PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
1504914-6	1992	Further, it was observed that LDL-B forms fewer precipitable complexes than normal LDL at 4 degrees C. However, at physiological temperature or with the addition of PEG, precipitation of the two LDLs was equal.	Polyethylene Glycols	165-168	component of oligomeric golgi complex 1	Homo sapiens	30-35
33960418-6	2021	Exome sequencing identified a homozygous COG1 variant (NM_018714.3: c.2665dup: p.(Arg889Profs*12)), which has been reported previously in one patient.	arg889profs	82-93	component of oligomeric golgi complex 1	Homo sapiens	41-45
7278649-7	1981	Low rates of LDL-B protein formation have been reported in other subjects with low LDL cholesterol concentrations and in the vegetarians presumably reflect the composite of several dietary factors.	Cholesterol	87-98	component of oligomeric golgi complex 1	Homo sapiens	13-18
3365983-4	1988	At baseline, ethanol consumption was found to be positively associated with triglycerides, HDL-C, and Apo-A1 and negatively associated with LDL-C/LDL-B.	Ethanol	13-20	component of oligomeric golgi complex 1	Homo sapiens	146-151
3930645-5	1985	The RID procedure at agarose concentrations of 1.5% to 2.5% can be used to estimate plasma LDL B protein levels in normotriglyceridemic subjects.	Sepharose	21-28	component of oligomeric golgi complex 1	Homo sapiens	91-96
172533-7	1975	By a deconvolution method, a quantitative description of the rate of entry of 131Ivldl-b into 131I-LDL-B was derived by analysis of 131I-LDL-B and 125I-ldl-b radioactivity in plasma.	131ivldl-b	78-88	component of oligomeric golgi complex 1	Homo sapiens	99-104
172533-7	1975	By a deconvolution method, a quantitative description of the rate of entry of 131Ivldl-b into 131I-LDL-B was derived by analysis of 131I-LDL-B and 125I-ldl-b radioactivity in plasma.	131ivldl-b	78-88	component of oligomeric golgi complex 1	Homo sapiens	137-142
16051600-8	2005	Only one or two of the seven Cog1- or Cog2-dependent Golgi membrane proteins called GEARs are also sensitive to Cog5 or Cog7 deficiency, indicating that the COG subunits play distinctive roles in controlling Golgi structure and function.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	157-160	component of oligomeric golgi complex 1	Homo sapiens	29-33
27385402-6	2016	We demonstrate that defective COG assembly or restriction of tethering complex disassembly by a covalent COG1-COG8 linkage is inhibitory to COG complex activity, supporting the model.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	30-33	component of oligomeric golgi complex 1	Homo sapiens	105-109
20972446-2	2010	To begin elucidating the molecular architecture of one well-studied example, the conserved oligomeric Golgi (COG) complex, we reconstituted its essential subunits (Cog1, Cog2, Cog3 and Cog4) and used single-particle electron microscopy to reveal a y-shaped structure with three flexible, highly extended legs.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	109-112	component of oligomeric golgi complex 1	Homo sapiens	164-168
17220172-0	2007	A new inborn error of glycosylation due to a Cog8 deficiency reveals a critical role for the Cog1-Cog8 interaction in COG complex formation.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	118-121	component of oligomeric golgi complex 1	Homo sapiens	93-97
17220172-5	2007	We showed that the molecular basis of this defect in N- and O-glycosylation is caused by the disruption of the Cog1-Cog8 interaction due to truncation.	Nitrogen	53-54	component of oligomeric golgi complex 1	Homo sapiens	111-115
20633274-2	2010	COG subunits are organized in two heterotrimeric groups, Cog2, -3, -4 and Cog5, -6, -7, linked by a dimeric group formed by Cog1 and Cog8.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	0-3	component of oligomeric golgi complex 1	Homo sapiens	124-128
16354716-4	2006	Here, we report that COGC-3 and COGC-1 proteins are homologous to mammalian COG-3/Sec34 and COG-1/ldlBp, respectively, two of the eight components of the conserved oligomeric Golgi (COG) complex required for Golgi function.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	21-24	component of oligomeric golgi complex 1	Homo sapiens	92-97
16354716-4	2006	Here, we report that COGC-3 and COGC-1 proteins are homologous to mammalian COG-3/Sec34 and COG-1/ldlBp, respectively, two of the eight components of the conserved oligomeric Golgi (COG) complex required for Golgi function.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	21-24	component of oligomeric golgi complex 1	Homo sapiens	98-103
11124340-9	2000	CONCLUSIONS: The LDL-B formula is a more reliable and accurate method than the LDL-F formula, especially at TG levels >2.26 mmol/L, although it underestimates LDL-C concentrations.	Triglycerides	108-110	component of oligomeric golgi complex 1	Homo sapiens	17-22
16020545-4	2005	The eight COG subunits (Cog1-8) are found to form two heterotrimeric subassemblies (Cog2/3/4 and Cog5/6/7) linked by a heterodimer composed of the remaining subunits (Cog1/8).	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	10-13	component of oligomeric golgi complex 1	Homo sapiens	24-30
16020545-4	2005	The eight COG subunits (Cog1-8) are found to form two heterotrimeric subassemblies (Cog2/3/4 and Cog5/6/7) linked by a heterodimer composed of the remaining subunits (Cog1/8).	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	10-13	component of oligomeric golgi complex 1	Homo sapiens	24-28
15047703-2	2004	The mammalian COG complex contains eight subunits: COG1/LdlBp, COG2/LdlCp, COG3/Sec34, COG4/Cod1, COG5/GTC-90/Cod4, COG6/Cod2, COG7, and COG8/Dor1.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	14-17	component of oligomeric golgi complex 1	Homo sapiens	51-55
15047703-2	2004	The mammalian COG complex contains eight subunits: COG1/LdlBp, COG2/LdlCp, COG3/Sec34, COG4/Cod1, COG5/GTC-90/Cod4, COG6/Cod2, COG7, and COG8/Dor1.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	14-17	component of oligomeric golgi complex 1	Homo sapiens	56-61
15004235-2	2004	Mammalian somatic cell mutants lacking the Cog1 (ldlB) or Cog2 (ldlC) subunits exhibit pleiotropic defects in Golgi-associated glycoprotein and glycolipid processing that suggest COG is involved in the localization, transport, and/or function of multiple Golgi processing proteins.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	179-182	component of oligomeric golgi complex 1	Homo sapiens	43-47
15004235-2	2004	Mammalian somatic cell mutants lacking the Cog1 (ldlB) or Cog2 (ldlC) subunits exhibit pleiotropic defects in Golgi-associated glycoprotein and glycolipid processing that suggest COG is involved in the localization, transport, and/or function of multiple Golgi processing proteins.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	179-182	component of oligomeric golgi complex 1	Homo sapiens	49-53
11980916-5	2002	EM of ldlB and ldlC mutants established that COG is required for normal Golgi morphology.	2,4-Diamino-6-[N-(2',5'-dimethoxybenzyl)-N-methylamino]quinazoline	45-48	component of oligomeric golgi complex 1	Homo sapiens	6-10