apolipoproteins C-II (apoC-II) and C-III (apoC-III), is essential for maintaining normal lipid homeostasis.	Triglycerides	0-12	apolipoprotein C2	Homo sapiens	66-86
175240-18	1976	The proportion of ApoC-II relative to ApoC-III in VLDL increased in each subject on the carbohydrate diet (mean rise was 1.55-fold).	Carbohydrates	88-100	apolipoprotein C2	Homo sapiens	18-25
175240-22	1976	Proportions of ApoC-II rose in both density subfractions on carbohydrate diets.	Carbohydrates	60-72	apolipoprotein C2	Homo sapiens	15-22
178329-3	1976	There were highly significant correlations between the concentration of VLDL triglycerides and apo CII (r---0.92), apo CIII1 (r=+0.88) and the ratio apo CII/apo CIII1 (r= --0.94).	Triglycerides	77-90	apolipoprotein C2	Homo sapiens	95-102
178329-4	1976	It was suggested that the decreasing ratio apo CII/CIII1 with increasing triglyceride levels might cause a resistance to lipoprotein lipase and therefore a defect lipolysis of VLDL based upon a changed ratio apo CII/apo CII1 might be part of the pathogenesis of the hypertriglyceridaemia.	Triglycerides	73-85	apolipoprotein C2	Homo sapiens	43-50
178329-4	1976	It was suggested that the decreasing ratio apo CII/CIII1 with increasing triglyceride levels might cause a resistance to lipoprotein lipase and therefore a defect lipolysis of VLDL based upon a changed ratio apo CII/apo CII1 might be part of the pathogenesis of the hypertriglyceridaemia.	Triglycerides	73-85	apolipoprotein C2	Homo sapiens	208-215
33934596-1	2021	Triglyceride hydrolysis by lipoprotein lipase (LPL), regulated by apolipoproteins C-II (apoC-II) and C-III (apoC-III), is essential for maintaining normal lipid homeostasis.	Triglycerides	0-12	apolipoprotein C2	Homo sapiens	88-95
33934596-9	2021	These results suggest that both apoC-II and apoC-III transfer disproportionately from VLDL to HDL2 and the larger HDL3, and these transfers might be involved in individual triglyceride metabolism.	Triglycerides	172-184	apolipoprotein C2	Homo sapiens	32-39
32562799-1	2020	RATIONALE: ApoC2 is an important activator for lipoprotein lipase-mediated hydrolysis of triglyceride-rich plasma lipoproteins.	Triglycerides	89-101	apolipoprotein C2	Homo sapiens	11-16
32947088-12	2020	ApoC-II may be associated with lower cortical and DGM perfusion.	dgm	50-53	apolipoprotein C2	Homo sapiens	0-7
32802915-1	2020	Apolipoprotein C2 (ApoC2) is a key activator of lipoprotein lipase for plasma triglyceride metabolism.	Triglycerides	78-90	apolipoprotein C2	Homo sapiens	0-17
32793115-3	2020	At the genetic level, severely elevated triglyceride levels resulting from familial chylomicronemia syndrome (FCS) are caused by homozygous or biallelic loss-of-function variants in LPL, APOC2, APOA5, LMF1, and GPIHBP1 genes.	Triglycerides	40-52	apolipoprotein C2	Homo sapiens	187-192
32802915-1	2020	Apolipoprotein C2 (ApoC2) is a key activator of lipoprotein lipase for plasma triglyceride metabolism.	Triglycerides	78-90	apolipoprotein C2	Homo sapiens	19-24
32802915-5	2020	Administration of AAV-hApoC2 via jugular or orbital vein in adult and neonatal ApoC2-deficient hamsters, respectively, could prevent the neonatal death and effectively improve severe hypertriglyceridemia of ApoC2-deficient hamsters without side effects in a long-term manner.	CHEMBL2031461	18-21	apolipoprotein C2	Homo sapiens	23-28
32802915-5	2020	Administration of AAV-hApoC2 via jugular or orbital vein in adult and neonatal ApoC2-deficient hamsters, respectively, could prevent the neonatal death and effectively improve severe hypertriglyceridemia of ApoC2-deficient hamsters without side effects in a long-term manner.	CHEMBL2031461	18-21	apolipoprotein C2	Homo sapiens	79-84
32332429-1	2020	PURPOSE OF REVIEW: Apolipoprotein C-II (apoC-II) is a critical cofactor for the activation of lipoprotein lipase (LPL), a plasma enzyme that hydrolyzes triglycerides (TG) on TG-rich lipoproteins (TRL).	Triglycerides	152-165	apolipoprotein C2	Homo sapiens	19-38
