count	source_label	source_id	relationship	target_label	target_id	entity_type	solr_id	publication_id	sentences
3	SYNE3	UNIPROT:Q6ZMZ3	increases		UNIPROT:P38936	Protein	ac18b242-3a8b-11e8-9192-001a4a160175	28366736	In conclusion, we have shown that: 1) PM2.5exposure could inhibit cell proliferation, induce cell cycle arrest at G2/M phase and increase cell apoptosis; 2) PM2.5exposure could induce the alteration of lncRNA expression profiles; 3) LINC00341 may modulate the PM2.5-induced cell cycle arrest by regulating the expression of p21.|||We identified a lncRNA, LINC00341, which was upregulated expression and mediated cell cycle arrest at G2/M phase by increasing the expression of p21 in 16HBE cell treated with PM2.5.|||LINC00341 mediate cell cycle alteration by regulating p21 expression In order to explore whether LINC00341 regulates the cell cycle by regulating cell-cycle-associated genes, the expressions of 14 genes associated with cell cycle were detected after 48h treatment with PM2.5at different concentrations using qRT-PCR (Fig. 5A), as well as, these genes were detected after different treatment times with the same concentration PM2.5(250μg/mL) (Fig. 5B).
3	SYNE3	UNIPROT:Q6ZMZ3	activates		MESH:D009362	Phenotype	05406db0-5c34-11e7-8e96-001a4ae51246	PMC5362486	Low expression of LINC00341 seems to increase cancer metastasis.|||To explain the reason why LINC00341 low expression increased risk of cancer metastasis, breast cancer patients in TCGA cohort were analyzed.|||The result demonstrated that low expression of LINC00341 increased risk of cancer metastasis, with odds ratio (OR) = 1.36 (95% CI: 1.06~1.75,Z= 2.44,P= 0.01) (Figure6A).
2	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:P50402	Protein	dde57708-bc05-11e5-9b9d-001a4ae51247	10.1016/j.yexcr.2007.03.033	Nesprin3, a part of the LINC-complex, is linked through its amino-terminus to plectin, thus allowing the association of the cytoplasmic IFs with lamins A/C and emerin through the SUN1,2 proteins[60,62,73–75].
2	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0007097	Phenotype	fb5d4964-5c8b-11e7-8c5f-001a4ae51246	PMC4887340	Depletion of Nesprin 3 caused a concomitant loss of nuclear positioning and intracellular pressure asymmetry during 3D migration.
2	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0007049	Phenotype	ac18b242-3a8b-11e8-9192-001a4a160175	28366736	We speculate that LINC00341 can modulate alterations of the cell cycle induced by PM2.5.Our previous studies also supported the function of lncRNAs in regulating the cell cycle (Hu et al., 2015).|||These results suggest that LINC00341 regulates the expression of p21 from both mRNA and protein levels, and mediated the cell cycle alteration induced by PM2.5.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:Q03001	Protein	e4e9c978-bc05-11e5-8abe-001a4ae51246	10.1016/j.yexcr.2008.06.021	This suggests that nesprin-3α promotes the NE localization of the dystonin fusion proteins.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:P08246	Protein	b9e38c08-bc3e-11e5-9b9d-001a4ae51247	PMC4571296	The finding that overexpression of nesprin-3α in an EBS-MD patient cell line only led to limited recruitment of rodless plectin to the NE (Ketemaet al., 2007) may be explained by the relatively low level of expression of the rodless plectin variant in the patient cells (Kosteret al., 2004).
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:P08246	Protein	673410c6-c478-11e5-9cc6-001a4ae51246	21303928	Because overexpression of nesprin-3α leads to the recruitment of endogenous plectin to the NE (Ketema et al., 2007;Wilhelmsen et al., 2005), we investigated the influence of deletion of the seven amino acid motif on plectin recruitment.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:P08246	Protein	e4e9c978-bc05-11e5-8abe-001a4ae51246	10.1016/j.yexcr.2008.06.021	This suggests that nesprin-3α promotes the NE localization of the dystonin fusion proteins.
1	SYNE3	UNIPROT:Q6ZMZ3	increases		UNIPROT:P12830	Protein	2f574d2e-c787-11ee-8b99-0050569a1f61	10.1016/j.biopha.2023.115242	In addition, downregulating LINC00341 increased the expression of p21, Bax, and E-cadherin[162].
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:P19320	Protein	3221fbce-f58e-11eb-8d1f-001a4a160175	30419187	Another lncRNA named LINC00341 could act as a pro-inflammatory inhibitor to prevent the ECs from inflammatory lesions by repressing the vascular cell adhesion molecule 1(VCAM1) [28].
