PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1645935-2	1991	We used cation-exchange medium-pressure liquid chromatography and kinetic microenzyme assay (or spectrophotometric monitoring) to analyze the secretion of MPO isoforms by neutrophils exposed to N-formylmethionylleucylphenylalanine (FMLP), digitonin, the ionophore A23187, and serum-opsonized zymosan A (SOZ).	Zymosan	292-301	myeloperoxidase	Homo sapiens	155-158	
17701359-4	2007	In addition, myeloperoxidase released from zymosan-stimulated polymorphonuclear leukocytes was also able to bind to pre-damaged spermatozoa.	Zymosan	43-50	myeloperoxidase	Homo sapiens	13-28	
9877082-4	1998	At this time point, myeloperoxidase activity and lipid peroxidation were markedly increased in the zymosan-activated plasma-treated paw (226 +/- 10.2 mU/100 mg wet tissue, 31 +/- 2.1 mM/mg wet tissue, respectively).	Zymosan	99-106	myeloperoxidase	Homo sapiens	20-35	
9258608-4	1997	Sodium azide inhibited the CLluc of haemocytes stimulated by zymosan, an effective stimulus for myeloperoxidase secretion in human polymorphonuclear leukocytes, but not the CLluc of haemocytes stimulated by PMA, indicating the presence of peroxidases with some properties of myeloperoxidase, in adherent haemocytes from M. galloprovincialis.	Zymosan	61-68	myeloperoxidase	Homo sapiens	96-111	
9176102-8	1997	Taxol at 28 microM also significantly inhibited chemiluminescence, superoxide anion production and myeloperoxidase release from neutrophils stimulated by opsonized zymosan.	Zymosan	164-171	myeloperoxidase	Homo sapiens	99-114	
7990082-5	1994	In the presence of saline unstimulated PMN released 4.48 +/- 0.68% and zymosan-stimulated cells released 7.28 +/- 0.76% of myeloperoxidase content and the enzyme release increased after incubation with captopril (5.55 +/- 0.71 and 8.74 +/- 0.72%), lisinopril (5.43 +/- 0.57 and 9.02 +/- 0.7%), enalaprilat (6.05 +/- 0.67 and 9.20 +/- 0.82%) and ramiprilat (5.82 +/- 0.69 and 9.26 +/- 0.74%), respectively.	Zymosan	71-78	myeloperoxidase	Homo sapiens	123-138	
1666206-1	1991	In four series of experiments human peripheral blood neutrophils were found capable of synthetizing the active forms of such enzymes as myeloperoxidase and acid phosphatase after stimulation with opsonized zymosan, and the optimum conditions for testing the synthetizing activity of neutrophils were established.	Zymosan	206-213	myeloperoxidase	Homo sapiens	136-151	
2982389-1	1985	Myeloperoxidase (MPO)-deficient neutrophils (PMN) released considerably more beta-glucuronidase, lysozyme and vitamin B12-binding activities, when exposed to opsonized zymosan (STZ), than the normal counterpart.	Zymosan	168-175	myeloperoxidase	Homo sapiens	0-15	
2159710-3	1990	The kinetics of MPO exocytosis induced by opsonized zymosan (OZ) and hyposmolarity were indistinguishable; the combination of hyposmolarity and OZ was additive.	Zymosan	52-59	myeloperoxidase	Homo sapiens	16-19	
2982389-1	1985	Myeloperoxidase (MPO)-deficient neutrophils (PMN) released considerably more beta-glucuronidase, lysozyme and vitamin B12-binding activities, when exposed to opsonized zymosan (STZ), than the normal counterpart.	Zymosan	168-175	myeloperoxidase	Homo sapiens	17-20	
180060-6	1976	Zymosan, the phagocytic particle employed in the intact cell system, considerably increased the chemiluminescence of a cell-free superoxide-H2O2 generating system (xanthine-xanthine oxidase) and a system containing myeloperoxidase, H2O2, and chloride.	Zymosan	0-7	myeloperoxidase	Homo sapiens	215-230	