31975384-5	2020	Luciferase reporter assay identified apolipoprotein C-II (APOC2) as a direct target of miR-4510.	C-II-a peptide	52-56	apolipoprotein C2	Homo sapiens	58-63
32332429-1	2020	PURPOSE OF REVIEW: Apolipoprotein C-II (apoC-II) is a critical cofactor for the activation of lipoprotein lipase (LPL), a plasma enzyme that hydrolyzes triglycerides (TG) on TG-rich lipoproteins (TRL).	Triglycerides	152-165	apolipoprotein C2	Homo sapiens	40-47
32332429-1	2020	PURPOSE OF REVIEW: Apolipoprotein C-II (apoC-II) is a critical cofactor for the activation of lipoprotein lipase (LPL), a plasma enzyme that hydrolyzes triglycerides (TG) on TG-rich lipoproteins (TRL).	Triglycerides	167-169	apolipoprotein C2	Homo sapiens	19-38
32332429-1	2020	PURPOSE OF REVIEW: Apolipoprotein C-II (apoC-II) is a critical cofactor for the activation of lipoprotein lipase (LPL), a plasma enzyme that hydrolyzes triglycerides (TG) on TG-rich lipoproteins (TRL).	Triglycerides	167-169	apolipoprotein C2	Homo sapiens	40-47
32332431-5	2020	Other approaches to reducing circulating triglyceride levels have been using an apoC2 mimetic and reducing apoC3.	Triglycerides	41-53	apolipoprotein C2	Homo sapiens	80-85
32194219-8	2020	Apo B-48, apo CII, and apo CIII levels decreased in the sitagliptin group, but not in the non-sitagliptin group.	Sitagliptin Phosphate	56-67	apolipoprotein C2	Homo sapiens	10-17
32281579-5	2020	High-density lipoprotein cholesterol (HDL-C) was slightly increased and very low-density lipoprotein cholesterol, non-HDL-C, ApoC-II, and ApoC-III were decreased with AZD0585 compared with placebo at the 12-week endpoint.	azd0585	167-174	apolipoprotein C2	Homo sapiens	125-132
31085627-6	2019	In MS patients, ApoC-II (all P <= 0.01) and ApoE (all P <= 0.01) changes were positively associated with all oxysterol levels.	Oxysterols	109-118	apolipoprotein C2	Homo sapiens	16-23
31935511-2	2020	In cardiovascular and cerebrovascular systems, the lipolytic activity of the LPL-ApoC2 complex is critical for the metabolism of triglyceride-rich lipoproteins and contributes to the pathogenesis of ischemic stroke (IS).	Triglycerides	129-141	apolipoprotein C2	Homo sapiens	81-86
31074692-8	2020	PS supplementation or fortification significantly changes Apo-E (r = -0.137, p nonlinearity = 0.006) and Apo-CIII (r = 1.26, p nonlinearity = 0.028) based on PS dosage (mg/d) and Apo-CIII (r = 3.34, p nonlinearity = 0.013) and Apo-CII (r = 1.09, p nonlinearity = 0.017) based on trial duration (weeks) in a nonlinear fashion.	ps	0-2	apolipoprotein C2	Homo sapiens	105-112
31074692-8	2020	PS supplementation or fortification significantly changes Apo-E (r = -0.137, p nonlinearity = 0.006) and Apo-CIII (r = 1.26, p nonlinearity = 0.028) based on PS dosage (mg/d) and Apo-CIII (r = 3.34, p nonlinearity = 0.013) and Apo-CII (r = 1.09, p nonlinearity = 0.017) based on trial duration (weeks) in a nonlinear fashion.	ps	158-160	apolipoprotein C2	Homo sapiens	105-112
31074692-14	2020	Phytosterols supplementation lowered atherogenic apo-lipoproteins (Apo-B and Apo-E) and increased anti-atherogenic apo-lipoproteins (Apo-AI, Apo-CII).	Phytosterols	0-12	apolipoprotein C2	Homo sapiens	141-148
30863636-2	2019	We previously reported that a human apoC-II mimetic peptide (C-II-a) decreased plasma TG in apoC-II mutant mice, as well as in apoE-knockout mice.	Triglycerides	86-88	apolipoprotein C2	Homo sapiens	36-43
30863636-2	2019	We previously reported that a human apoC-II mimetic peptide (C-II-a) decreased plasma TG in apoC-II mutant mice, as well as in apoE-knockout mice.	Triglycerides	86-88	apolipoprotein C2	Homo sapiens	92-99
30197986-9	2018	Proteomic analysis of Congo red-positive amyloid deposits detected large amounts of apolipoprotein CII (APOC2) protein.	Congo Red	22-31	apolipoprotein C2	Homo sapiens	84-102
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
