PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33462887-3	2020	Herein, we report the development and application of a mass-spectrometry-based approach to both uncover and characterise the effects of O-glycans on the stability of DC-SIGN.	o-glycans	136-145	CD209 molecule	Homo sapiens	166-173	
32939912-0	2020	Chemo-Enzymatic Synthesis of S. mansoni O-Glycans and Their Evaluation as Ligands for C-Type Lectin Receptors MGL, DC-SIGN, and DC-SIGNR.	o-glycans	40-49	CD209 molecule	Homo sapiens	115-122	
33462887-5	2020	Using ion mobility mass spectrometry, we show how specific O-glycans, and/or single monosaccharide substitutions, alter both the overall collision cross section and the gas-phase stability of the DC-SIGN isoforms.	o-glycans	59-68	CD209 molecule	Homo sapiens	196-203	
22982058-4	2012	Proteins with humanized N-glycans including Man5 structures and O-glycans (up to as many as 24) with single mannose chain length showed DC-SIGN binding that was comparable to that measured for a CHO-produced IgG1 which lacks O-linked mannose.	o-glycans	64-73	CD209 molecule	Homo sapiens	136-143	
22982058-5	2012	Glycoproteins with wild-type N-glycans and mannotriose and higher O-glycans bound to DC-SIGN in a manner that was strongly inhibited by either the use of enzymatic N-deglycosylation or sodium meta-periodate oxidation.	o-glycans	66-75	CD209 molecule	Homo sapiens	85-92