PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30740857-3	2019	CLEC4M binds to mannose-containing glycans on FVIII.	Mannose	16-23	coagulation factor VIII	Homo sapiens	46-51	
32273875-0	2020	Removal of Mannose-Ending Glycan at Asn2118 Abrogates FVIII Presentation by Human Monocyte-Derived Dendritic Cells.	Mannose	11-18	coagulation factor VIII	Homo sapiens	54-59	
30740857-13	2019	CLEC4M binding to recombinant FVIII was dependent on mannose-exposed N-linked glycans.	Mannose	53-60	coagulation factor VIII	Homo sapiens	30-35	
30740857-16	2019	Conclusions These findings suggest that CLEC4M is a novel clearance receptor that interacts with mannose-exposed glycans on FVIII in the presence or absence of VWF.	Mannose	97-104	coagulation factor VIII	Homo sapiens	124-129	
20817851-1	2010	The LMAN1-MCFD2 (lectin, mannose binding 1/multiple coagulation factor deficiency protein 2) cargo receptor complex transports coagulation factors V (FV) and VIII (FVIII) from the endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC).	Mannose	25-32	coagulation factor VIII	Homo sapiens	164-169	
23852824-9	2013	FV and FVIII likely bind LMAN1 through the high-mannose N-linked glycans under the higher Ca2+ conditions in the ER and dissociate in the lower Ca2+ environment of the ER-Golgi intermediate compartment.	Mannose	48-55	coagulation factor VIII	Homo sapiens	7-12	
23709226-6	2013	Our structural data, combined with mutagenesis and in vitro binding assays, define the central mannose-binding site on LMAN1 and pinpoint histidine 178 and glycines 251/252 as critical residues for FV/FVIII binding.	Mannose	95-102	coagulation factor VIII	Homo sapiens	201-206	
14726380-4	2004	FVIII expression is limited by unstable mRNA, interaction with endoplasmic reticulum (ER) chaperones, and a requirement for facilitated ER to Golgi transport through interaction with the mannose-binding lectin LMAN1.	Mannose	187-194	coagulation factor VIII	Homo sapiens	0-5	
17502612-8	2007	We demonstrate that entry of FVIII into human dendritic cells (DC) leading to T cell activation, is mediated by mannose-terminating glycans on FVIII.	Mannose	112-119	coagulation factor VIII	Homo sapiens	29-34	
17502612-8	2007	We demonstrate that entry of FVIII into human dendritic cells (DC) leading to T cell activation, is mediated by mannose-terminating glycans on FVIII.	Mannose	112-119	coagulation factor VIII	Homo sapiens	143-148	
17502612-11	2007	The interaction between FVIII and CD206 was blocked by VWF, suggesting that, under physiological conditions, the intrinsic mannose-dependent immunogenicity of FVIII is quenched by endogenous immunochaperones.	Mannose	123-130	coagulation factor VIII	Homo sapiens	24-29	
17502612-11	2007	The interaction between FVIII and CD206 was blocked by VWF, suggesting that, under physiological conditions, the intrinsic mannose-dependent immunogenicity of FVIII is quenched by endogenous immunochaperones.	Mannose	123-130	coagulation factor VIII	Homo sapiens	159-164	
8054845-5	1994	The bound FVIII was specifically dissociated from LCA-Sepharose by methyl-alpha-D-mannopyranoside, and to a lesser extent by other monosaccharides such as D-glucose, methyl-alpha-D-glucopyranoside, D-mannose, and D-galactose.	Mannose	198-207	coagulation factor VIII	Homo sapiens	10-15	
14629470-5	2003	The interaction was mediated via high mannose-containing asparagine-linked oligosaccharides that are densely situated within the B domain of FVIII, as well as protein-protein interactions.	Mannose	38-45	coagulation factor VIII	Homo sapiens	141-146