PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
1423500-3	1992	Isolated chromaffin granules contained very little synexin, whereas chromaffin granules aggregated with synexin (24 micrograms/mg) and Ca2+ (1 mM) clearly showed synexin-associated immunogold particles in the vicinity of the granule membrane (1.88 gold particles per granule profile).	chromaffin	68-78	annexin A7	Bos taurus	104-111
7696302-1	1995	The effects of the protein synthesis inhibitors actinomycin D and cycloheximide on the cellular content of the calcium binding protein synexin, and on the secretory response of cultured bovine adrenal medullary chromaffin cells were determined.	Cycloheximide	66-79	annexin A7	Bos taurus	135-142
7696302-1	1995	The effects of the protein synthesis inhibitors actinomycin D and cycloheximide on the cellular content of the calcium binding protein synexin, and on the secretory response of cultured bovine adrenal medullary chromaffin cells were determined.	Calcium	111-118	annexin A7	Bos taurus	135-142
7696302-3	1995	The synexin level was reduced by 50% after 133 h of incubation in the presence of 2 micrograms/ml actinomycin D or 5 micrograms/ml cycloheximide.	Dactinomycin	98-111	annexin A7	Bos taurus	4-11
7696302-3	1995	The synexin level was reduced by 50% after 133 h of incubation in the presence of 2 micrograms/ml actinomycin D or 5 micrograms/ml cycloheximide.	Cycloheximide	131-144	annexin A7	Bos taurus	4-11
7696302-4	1995	However, this was partly due to an artefactual stabilization of synexin, since metabolic labelling of synexin with [35S]methionine showed that the half-time of degradation was only 40 h. The secretory response of chromaffin cells was quickly diminished in the presence of protein synthesis inhibitors.	Sulfur-35	116-119	annexin A7	Bos taurus	102-109
7696302-4	1995	However, this was partly due to an artefactual stabilization of synexin, since metabolic labelling of synexin with [35S]methionine showed that the half-time of degradation was only 40 h. The secretory response of chromaffin cells was quickly diminished in the presence of protein synthesis inhibitors.	Methionine	120-130	annexin A7	Bos taurus	102-109
1423500-0	1992	Immunolocalization of synexin (annexin VII) in adrenal chromaffin granules and chromaffin cells: evidence for a dynamic role in the secretory process.	chromaffin	55-65	annexin A7	Bos taurus	22-29
1423500-0	1992	Immunolocalization of synexin (annexin VII) in adrenal chromaffin granules and chromaffin cells: evidence for a dynamic role in the secretory process.	chromaffin	55-65	annexin A7	Bos taurus	31-42
1423500-1	1992	Synexin (annexin VII) is a Ca(2+)- and phospholipid-binding protein which has been proposed to play a role in Ca(2+)-dependent membrane fusion processes.	Phospholipids	39-51	annexin A7	Bos taurus	0-7
1423500-3	1992	Isolated chromaffin granules contained very little synexin, whereas chromaffin granules aggregated with synexin (24 micrograms/mg) and Ca2+ (1 mM) clearly showed synexin-associated immunogold particles in the vicinity of the granule membrane (1.88 gold particles per granule profile).	chromaffin	68-78	annexin A7	Bos taurus	104-111
1423500-1	1992	Synexin (annexin VII) is a Ca(2+)- and phospholipid-binding protein which has been proposed to play a role in Ca(2+)-dependent membrane fusion processes.	Phospholipids	39-51	annexin A7	Bos taurus	9-20
1423500-2	1992	Using a monoclonal antibody against synexin, Mab 10E7, and immunogold, we carried out a semiquantitative localization study of synexin in bovine adrenal medullary chromaffin granules, and in resting and nicotine-stimulated adrenal chromaffin cells.	chromaffin	163-173	annexin A7	Bos taurus	127-134
1423500-5	1992	During the active phase of cholinergically stimulated catecholamine secretion, the amount of synexin label was reduced by 33% in the nucleus, by 23% in the cytosol, and by 51% in the granule area.	Catecholamines	54-67	annexin A7	Bos taurus	93-100
1423500-7	1992	We conclude that synexin is involved in the secretory process in chromaffin cells.	chromaffin	65-75	annexin A7	Bos taurus	17-24
2967699-2	1988	Synexin was isolated from bovine liver by high resolution cation exchange chromatography and fragmented with cyanogen bromide or trypsin.	Cyanogen Bromide	109-125	annexin A7	Bos taurus	0-7
1834175-2	1991	Since synexin from adrenal glands promotes aggregation and fusion of chromaffin granules, we purified synexin-like proteins from bovine lung cytosolic fraction, and evaluated their effect on the fusion of isolated lamellar bodies and plasma membrane fractions.	chromaffin	69-79	annexin A7	Bos taurus	6-13
