PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20735720-7	2010	Responses are prevented by N-acetyl-D-glucosamine (GN), which blocks GPIbalpha-clustering, and by O-sialoglycoprotein endopeptidase, which removes extracellular GPIbalpha.	Acetylglucosamine	27-49	glycoprotein Ib platelet subunit alpha	Homo sapiens	69-78	
22733027-4	2012	RESULTS: Cold storage induced deglycosylation of glycoprotein Ibalpha ectodomain, exposing N-acetyl-D-glucosamine residues, which sequestered with GM1 gangliosides in lipid rafts.	Acetylglucosamine	91-113	glycoprotein Ib platelet subunit alpha	Homo sapiens	49-69	
20735720-7	2010	Responses are prevented by N-acetyl-D-glucosamine (GN), which blocks GPIbalpha-clustering, and by O-sialoglycoprotein endopeptidase, which removes extracellular GPIbalpha.	Acetylglucosamine	51-53	glycoprotein Ib platelet subunit alpha	Homo sapiens	69-78	
20735720-7	2010	Responses are prevented by N-acetyl-D-glucosamine (GN), which blocks GPIbalpha-clustering, and by O-sialoglycoprotein endopeptidase, which removes extracellular GPIbalpha.	Acetylglucosamine	51-53	glycoprotein Ib platelet subunit alpha	Homo sapiens	161-170	
17319824-2	2007	Blocking beta-N-acetylglucosamine (beta-GlcNAc) residues of glycoprotein Ibalpha (GPIbalpha) with galactose prevents binding of refrigerated human and mouse PLTs to macrophages and prolongs the circulation times of refrigerated mouse PLTs.	Acetylglucosamine	9-33	glycoprotein Ib platelet subunit alpha	Homo sapiens	60-80	
17319824-2	2007	Blocking beta-N-acetylglucosamine (beta-GlcNAc) residues of glycoprotein Ibalpha (GPIbalpha) with galactose prevents binding of refrigerated human and mouse PLTs to macrophages and prolongs the circulation times of refrigerated mouse PLTs.	Acetylglucosamine	9-33	glycoprotein Ib platelet subunit alpha	Homo sapiens	82-91	
17319824-2	2007	Blocking beta-N-acetylglucosamine (beta-GlcNAc) residues of glycoprotein Ibalpha (GPIbalpha) with galactose prevents binding of refrigerated human and mouse PLTs to macrophages and prolongs the circulation times of refrigerated mouse PLTs.	Acetylglucosamine	35-46	glycoprotein Ib platelet subunit alpha	Homo sapiens	60-80	
17319824-2	2007	Blocking beta-N-acetylglucosamine (beta-GlcNAc) residues of glycoprotein Ibalpha (GPIbalpha) with galactose prevents binding of refrigerated human and mouse PLTs to macrophages and prolongs the circulation times of refrigerated mouse PLTs.	Acetylglucosamine	35-46	glycoprotein Ib platelet subunit alpha	Homo sapiens	82-91	
17176320-6	2006	N-Acetylglucosamine, known to interfere with macrophage recognition of GPIbalpha clusters, restored normal AN51-PE binding to cold-stored PLTs and suppressed phagocytosis.	Acetylglucosamine	0-19	glycoprotein Ib platelet subunit alpha	Homo sapiens	71-80	
16232387-7	2005	That is, they show that exposed, terminal, beta-linked N-acetylglucosamine (beta-GlcNAc) residues on clustered GPIbalpha are recognized by the lectin domain of type 3 complement receptors on liver macrophages, leading to rapid clearance by phagocytosis.	Acetylglucosamine	76-87	glycoprotein Ib platelet subunit alpha	Homo sapiens	111-120	
16232387-8	2005	They also demonstrate that phagocytosis of chilled platelets can be inhibited--and in vivo survival prolonged--by enzymatically galactosylating the terminal beta-GlcNAc residues on GPIbalpha.	Acetylglucosamine	157-168	glycoprotein Ib platelet subunit alpha	Homo sapiens	181-190	
16232387-9	2005	Disguising the exposed beta-GlcNAc residues on the N-glycans of the clustered GPIbalpha molecules by galactosylation is a promising approach to storing platelets at 4 degrees C without affecting platelet function.	Acetylglucosamine	23-34	glycoprotein Ib platelet subunit alpha	Homo sapiens	78-87	
15741160-4	2005	alpha(M)beta(2) also recognizes beta-GlcNAc residues on GPIbalpha that are clustered on platelets after cooling.	Acetylglucosamine	32-43	glycoprotein Ib platelet subunit alpha	Homo sapiens	56-65	
15741160-8	2005	Therefore chilled platelets are removed from blood by an interaction between beta-GlcNAc residues on clustered GPIbalpha and the lectin domain of alpha(M) chain of the alpha(M)beta(2) integrin, distinguishing this interaction from those mediated by the alpha(M) I domain.	Acetylglucosamine	77-88	glycoprotein Ib platelet subunit alpha	Homo sapiens	111-120	
12970565-4	2003	We document that alphaMbeta2 is a lectin that recognizes exposed beta-N-acetylglucosamine residues of N-linked glycans on GPIbalpha.	Acetylglucosamine	65-89	glycoprotein Ib platelet subunit alpha	Homo sapiens	122-131