PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
8432690-2	1993	These two proteins, provisionally termed OCP1 and OCP2, were originally demonstrated by two-dimensional polyacrylamide gel electrophoresis; their presence at high concentrations in the inner ear sensory epithelia strongly suggests that OCP1 and OCP2 serve some important function in the ear.	polyacrylamide gels	104-122	F-box protein 2	Homo sapiens	41-45
8432690-2	1993	These two proteins, provisionally termed OCP1 and OCP2, were originally demonstrated by two-dimensional polyacrylamide gel electrophoresis; their presence at high concentrations in the inner ear sensory epithelia strongly suggests that OCP1 and OCP2 serve some important function in the ear.	polyacrylamide gels	104-122	F-box protein 2	Homo sapiens	236-240
31296343-8	2020	Generalized linear models were conducted to examine the associations of cholesterol intake with fasting blood glucose (FBG), 1-h post-load blood glucose (PBG) and 2-h PBG.	Cholesterol	72-83	F-box protein 2	Homo sapiens	96-126
35162013-6	2022	However, the compression and water level decrease tests showed that the system (R2 = 0.97142) had greater linearity with FBG2 (0.94123) and lower linearity with FBG1 (0.98271).	Water	29-34	F-box protein 2	Homo sapiens	161-165
32931479-5	2020	Moreover, we describe a role for the glycan binding F-box protein Fbxo2 in CNS lysophagy.	Polysaccharides	37-43	F-box protein 2	Homo sapiens	66-71
31296343-8	2020	Generalized linear models were conducted to examine the associations of cholesterol intake with fasting blood glucose (FBG), 1-h post-load blood glucose (PBG) and 2-h PBG.	pbg	154-157	F-box protein 2	Homo sapiens	96-126
30052682-5	2018	gB possesses seven N-glycosylation sites, and FBXO2 directly binds to these high-mannose moieties through its sugar-binding domain.	Mannose	81-88	F-box protein 2	Homo sapiens	46-51
30052682-4	2018	Here, we report the identification of F-box only protein 2 (FBXO2), an SCF ubiquitin ligase substrate adaptor that preferentially binds high-mannose glycans and attenuates EBV infectivity by targeting N-glycosylated gB for degradation.	high-mannose glycans	136-156	F-box protein 2	Homo sapiens	60-65
30052682-4	2018	Here, we report the identification of F-box only protein 2 (FBXO2), an SCF ubiquitin ligase substrate adaptor that preferentially binds high-mannose glycans and attenuates EBV infectivity by targeting N-glycosylated gB for degradation.	Nitrogen	201-202	F-box protein 2	Homo sapiens	60-65
30052682-4	2018	Here, we report the identification of F-box only protein 2 (FBXO2), an SCF ubiquitin ligase substrate adaptor that preferentially binds high-mannose glycans and attenuates EBV infectivity by targeting N-glycosylated gB for degradation.	gb	216-218	F-box protein 2	Homo sapiens	60-65
32306330-4	2020	Recently, the recombinant Fbs1 derivative protein has been developed as a tool for comprehensive enrichment of N-glycopeptides.	n-glycopeptides	111-126	F-box protein 2	Homo sapiens	26-30
30837888-5	2019	Two cytosolic F-box proteins, Fbs1 and Fbs2, recognize high-mannose glycans synthesized in the ER, and SCFFbs1 and SCFFbs2 ubiquitinate excess unassembled or misfolded glycoproteins in the ERAD pathway by recognizing the innermost glycans, which serve as signals for aberrant proteins.	mannose glycans	60-75	F-box protein 2	Homo sapiens	30-34
30837888-5	2019	Two cytosolic F-box proteins, Fbs1 and Fbs2, recognize high-mannose glycans synthesized in the ER, and SCFFbs1 and SCFFbs2 ubiquitinate excess unassembled or misfolded glycoproteins in the ERAD pathway by recognizing the innermost glycans, which serve as signals for aberrant proteins.	Polysaccharides	68-75	F-box protein 2	Homo sapiens	30-34
30052682-5	2018	gB possesses seven N-glycosylation sites, and FBXO2 directly binds to these high-mannose moieties through its sugar-binding domain.	Sugars	110-115	F-box protein 2	Homo sapiens	46-51
30052682-7	2018	Depletion of FBXO2 not only stabilizes gB but also promotes its transport from the ER to the PM, resulting in enhanced membrane fusion and viral entry.	gb	39-41	F-box protein 2	Homo sapiens	13-18