1834175-6	1991	Lung synexin promoted fusion only in the presence of calcium.	Calcium	53-60	annexin A7	Bos taurus	5-12
2974861-0	1988	A molecular basis for synexin-driven, calcium-dependent membrane fusion.	Calcium	38-45	annexin A7	Bos taurus	22-29
2974861-2	1988	The probable role of calcium in the process is now widely accepted, and it is possible that at least one cytosolic mediator of calcium action is synexin.	Calcium	127-134	annexin A7	Bos taurus	145-152
2974861-3	1988	Synexin is a 47,000 Mr calcium-binding protein, initially discovered in the bovine adrenal medulla, which binds to granule membranes and to inner aspects of chromaffin cell plasma membranes.	Calcium	23-30	annexin A7	Bos taurus	0-7
2974861-3	1988	Synexin is a 47,000 Mr calcium-binding protein, initially discovered in the bovine adrenal medulla, which binds to granule membranes and to inner aspects of chromaffin cell plasma membranes.	chromaffin	157-167	annexin A7	Bos taurus	0-7
2974861-4	1988	Synexin causes chromaffin granules to aggregate, and such aggregates can be caused to fuse in the additional presence of arachidonic acid.	chromaffin	15-25	annexin A7	Bos taurus	0-7
2974861-5	1988	Synexin also mediates the direct fusion of liposomes and chromaffin granule ghosts.	chromaffin	57-67	annexin A7	Bos taurus	0-7
2974861-7	1988	Our initial efforts were directed towards purification of bovine synexin in sufficient amounts to allow us to sequence tryptic peptides.	Peptides	127-135	annexin A7	Bos taurus	65-72
2974861-14	1988	Additional evidence is the fact that synexin also forms calcium-selective channels when the protein is applied to the cytosolic aspect of the plasmalemma when that side is also exposed to calcium at sub-millimolar concentrations.	Calcium	56-63	annexin A7	Bos taurus	37-44
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	phosphatidate	205-218	annexin A7	Bos taurus	38-45
2960380-14	1987	We conclude that the coincident pCa and pH sensitivity of synexin-mediated binding to chromaffin granule membranes and their subsequent fusion might be associated with physiological changes in the concentration of both cations in the cytoplasm of secreting chromaffin cells.	chromaffin	86-96	annexin A7	Bos taurus	58-65
2960380-14	1987	We conclude that the coincident pCa and pH sensitivity of synexin-mediated binding to chromaffin granule membranes and their subsequent fusion might be associated with physiological changes in the concentration of both cations in the cytoplasm of secreting chromaffin cells.	chromaffin	257-267	annexin A7	Bos taurus	58-65
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	Protactinium	220-222	annexin A7	Bos taurus	38-45
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	phosphatidylethanolamine	224-248	annexin A7	Bos taurus	38-45
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	phosphatidylethanolamine	250-252	annexin A7	Bos taurus	38-45
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	Phosphatidylserines	264-282	annexin A7	Bos taurus	38-45
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	phosphatidylethanolamine	283-285	annexin A7	Bos taurus	38-45
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	Spermine	319-327	annexin A7	Bos taurus	38-45
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	Protactinium	346-348	annexin A7	Bos taurus	38-45
2953727-4	1987	These PMN proteins, like bovine liver synexin, promoted aggregation of isolated PMN specific granules in the presence of Ca2+ and increased the overall rate of Ca2+-induced fusion of liposomes composed of phosphatidate (PA)/phosphatidylethanolamine (PE) (1:3) and phosphatidylserine/PE (1:3), but decreased the rate of spermine-induced fusion of PA/PE (1:3) liposomes.	phosphatidylethanolamine	283-285	annexin A7	Bos taurus	38-45
6121822-0	1982	Further characterization of the aggregation and fusion of chromaffin granules by synexin as a model for compound exocytosis.	chromaffin	58-68	annexin A7	Bos taurus	81-88
6459804-5	1982	Depending on the phospholipid composition, synexin could either facilitate or inhibit Ca2+-induced fusion of vesicles.	Phospholipids	17-29	annexin A7	Bos taurus	43-50
2960380-0	1987	Synexin-mediated fusion of bovine chromaffin granule ghosts.	chromaffin	34-44	annexin A7	Bos taurus	0-7
2960380-2	1987	Synexin induces chromaffin granule ghosts to fuse one to another, a process which is followed continuously and quantitatively by monitoring the mixing of the intragranular aqueous compartments.	chromaffin	16-26	annexin A7	Bos taurus	0-7