29791776-5	2018	Structural analysis of rod-like apoC-II fibrils, using hydrogen-deuterium exchange and NMR analysis showed exchange protection consistent with a core cross-beta structure comprising the C-terminal 58-76 region.	Hydrogen	55-63	apolipoprotein C2	Homo sapiens	32-39
29791776-5	2018	Structural analysis of rod-like apoC-II fibrils, using hydrogen-deuterium exchange and NMR analysis showed exchange protection consistent with a core cross-beta structure comprising the C-terminal 58-76 region.	Deuterium	64-73	apolipoprotein C2	Homo sapiens	32-39
30197986-9	2018	Proteomic analysis of Congo red-positive amyloid deposits detected large amounts of apolipoprotein CII (APOC2) protein.	Congo Red	22-31	apolipoprotein C2	Homo sapiens	104-109
29100061-0	2017	Apolipoprotein C-II: New findings related to genetics, biochemistry, and role in triglyceride metabolism.	Triglycerides	81-93	apolipoprotein C2	Homo sapiens	0-19
29206648-7	2018	The positive relationship between plasma protein S levels and apoC-II, a key regulator of triglycerides hydrolysis, may contribute to the pathogenesis of increased concentrations of plasma protein S.	Triglycerides	90-103	apolipoprotein C2	Homo sapiens	62-69
29653812-6	2018	Vitamin D supplementation significantly increased total cholesterol, triglycerides, very-low-density lipoprotein (VLDL) triglycerides, low-density lipoprotein (LDL) triglycerides, high-density lipoprotein (HDL) triglycerides, apolipoprotein B (ApoB), LDL-ApoB, ApoCII, ApoCIII, phospholipids, and ApoE (P &lt; .05 for all).	Vitamin D	0-9	apolipoprotein C2	Homo sapiens	261-267
29100061-2	2017	ApoC-II plays a critical role in TRL metabolism by acting as a cofactor of lipoprotein lipase (LPL), the main enzyme that hydrolyses plasma triglycerides (TG) on TRL.	Triglycerides	140-153	apolipoprotein C2	Homo sapiens	0-7
29100061-2	2017	ApoC-II plays a critical role in TRL metabolism by acting as a cofactor of lipoprotein lipase (LPL), the main enzyme that hydrolyses plasma triglycerides (TG) on TRL.	Triglycerides	155-157	apolipoprotein C2	Homo sapiens	0-7
28107429-2	2017	Apolipoprotein C-II (APOC2) is an obligatory cofactor for lipoprotein lipase (LPL), the major enzyme catalyzing plasma triglyceride hydrolysis.	Triglycerides	119-131	apolipoprotein C2	Homo sapiens	0-19
28314859-2	2017	This study describes the mechanisms responsible for TG lowering by examining the kinetics of VLDL-TG, apoC-II, apoC-III, and apoE.	Triglycerides	52-54	apolipoprotein C2	Homo sapiens	102-109
28209220-10	2017	ApoC-III inhibition by volanesorsen reduced plasma levels of apoC-II, apoC-III, triacylglycerols, and diacylglycerols, and increased apoA-I, apoA-II, and apoM (all p &lt; 0.05 vs. placebo) without affecting apoB-100 (p = 0.73).	ISIS 304801	23-35	apolipoprotein C2	Homo sapiens	61-68
27297947-5	2017	Proteomic analysis of Congo red-positive deposits detected large amounts of the Apo-CII protein.	Congo Red	22-31	apolipoprotein C2	Homo sapiens	80-87
28107429-2	2017	Apolipoprotein C-II (APOC2) is an obligatory cofactor for lipoprotein lipase (LPL), the major enzyme catalyzing plasma triglyceride hydrolysis.	Triglycerides	119-131	apolipoprotein C2	Homo sapiens	21-26
27378472-5	2016	ApoC-II production rate (PR) was positively associated with VLDL1 -apoB-100 concentration, VLDL1 triglyceride concentration and VLDL1 triglyceride PR, while apoC-II fractional catabolic rate (FCR) was positively associated with VLDL1 triglyceride FCR (all P &lt; 0 05).	Triglycerides	97-109	apolipoprotein C2	Homo sapiens	0-7
27378472-5	2016	ApoC-II production rate (PR) was positively associated with VLDL1 -apoB-100 concentration, VLDL1 triglyceride concentration and VLDL1 triglyceride PR, while apoC-II fractional catabolic rate (FCR) was positively associated with VLDL1 triglyceride FCR (all P &lt; 0 05).	Triglycerides	134-146	apolipoprotein C2	Homo sapiens	0-7