26460611-3	2015	Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27 recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no sugar-binding activity, despite the high sequence homology and conservation of the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3.	Sugars	137-142	F-box protein 2	Homo sapiens	13-17
29658560-1	2018	Tetrazines react with OCP-1 through a reverse electron demand Diels-Alder process to produce 3,6-disubstituted-1,2,4-diazaphosphinin-5-olates.	tetrazines	0-10	F-box protein 2	Homo sapiens	22-27
29658560-1	2018	Tetrazines react with OCP-1 through a reverse electron demand Diels-Alder process to produce 3,6-disubstituted-1,2,4-diazaphosphinin-5-olates.	3,6-disubstituted-1,2,4-diazaphosphinin-5-olates	93-141	F-box protein 2	Homo sapiens	22-27
26460611-7	2015	Structure-based mutational analysis shows that distinct hydrogen bond networks of four FBG3 loops, i.e., beta2-beta3, beta5-beta6, beta7-beta8, and beta9-beta10, prevent the formation of the carbohydrate-binding pocket shown in Fbs1.	Carbohydrates	191-203	F-box protein 2	Homo sapiens	228-232
26460611-3	2015	Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27 recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no sugar-binding activity, despite the high sequence homology and conservation of the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3.	Sugars	137-142	F-box protein 2	Homo sapiens	18-22
26460611-3	2015	Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27 recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no sugar-binding activity, despite the high sequence homology and conservation of the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3.	Oligosaccharides	243-258	F-box protein 2	Homo sapiens	13-17
26460611-3	2015	Among these, Fbs1/FBG1/FBXO2, Fbs2/FBG2/FBXO6, and Fbs3/FBG5/FBXO27 recognize the N-glycans of glycoproteins, whereas FBG3/FBXO44 has no sugar-binding activity, despite the high sequence homology and conservation of the residues necessary for oligosaccharide binding between Fbs1-3 and FBG3.	Oligosaccharides	243-258	F-box protein 2	Homo sapiens	18-22
26460611-6	2015	Although the overall structure of FBG3 is similar to that of Fbs1, the residues that form the Fbs1 carbohydrate-binding pocket failed to be superposed with the corresponding residues of FBG3.	Carbohydrates	99-111	F-box protein 2	Homo sapiens	94-98
26460611-7	2015	Structure-based mutational analysis shows that distinct hydrogen bond networks of four FBG3 loops, i.e., beta2-beta3, beta5-beta6, beta7-beta8, and beta9-beta10, prevent the formation of the carbohydrate-binding pocket shown in Fbs1.	Hydrogen	56-64	F-box protein 2	Homo sapiens	228-232
22227190-6	2012	Recently, FBXO2 was shown to bind high mannose glycans and participate in ERAD.	mannose glycans	39-54	F-box protein 2	Homo sapiens	10-15
22227190-7	2012	Using glycan arrays, immobilized glycoprotein pulldowns, and glycan competition assays we demonstrate that FBXO2 preferentially binds unfolded glycoproteins.	Polysaccharides	6-12	F-box protein 2	Homo sapiens	107-112
22227190-7	2012	Using glycan arrays, immobilized glycoprotein pulldowns, and glycan competition assays we demonstrate that FBXO2 preferentially binds unfolded glycoproteins.	Polysaccharides	61-67	F-box protein 2	Homo sapiens	107-112
22206664-6	2012	To learn more about the interactome of NgR2 we performed pull down experiments and were able to identify F-box protein that recognizes sugar chain 1 (Fbs1) as binding partner.	Sugars	135-140	F-box protein 2	Homo sapiens	150-154
17986767-5	2007	In this review, I focus on the in vivo function of Fbs1 and homologous proteins, novel intracellular oligosaccharide recognition molecules involved in the quality control system.	Oligosaccharides	101-116	F-box protein 2	Homo sapiens	51-55
15857118-0	2005	Thermodynamic analysis of interactions between N-linked sugar chains and F-box protein Fbs1.	n-linked sugar	47-61	F-box protein 2	Homo sapiens	87-91
15857118-3	2005	These analyses revealed that Man(3)GlcNAc(2) had the strongest affinity and the chitobiose and alpha1-->6 linked Man residue are necessary for Fbs1 to recognize a sugar.	Sugars	166-171	F-box protein 2	Homo sapiens	146-150
