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PubMed_ArguminSci

Id	Subject	Object	Predicate	Lexical cue
T1	171-265	DRI_Background	denotes	The developmental cycle of Chlamydiaceae occurs in a membrane compartment called an inclusion.
T2	266-372	DRI_Background	denotes	IncA is a member of a family of proteins synthesized and secreted onto the inclusion membrane by bacteria.
T3	373-459	DRI_Background	denotes	IncA proteins from different species of Chlamydiaceae show little sequence similarity.
T4	460-562	DRI_Outcome	denotes	We report that the biochemical properties of Chlamydia trachomatis and Chlamydia caviae are conserved.
T5	563-610	DRI_Approach	denotes	Both proteins self-associate to form multimers.
T6	611-700	DRI_Background	denotes	When artificially expressed by the host cell, they localize to the endoplasmic reticulum.
T7	701-828	DRI_Background	denotes	Strikingly, heterologous expression of IncA in the endoplasmic reticulum completely inhibits concomitant inclusion development.
T8	829-1054	DRI_Outcome	denotes	Using truncated forms of IncA from C. caviae, we show that expression of the C-terminal cytoplasmic domain of the protein at the surface of the endoplasmic reticulum is sufficient to disrupt the bacterial developmental cycle.
T9	1055-1360	DRI_Outcome	denotes	On the other hand, development of a C. trachomatis strain that does not express IncA is not inhibited by artificial IncA expression, showing that the disruptive effect observed with the wild-type strain requires direct interactions between IncA molecules at the inclusion and on the endoplasmic reticulum.
T10	1361-1542	DRI_Approach	denotes	Finally, we modeled IncA tetramers in parallel four helix bundles based on the structure of the SNARE complex, a conserved structure involved in membrane fusion in eukaryotic cells.
T11	1543-1625	DRI_Background	denotes	Both C. trachomatis and C. caviae IncA tetramers were highly stable in this model.
T12	1626-1874	DRI_Outcome	denotes	In conclusion, we show that the property of IncA proteins to assemble into multimeric structures is conserved between chlamydial species, and we propose that these proteins may have co-evolved with the SNARE machinery for a role in membrane fusion.

sentences

Id	Subject	Object	Predicate	Lexical cue
T1	0-170	Sentence	denotes	Conservation of the biochemical properties of IncA from Chlamydia trachomatis and Chlamydia caviae: oligomerization of IncA mediates interaction between facing membranes.
T2	171-265	Sentence	denotes	The developmental cycle of Chlamydiaceae occurs in a membrane compartment called an inclusion.
T3	266-372	Sentence	denotes	IncA is a member of a family of proteins synthesized and secreted onto the inclusion membrane by bacteria.
T4	373-459	Sentence	denotes	IncA proteins from different species of Chlamydiaceae show little sequence similarity.
T5	460-562	Sentence	denotes	We report that the biochemical properties of Chlamydia trachomatis and Chlamydia caviae are conserved.
T6	563-610	Sentence	denotes	Both proteins self-associate to form multimers.
T7	611-700	Sentence	denotes	When artificially expressed by the host cell, they localize to the endoplasmic reticulum.
T8	701-828	Sentence	denotes	Strikingly, heterologous expression of IncA in the endoplasmic reticulum completely inhibits concomitant inclusion development.
T9	829-1054	Sentence	denotes	Using truncated forms of IncA from C. caviae, we show that expression of the C-terminal cytoplasmic domain of the protein at the surface of the endoplasmic reticulum is sufficient to disrupt the bacterial developmental cycle.
T10	1055-1360	Sentence	denotes	On the other hand, development of a C. trachomatis strain that does not express IncA is not inhibited by artificial IncA expression, showing that the disruptive effect observed with the wild-type strain requires direct interactions between IncA molecules at the inclusion and on the endoplasmic reticulum.
T11	1361-1542	Sentence	denotes	Finally, we modeled IncA tetramers in parallel four helix bundles based on the structure of the SNARE complex, a conserved structure involved in membrane fusion in eukaryotic cells.
T12	1543-1625	Sentence	denotes	Both C. trachomatis and C. caviae IncA tetramers were highly stable in this model.
T13	1626-1874	Sentence	denotes	In conclusion, we show that the property of IncA proteins to assemble into multimeric structures is conserved between chlamydial species, and we propose that these proteins may have co-evolved with the SNARE machinery for a role in membrane fusion.

