PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24790092-4	2014	We observed that ZG16p preferentially binds to alpha-mannose-terminating short glycans such as Ser/Thr-linked O-mannose, but not to high mannose-type N-glycans.	Polysaccharides	79-86	zymogen granule protein 16	Homo sapiens	17-22	
34077620-3	2021	One prominent attribute of ZG16 is its ability to bind glycans, but other aspects of the protein may also contribute to activity.	Polysaccharides	55-62	zymogen granule protein 16	Homo sapiens	27-31	
21893569-1	2012	Human zymogen granule protein 16 (ZG16p) contains a Jacalin-like lectin domain, although its glycan-binding properties are not fully understood.	Polysaccharides	93-99	zymogen granule protein 16	Homo sapiens	6-32	
21893569-1	2012	Human zymogen granule protein 16 (ZG16p) contains a Jacalin-like lectin domain, although its glycan-binding properties are not fully understood.	Polysaccharides	93-99	zymogen granule protein 16	Homo sapiens	34-39	
21893569-2	2012	Here, we screened the glycan-binding specificity of ZG16p by recently developed glycoconjugate microarray.	Polysaccharides	22-28	zymogen granule protein 16	Homo sapiens	52-57	
34077620-7	2021	ZG16 crystal structures also draw attention to a non-proline cis peptide bond that can isomerize within the protein and to the mobility of glycine-rich loops in the glycan-binding site.	Polysaccharides	165-171	zymogen granule protein 16	Homo sapiens	0-4	
34077620-8	2021	An understanding of the properties of the ZG16 CXXC motif and the discovery of internal conformational switches extend existing knowledge relating to the glycan-binding activity of the protein.	Polysaccharides	154-160	zymogen granule protein 16	Homo sapiens	42-46	
25919894-2	2015	Here we describe detailed analysis of the interaction of human ZG16p with mycobacterial phosphatidylinositol mannosides (PIMs) by glycan microarray and NMR.	Polysaccharides	130-136	zymogen granule protein 16	Homo sapiens	63-68	
25919894-3	2015	Pathogen-related glycan microarray analysis identified phosphatidylinositol mono- and di-mannosides (PIM1 and PIM2) as novel ligand candidates of ZG16p.	Polysaccharides	17-23	zymogen granule protein 16	Homo sapiens	146-151	
25919894-4	2015	Saturation transfer difference (STD) NMR and transferred NOE experiments with chemically synthesized PIM glycans indicate that PIMs preferentially interact with ZG16p by using the mannose residues.	Polysaccharides	105-112	zymogen granule protein 16	Homo sapiens	161-166	
25919894-6	2015	NMR results with docking simulations suggest a binding mode of ZG16p and PIM glycan; this will help to elucidate the physiological role of ZG16p.	Polysaccharides	77-83	zymogen granule protein 16	Homo sapiens	139-144