17592722-12	2007	It was shown that the presence of Fbs1 perturb the activity of PNGase toward high-mannose-type glycopeptides.	Mannose	82-89	F-box protein 2	Homo sapiens	34-38
17592722-12	2007	It was shown that the presence of Fbs1 perturb the activity of PNGase toward high-mannose-type glycopeptides.	Glycopeptides	95-108	F-box protein 2	Homo sapiens	34-38
17389369-3	2007	Fbs1/Fbx2, a member of the F-box protein family, recognizes high-mannose oligosaccharides.	high-mannose oligosaccharides	60-89	F-box protein 2	Homo sapiens	0-4
17389369-3	2007	Fbs1/Fbx2, a member of the F-box protein family, recognizes high-mannose oligosaccharides.	high-mannose oligosaccharides	60-89	F-box protein 2	Homo sapiens	5-9
17389369-4	2007	To elucidate the structural basis of SCF(Fbs1) function, we determined the crystal structures of the Skp1-Fbs1 complex and the sugar-binding domain (SBD) of the Fbs1-glycoprotein complex.	Sugars	127-132	F-box protein 2	Homo sapiens	41-45
17389369-7	2007	Comparison of two crystal structures of the Skp1-Fbs1 complex revealed the relative motion of a linker segment between the F-box and the SBD domains, which might underlie the ability of the complex to recognize different acceptor lysine residues for ubiquitination.	Lysine	230-236	F-box protein 2	Homo sapiens	49-53
17215248-2	2007	Similar to the ubiquitously expressed Fbs2, Fbs1 recognizes N-glycans at the innermost position as a signal for unfolded glycoproteins, probably in the endoplasmic reticulum-associated degradation pathway.	n-glycans	60-69	F-box protein 2	Homo sapiens	44-48
17215248-4	2007	The inefficient SCF complex formation of Fbs1 and the restricted presence of SCF(Fbs1) bound on the endoplasmic reticulum membrane were due to the short linker sequence between the F-box domain and the sugar-binding domain.	Sugars	202-207	F-box protein 2	Homo sapiens	41-45
17215248-4	2007	The inefficient SCF complex formation of Fbs1 and the restricted presence of SCF(Fbs1) bound on the endoplasmic reticulum membrane were due to the short linker sequence between the F-box domain and the sugar-binding domain.	Sugars	202-207	F-box protein 2	Homo sapiens	81-85
17116465-1	2006	N-glycans serve as a degradation signal by the SCF(Fbx2) ubiquitin ligase complex in the cytosol.	n-glycans	0-9	F-box protein 2	Homo sapiens	51-55
17116465-2	2006	Fbx2, an F-box protein, binds specifically to proteins attached with N-linked high-mannose type oligosaccharides, and subsequently contributes to ubiquitination of glycoproteins.	n-linked high-mannose type oligosaccharides	69-112	F-box protein 2	Homo sapiens	0-4
15809437-2	2005	Here, we determined that the F-box protein, Fbx2, bound to high-mannose glycans of the NR1 ectodomain.	mannose glycans	64-79	F-box protein 2	Homo sapiens	44-48
14990996-2	2004	Fbs1/Fbx2, a member of the F-box proteins, recognizes high-mannose oligosaccharides.	high-mannose oligosaccharides	54-83	F-box protein 2	Homo sapiens	0-4
14990996-2	2004	Fbs1/Fbx2, a member of the F-box proteins, recognizes high-mannose oligosaccharides.	high-mannose oligosaccharides	54-83	F-box protein 2	Homo sapiens	5-9
14990996-4	2004	Here we report the crystal structures of the sugar-binding domain (SBD) of Fbs1 alone and in complex with chitobiose.	Sugars	45-50	F-box protein 2	Homo sapiens	75-79
14990996-6	2004	The structure of the SBD-chitobiose complex includes hydrogen bonds between Fbs1 and chitobiose and insertion of the methyl group of chitobiose into a small hydrophobic pocket of Fbs1.	Hydrogen	53-61	F-box protein 2	Homo sapiens	76-80
14990996-8	2004	Considering that the innermost chitobiose moieties in N-glycans are usually involved in intramolecular interactions with the polypeptide moieties, we propose that Fbs1 interacts with the chitobiose in unfolded N-glycoprotein, pointing the protein moiety toward E2 for ubiquitination.	n-glycans	54-63	F-box protein 2	Homo sapiens	163-167
12140560-2	2002	Here we report that N-glycan serves as a signal for degradation by the Skp1-Cullin1-Fbx2-Roc1 (SCF(Fbx2)) ubiquitin ligase complex.	n-glycan	20-28	F-box protein 2	Homo sapiens	84-88
12140560-2	2002	Here we report that N-glycan serves as a signal for degradation by the Skp1-Cullin1-Fbx2-Roc1 (SCF(Fbx2)) ubiquitin ligase complex.	n-glycan	20-28	F-box protein 2	Homo sapiens	99-103