27378472-4	2016	RESULTS: Plasma apoC-II and apoC-III concentrations were positively associated with the concentrations of plasma triglycerides, VLDL1 - and VLDL2 -apoB-100 and triglyceride (all P &lt; 0 05).	Triglycerides	113-126	apolipoprotein C2	Homo sapiens	16-23
27378472-5	2016	ApoC-II production rate (PR) was positively associated with VLDL1 -apoB-100 concentration, VLDL1 triglyceride concentration and VLDL1 triglyceride PR, while apoC-II fractional catabolic rate (FCR) was positively associated with VLDL1 triglyceride FCR (all P &lt; 0 05).	Triglycerides	134-146	apolipoprotein C2	Homo sapiens	0-7
27378472-4	2016	RESULTS: Plasma apoC-II and apoC-III concentrations were positively associated with the concentrations of plasma triglycerides, VLDL1 - and VLDL2 -apoB-100 and triglyceride (all P &lt; 0 05).	Triglycerides	113-125	apolipoprotein C2	Homo sapiens	16-23
27378472-9	2016	In multivariable analysis, including homoeostasis model assessment score, menopausal status and obesity, apoC-II concentration was significantly associated with plasma triglyceride, VLDL1 -apoB-100 and VLDL1 triglyceride concentrations and PR.	Triglycerides	168-180	apolipoprotein C2	Homo sapiens	105-112
27378472-9	2016	In multivariable analysis, including homoeostasis model assessment score, menopausal status and obesity, apoC-II concentration was significantly associated with plasma triglyceride, VLDL1 -apoB-100 and VLDL1 triglyceride concentrations and PR.	Triglycerides	208-220	apolipoprotein C2	Homo sapiens	105-112
26756862-1	2016	Lipoprotein lipase (LPL)-mediated triacylglycerol (TAG) hydrolysis in very low density lipoprotein (VLDL) is accompanied by the release of surface material containing phospholipids (PL), free cholesterol (FC) and apolipoproteins, E (apoE) and Cs (apoCII, apoCIII).	Triglycerides	34-49	apolipoprotein C2	Homo sapiens	247-253
27206937-3	2016	OBJECTIVE: To examine the genetic variants of 3 candidate genes known to influence triglyceride metabolism, LPL, APOC2, and APOA5, which encode lipoprotein lipase, apolipoprotein C-II, and apolipoprotein A-V, respectively, in a large group of Thai subjects with severe hypertriglyceridemia.	Triglycerides	83-95	apolipoprotein C2	Homo sapiens	164-183
27311794-5	2016	However, we found that fibril formation by K30D apoC-II proceeded readily at low pH and a higher salt or protein concentration.	Salts	97-101	apolipoprotein C2	Homo sapiens	48-55
26772541-10	2016	A novel mutation (c.86A &gt; CC) was identified on exon 3 [corrected] of the APOC2 gene, which converted the Asp [corrected] codon at position 29 into Ala, followed by a termination codon (TGA).	Aspartic Acid	109-112	apolipoprotein C2	Homo sapiens	77-82
26772541-10	2016	A novel mutation (c.86A &gt; CC) was identified on exon 3 [corrected] of the APOC2 gene, which converted the Asp [corrected] codon at position 29 into Ala, followed by a termination codon (TGA).	Alanine	151-154	apolipoprotein C2	Homo sapiens	77-82
26745412-0	2016	Apolipoprotein C-II Adopts Distinct Structures in Complex with Micellar and Submicellar Forms of the Amyloid-Inhibiting Lipid-Mimetic Dodecylphosphocholine.	dodecylphosphocholine	134-155	apolipoprotein C2	Homo sapiens	0-19
26196342-0	2015	Hydrogen/Deuterium Exchange and Molecular Dynamics Analysis of Amyloid Fibrils Formed by a D69K Charge-Pair Mutant of Human Apolipoprotein C-II.	Hydrogen	0-8	apolipoprotein C2	Homo sapiens	124-143
26745412-6	2016	Apolipoprotein C-II is a well-studied model system of systemic amyloid fibril formation, with a clear and well-defined pathway for fibril formation, where the effects of lipid interaction are characterized, particularly for the lipid mimetic dodecylphosphocholine.	dodecylphosphocholine	242-263	apolipoprotein C2	Homo sapiens	0-19
26280786-9	2015	Subgroup analysis revealed an increase in apoCII during treatment only in patients receiving LDV/SOF without RBV (+5.52 +- 11.92 mug/mL, P = 0.0007) but not in patients receiving LDV/SOF + RBV (P = 0.638).	Ribavirin	109-112	apolipoprotein C2	Homo sapiens	42-48