6195265-7	1983	Additionally, heparin was able to reduce the myeloperoxidase release from zymosan-stimulated neutrophils by nearly 50%.	Zymosan	74-81	myeloperoxidase	Homo sapiens	45-60	
6308055-2	1983	Stimulation of neutrophil oxygen (O2) metabolism with phorbol myristate acetate or opsonized zymosan resulted in production of hydrogen peroxide (H2O2), myeloperoxidase-catalyzed oxidation of chloride (C1-) to hypochlorous acid (HOC1), and the reaction of HOC1 with the added compounds to yield nitrogen-chlorine (N-C1) derivatives.	Zymosan	93-100	myeloperoxidase	Homo sapiens	153-168	
6265362-3	1981	We observed that these mannans inhibited the respiratory burst and release of myeloperoxidase stimulated by phagocytosis of serum-opsonized zymosan in vitro.	Zymosan	140-147	myeloperoxidase	Homo sapiens	78-93	
229598-5	1979	Using the myeloperoxidase reaction, this study also demonstrates a morphological alteration in the degranulation process after the ingestion of zymosan particles in both the blasts and the mature PMN cells of leukemic patients.	Zymosan	144-151	myeloperoxidase	Homo sapiens	10-25	
207730-5	1978	Exposure to zymosan under conditions in which the myeloperoxidase system was inactive (i.e., in the presence of myeloperoxidase inhibitors, or in the absence of oxygen) resulted in a substantial increase in the initial O(2) (-)-forming activity of particles from the zymosan-treated cells, but did not prevent the sharp fall in activity seen when zymosan exposure exceeded 10 min.	Zymosan	12-19	myeloperoxidase	Homo sapiens	50-65	
207730-5	1978	Exposure to zymosan under conditions in which the myeloperoxidase system was inactive (i.e., in the presence of myeloperoxidase inhibitors, or in the absence of oxygen) resulted in a substantial increase in the initial O(2) (-)-forming activity of particles from the zymosan-treated cells, but did not prevent the sharp fall in activity seen when zymosan exposure exceeded 10 min.	Zymosan	12-19	myeloperoxidase	Homo sapiens	112-127	
6309288-2	1983	As previously demonstrated with neutrophils, MPO-deficient monocytes had a greater initial rate, duration, and total superoxide production in response to phagocytosis of zymosan than did normal monocytes.	Zymosan	170-177	myeloperoxidase	Homo sapiens	45-48	
6309288-3	1983	Introduction of purified eosinophil peroxidase (EPO) into the phagosome by binding the enzyme to the surface of the zymosan particles changed the hypermetabolic characteristics of superoxide production in MPO-deficient cells to more closely resemble normal cells, but had no effect on superoxide generation by the normal monocytes.	Zymosan	116-123	myeloperoxidase	Homo sapiens	205-208	
6309288-5	1983	Iodination by MPO-deficient monocytes was significantly depressed as compared to normal monocytes following the ingestion of zymosan (1.9 versus 10.1 nmole I-/10(7) monocytes/30 min; p less than 0.01).	Zymosan	125-132	myeloperoxidase	Homo sapiens	14-17	
6309288-6	1983	In contrast, iodination was markedly augmented in MPO-deficient cells compared to normal cells after ingestion of zymosan coated with EPO (208 versus 70 nmole I-/10(7) monocytes/30 min; p less than 0.005), presumably reflecting the greater amounts of hydrogen peroxide formed by MPO-deficient cells.	Zymosan	114-121	myeloperoxidase	Homo sapiens	279-282	
27885574-4	2017	SWCNTs were significantly degraded in zymosan-stimulated macrophages, and the degradation mechanism was dependent on MPO and ONOO--driven oxidative pathways of activated macrophages, where NADPH oxidase was found to be a major determinant of the biodegradation process.	Zymosan	38-45	myeloperoxidase	Homo sapiens	117-120