Glycosmos6-MAT

Id	Subject	Object	Predicate	Lexical cue
T1	1068-1072	http://purl.obolibrary.org/obo/MAT_0000091	denotes	hand

mondo_disease

Id	Subject	Object	Predicate	Lexical cue	mondo_id
T1	56-65	Disease	denotes	Chlamydia	http://purl.obolibrary.org/obo/MONDO_0005701
T2	82-91	Disease	denotes	Chlamydia	http://purl.obolibrary.org/obo/MONDO_0005701
T3	505-514	Disease	denotes	Chlamydia	http://purl.obolibrary.org/obo/MONDO_0005701
T4	531-540	Disease	denotes	Chlamydia	http://purl.obolibrary.org/obo/MONDO_0005701

Anatomy-MAT

Id	Subject	Object	Predicate	Lexical cue	mat_id
T1	1068-1072	Body_part	denotes	hand	http://purl.obolibrary.org/obo/MAT_0000091

NCBITAXON

Id	Subject	Object	Predicate	Lexical cue	db_id
T1	46-50	OrganismTaxon	denotes	IncA	1207154
T2	56-77	OrganismTaxon	denotes	Chlamydia trachomatis	813
T3	82-98	OrganismTaxon	denotes	Chlamydia caviae	83557
T4	119-123	OrganismTaxon	denotes	IncA	1207154
T5	198-211	OrganismTaxon	denotes	Chlamydiaceae	809
T6	266-270	OrganismTaxon	denotes	IncA	1207154
T7	363-371	OrganismTaxon	denotes	bacteria	2\|629395
T9	373-377	OrganismTaxon	denotes	IncA	1207154
T10	413-426	OrganismTaxon	denotes	Chlamydiaceae	809
T11	505-526	OrganismTaxon	denotes	Chlamydia trachomatis	813
T12	531-547	OrganismTaxon	denotes	Chlamydia caviae	83557
T13	740-744	OrganismTaxon	denotes	IncA	1207154
T14	854-858	OrganismTaxon	denotes	IncA	1207154
T15	1135-1139	OrganismTaxon	denotes	IncA	1207154
T16	1171-1175	OrganismTaxon	denotes	IncA	1207154
T17	1295-1299	OrganismTaxon	denotes	IncA	1207154
T18	1381-1385	OrganismTaxon	denotes	IncA	1207154
T19	1577-1581	OrganismTaxon	denotes	IncA	1207154
T20	1670-1674	OrganismTaxon	denotes	IncA	1207154

Anatomy-UBERON

Id	Subject	Object	Predicate	Lexical cue	uberon_id
T1	160-169	Body_part	denotes	membranes	http://purl.obolibrary.org/obo/GO_0016020\|http://purl.obolibrary.org/obo/UBERON_0000094\|http://purl.obolibrary.org/obo/UBERON_0000158
T4	224-232	Body_part	denotes	membrane	http://purl.obolibrary.org/obo/GO_0016020\|http://purl.obolibrary.org/obo/UBERON_0000094\|http://purl.obolibrary.org/obo/UBERON_0000158
T7	351-359	Body_part	denotes	membrane	http://purl.obolibrary.org/obo/GO_0016020\|http://purl.obolibrary.org/obo/UBERON_0000094\|http://purl.obolibrary.org/obo/UBERON_0000158
T10	690-699	Body_part	denotes	reticulum	http://purl.obolibrary.org/obo/UBERON_0007361
T11	764-773	Body_part	denotes	reticulum	http://purl.obolibrary.org/obo/UBERON_0007361
T12	917-928	Body_part	denotes	cytoplasmic	http://purl.obolibrary.org/obo/GO_0005737
T13	985-994	Body_part	denotes	reticulum	http://purl.obolibrary.org/obo/UBERON_0007361
T14	1068-1072	Body_part	denotes	hand	http://purl.obolibrary.org/obo/UBERON_0002398
T15	1350-1359	Body_part	denotes	reticulum	http://purl.obolibrary.org/obo/UBERON_0007361
T16	1413-1418	Body_part	denotes	helix	http://purl.obolibrary.org/obo/UBERON_0002488
T17	1506-1514	Body_part	denotes	membrane	http://purl.obolibrary.org/obo/GO_0016020\|http://purl.obolibrary.org/obo/UBERON_0000094\|http://purl.obolibrary.org/obo/UBERON_0000158
T20	1525-1541	Body_part	denotes	eukaryotic cells	http://purl.obolibrary.org/obo/CL_0000255
T21	1858-1866	Body_part	denotes	membrane	http://purl.obolibrary.org/obo/GO_0016020\|http://purl.obolibrary.org/obo/UBERON_0000094\|http://purl.obolibrary.org/obo/UBERON_0000158

CL-cell

Id	Subject	Object	Predicate	Lexical cue	cl_id
T1	1525-1541	Cell	denotes	eukaryotic cells	http://purl.obolibrary.org/obo/CL:0000255