26280786-9	2015	Subgroup analysis revealed an increase in apoCII during treatment only in patients receiving LDV/SOF without RBV (+5.52 +- 11.92 mug/mL, P = 0.0007) but not in patients receiving LDV/SOF + RBV (P = 0.638).	Ribavirin	189-192	apolipoprotein C2	Homo sapiens	42-48
26196342-0	2015	Hydrogen/Deuterium Exchange and Molecular Dynamics Analysis of Amyloid Fibrils Formed by a D69K Charge-Pair Mutant of Human Apolipoprotein C-II.	Deuterium	9-18	apolipoprotein C2	Homo sapiens	124-143
26196342-6	2015	Fluorescence studies indicated more rapid fibril formation and less solvent accessibility of tryptophan (W26) in D69K apoC-II fibrils than in wild-type (WT) fibrils.	Tryptophan	93-103	apolipoprotein C2	Homo sapiens	118-125
23990203-7	2013	Triglyceride (TG)-metabolism-related markers (TG, remnant-like particle cholesterol, apolipoprotein [apo] B, apoC-2, and apoC-3) had decreased significantly.	Triglycerides	0-12	apolipoprotein C2	Homo sapiens	109-115
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
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
26026161-4	2015	ApoC-II adsorption to a triacylglycerol/water interface resulted in large increases in surface pressure.	Triglycerides	24-39	apolipoprotein C2	Homo sapiens	0-7
26026161-4	2015	ApoC-II adsorption to a triacylglycerol/water interface resulted in large increases in surface pressure.	Water	40-45	apolipoprotein C2	Homo sapiens	0-7
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
26026161-8	2015	We characterized apoC-II at phospholipid/triacylglycerol/water interfaces, which more closely mimic lipoprotein surfaces.	Triglycerides	41-56	apolipoprotein C2	Homo sapiens	17-24
26026161-8	2015	We characterized apoC-II at phospholipid/triacylglycerol/water interfaces, which more closely mimic lipoprotein surfaces.	Water	57-62	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
26021642-5	2015	Epigallocatechin gallate (EGCG), a green tea catechin, was an effective inhibitor of apoC-II fibril formation, and the antipsychotic drug, fluphenazine HCl, was a potent activator.	epigallocatechin gallate	0-24	apolipoprotein C2	Homo sapiens	85-92
26021642-5	2015	Epigallocatechin gallate (EGCG), a green tea catechin, was an effective inhibitor of apoC-II fibril formation, and the antipsychotic drug, fluphenazine HCl, was a potent activator.	epigallocatechin gallate	26-30	apolipoprotein C2	Homo sapiens	85-92
26021642-6	2015	Both EGCG and fluphenazine HCl exerted concentration-dependent effects on the rate of fibril formation, bound to apoC-II fibrils with high affinity, and competitively reduced thioflavin T binding.	epigallocatechin gallate	5-9	apolipoprotein C2	Homo sapiens	113-120
26021642-6	2015	Both EGCG and fluphenazine HCl exerted concentration-dependent effects on the rate of fibril formation, bound to apoC-II fibrils with high affinity, and competitively reduced thioflavin T binding.	Fluphenazine	14-30	apolipoprotein C2	Homo sapiens	113-120
26021642-8	2015	Fluphenazine HCl did not significantly alter the size distribution of fibrils, but it may induce the formation of a small population of rod-like fibrils that differ from the characteristic ribbon-like fibrils normally observed for apoC-II.	Fluphenazine	0-16	apolipoprotein C2	Homo sapiens	231-238
24120821-13	2013	Turbidimetric assay showed that the mean serum levels of ApoC-II tended to decrease in CD group when compared with NED group (P=.078).	Cadmium	87-89	apolipoprotein C2	Homo sapiens	57-64
24120821-13	2013	Turbidimetric assay showed that the mean serum levels of ApoC-II tended to decrease in CD group when compared with NED group (P=.078).	ned	115-118	apolipoprotein C2	Homo sapiens	57-64
24121499-8	2013	In the presence of the LPL activator protein apoC-II, more of apoC-I or apoC-III was needed for displacement of LPL from the lipid/water interface.	Water	131-136	apolipoprotein C2	Homo sapiens	45-52