2960380-10	1987	In our attempt to determine whether the pH effect was on the synexin or on the membranes, we found that fusion was blocked only by treatment of the membranes with the membrane-impermeant carboxyl group modifier 1-ethyl-3-(4-azonia-4,4-dimethylpentyl)carbodiimide.	1-ethyl-3-(4-azonia-4,4-dimethylpentyl)carbodiimide	211-262	annexin A7	Bos taurus	61-68
2933036-1	1985	Three synexin isotypes were identified in bovine liver or adrenal medullary tissues by immune blotting of one- or two-dimensional SDS gels and by two-dimensional tryptic peptide mapping of gel bands or spots.	Sodium Dodecyl Sulfate	130-133	annexin A7	Bos taurus	6-13
6121822-1	1982	Synexin was isolated from bovine liver and found to aggregate adrenal chromaffin granules in the same Ca2+-dependent manner as previously described for adrenal synexin.	chromaffin	70-80	annexin A7	Bos taurus	0-7
6121822-2	1982	The chromaffin granule aggregating activity of liver synexin was blocked in vitro by the addition of an antibody prepared to the 47,000 molecular weight band extracted from an SDS gel of an adrenal medullary synexin preparation.	chromaffin	4-14	annexin A7	Bos taurus	53-60
6121822-2	1982	The chromaffin granule aggregating activity of liver synexin was blocked in vitro by the addition of an antibody prepared to the 47,000 molecular weight band extracted from an SDS gel of an adrenal medullary synexin preparation.	chromaffin	4-14	annexin A7	Bos taurus	208-215
6121822-2	1982	The chromaffin granule aggregating activity of liver synexin was blocked in vitro by the addition of an antibody prepared to the 47,000 molecular weight band extracted from an SDS gel of an adrenal medullary synexin preparation.	Sodium Dodecyl Sulfate	176-179	annexin A7	Bos taurus	53-60
6121822-3	1982	Chromaffin granules aggregated by synexin fused when exposed to cis-unsaturated fatty acids at concentrations comparable to those released from phospholipids by stimulated secretory cells.	chromaffin	0-10	annexin A7	Bos taurus	34-41
6121822-3	1982	Chromaffin granules aggregated by synexin fused when exposed to cis-unsaturated fatty acids at concentrations comparable to those released from phospholipids by stimulated secretory cells.	cis-unsaturated fatty acids	64-91	annexin A7	Bos taurus	34-41
6121822-4	1982	The synexin-induced aggregation reaction was blocked by Erythrosin B, a common food coloring, and by the phenothiazine antipsychotic trifluoperazine and promethazine.	Erythrosine	56-68	annexin A7	Bos taurus	4-11
6121822-4	1982	The synexin-induced aggregation reaction was blocked by Erythrosin B, a common food coloring, and by the phenothiazine antipsychotic trifluoperazine and promethazine.	phenothiazine	105-118	annexin A7	Bos taurus	4-11
6121822-4	1982	The synexin-induced aggregation reaction was blocked by Erythrosin B, a common food coloring, and by the phenothiazine antipsychotic trifluoperazine and promethazine.	Trifluoperazine	133-148	annexin A7	Bos taurus	4-11
6121822-4	1982	The synexin-induced aggregation reaction was blocked by Erythrosin B, a common food coloring, and by the phenothiazine antipsychotic trifluoperazine and promethazine.	Promethazine	153-165	annexin A7	Bos taurus	4-11
6121822-5	1982	The aggregation and fusion of chromaffin granules thus appears to be a useful model system for studying synexin from diverse tissues and for testing pharmacologically or toxicologically active substances for effects on secretory systems.	chromaffin	30-40	annexin A7	Bos taurus	104-111
6112701-3	1980	We have discovered and isolated a new 47,000 MW protein (synexin) from adrenal medulla tissue that fuses chromaffin granule membranes only in the presence of calcium.	chromaffin	105-115	annexin A7	Bos taurus	57-64
6112701-3	1980	We have discovered and isolated a new 47,000 MW protein (synexin) from adrenal medulla tissue that fuses chromaffin granule membranes only in the presence of calcium.	Calcium	158-165	annexin A7	Bos taurus	57-64
6112701-4	1980	Synexin activity was detected in a number of secretory tissues including human platelets and bovine brain, and the synexin molecule was found by immunofluorescent cytochemistry to be localized to the cytoplasm of chromaffin cells.	chromaffin	213-223	annexin A7	Bos taurus	115-122
6112701-6	1980	On the basis of these data we suggest that synexin may be the intracellular receptor for calcium during exocytosis.	Calcium	89-96	annexin A7	Bos taurus	43-50