PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22888537-2	2012	In this study, L-asparaginase was N-terminal site-specifically modified by alkylating PEG with monomethoxy polyethylene glycol-propionaldehyde (mPEG-ALD20000).	monomethoxypolyethylene glycol	144-148	asparaginase and isoaspartyl peptidase 1	Homo sapiens	15-29	
1861535-0	1991	High efficacy of monomethoxypolyethylene glycol-conjugated L-asparaginase (PEG2-ASP) in two patients with hematological malignancies.	monomethoxypolyethylene glycol	17-47	asparaginase and isoaspartyl peptidase 1	Homo sapiens	59-73	
1861535-1	1991	Two patients with hematological malignancies were successfully treated with monomethoxypolyethylene glycol-conjugated Escherichia coli L-asparaginase (PEG2-ASP), which reportedly lacks both antigenicity and immunogenicity but retains catalytic activity as well as slow clearance in an experimental animal model.	monomethoxypolyethylene glycol	76-106	asparaginase and isoaspartyl peptidase 1	Homo sapiens	135-149	
30052638-4	2018	A popular strategy is to randomly conjugate L-asparaginase with mono-methoxy polyethylene glycol, which became a commercial FDA approved formulation widely used in recent years.	monomethoxypolyethylene glycol	64-96	asparaginase and isoaspartyl peptidase 1	Homo sapiens	44-58	
1712146-1	1990	Acetic anhydride, dextran and monomethoxypolyethylene glycol and different modification methods were used for modification of L-asparaginase to maintain enzyme activity and completely remove its antigenicity.	monomethoxypolyethylene glycol	30-60	asparaginase and isoaspartyl peptidase 1	Homo sapiens	126-140	
22888537-3	2012	The optimum reaction parameters were determined as pH 5.0, a molar ratio of mPEG-ALD2000 to L-asparaginase of 10:1, a reaction time of 16 h and temperature of 25 degrees C. PEG-L-asparaginase (PEG-L-ASNase) was isolated and purified with consecutive anion-exchange (XK, 16 x 20 cm, Q Sepharose FF) and gel-filtration (Tricorn, 10 x 600 cm, Sephacryl S-300 HR) chromatography, respectively.	monomethoxypolyethylene glycol	76-80	asparaginase and isoaspartyl peptidase 1	Homo sapiens	177-191	
15274089-0	2004	Hydration of proteins: SAXS study of native and methoxy polyethyleneglycol (mPEG)-modified L-asparaginase and bovine serum albumin in mPEG solutions.	monomethoxypolyethylene glycol	48-74	asparaginase and isoaspartyl peptidase 1	Homo sapiens	91-105	
15274089-0	2004	Hydration of proteins: SAXS study of native and methoxy polyethyleneglycol (mPEG)-modified L-asparaginase and bovine serum albumin in mPEG solutions.	monomethoxypolyethylene glycol	76-80	asparaginase and isoaspartyl peptidase 1	Homo sapiens	91-105	
15274089-3	2004	We show that an mPEG-depleted layer can account for the decrease in the measured radius of gyration R(g) from 34.1 to 31.1 A in native L-asparaginase, and from 32.4 to 31.0 A in native bovine serum albumin (BSA) in mPEG-containing solvents.	monomethoxypolyethylene glycol	16-20	asparaginase and isoaspartyl peptidase 1	Homo sapiens	135-149	
15274089-4	2004	For mPEG-modified proteins in mPEG-free solvents, we attribute the observed increase in the R(g) over that of the native proteins (approximately 3% in L-asparaginase, and 10% in BSA) to the presence of mPEG on the protein surface.	monomethoxypolyethylene glycol	4-8	asparaginase and isoaspartyl peptidase 1	Homo sapiens	151-165