1	SYNE3	UNIPROT:Q6ZMZ3	inhibits		UNIPROT:P19320	Protein	fdd2fa80-f53a-11eb-ba38-001a4a160176	29655896	Tse-Shun Huang's study have shown that LINC00341 mediates PI3K-AKT signaling pathway and inhibits VCAM1 to play an anti-inflammatory effect on vascular endothelial cells (Huang et al., 2017).
1	SYNE3	UNIPROT:Q6ZMZ3	inhibits		UNIPROT:P19320	Protein	3221fbce-f58e-11eb-8d1f-001a4a160175	30419187	Another lncRNA named LINC00341 could act as a pro-inflammatory inhibitor to prevent the ECs from inflammatory lesions by repressing the vascular cell adhesion molecule 1(VCAM1) [28].
1	SYNE3	UNIPROT:Q6ZMZ3	increases		UNIPROT:Q07812	Protein	2f574d2e-c787-11ee-8b99-0050569a1f61	10.1016/j.biopha.2023.115242	In addition, downregulating LINC00341 increased the expression of p21, Bax, and E-cadherin[162].
1	SYNE3	UNIPROT:Q6ZMZ3	inhibits		UNIPROT:Q8WXH0	Protein	61a41858-bc13-11e5-9b9d-001a4ae51247	PMC3388469	Vice versa,the depletion of Nesprin 3 seemed to induce a higher density of Nesprin 2 giant at the nuclear envelope (Fig. 4I; bottom left panel), indicative of a possible competition for SUN-domain binding sites between Nesprin 3 and Nesprin 2 giant.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:Q8WXH0	Protein	d2b749e0-bc3e-11e5-8d2d-001a4ae51247	PMC3727937	Overexpression of nesprin-3 caused a displacement of endogenous nesprin-2 from the NE (data not shown) but did not alter the overall expression level of nesprin-2 giant (Figure 4A).
1	SYNE3	UNIPROT:Q6ZMZ3	increases		UNIPROT:Q15149	Protein	068a946c-739c-11ee-9572-0050569a1f61	10.1007/s12032-023-02132-4	Wilhelmsen et al. used the mouse Sertoli cell line TM-4 to find that the overexpression of nesprin-3 caused a large amount of plectin to gather around the nucleus.
1	SYNE3	UNIPROT:Q6ZMZ3	inhibits		UNIPROT:Q15149	Protein	0aad650c-bc47-11e5-8d2d-001a4ae51247	PMC2171291	It is possible that the function of nesprin-3α is to sequester plectin during such processes as cell division or migration when the cells contract and become more rounded because of cytoskeletal rearrangements.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:Q15149	Protein	cc23f3b6-bc17-11e5-9b9d-001a4ae51247	PMC2586579	Nesprin3 also allows for plectin to link the nucleus to all three cytoskeletal filament systems, including intermediate filaments, F-actin, and microtubules.
1	SYNE3	UNIPROT:Q6ZMZ3	increases		UNIPROT:P38936	Protein	2f574d2e-c787-11ee-8b99-0050569a1f61	10.1016/j.biopha.2023.115242	In addition, downregulating LINC00341 increased the expression of p21, Bax, and E-cadherin[162].
1	SYNE3	UNIPROT:Q6ZMZ3	increases		UNIPROT:P38936	Protein	0bfda32c-c89b-11ee-b346-0050569a791b	10.1016/j.ijbiomac.2023.123790	Their functional analysis showed that p21 expression and PM2.5-induced G2/M phase cell cycle arrest were reversed by lncRNA LINC00341 suppression.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:P08670	Protein	e572209a-c464-11e5-85e4-001a4ae51246	PMC3779758	This possibility is consistent with the observation that knockdown of nesprin-3α triggers a reduction in vimentin networking around the nucleus (68,69), a phenotype that is similar to the one described here upon decreasing expression of either plec1 or endoB2.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:P42858	Protein	2659594c-374b-11e8-8f56-001a4a160175	22202438	LINC00341 and RPS20P22 are elevated in HD compared to controls, whereas LINC00342 is decreased.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		UNIPROT:Q9UNIPROTN3	Protein	20162b16-c8e7-11e5-a1fd-001a4ae51246	17881500	However, we were unable to show that overexpression of nesprin-3α causes a redistribution of MACF to the NE, unlike the effect on plectin.
1	SYNE3	UNIPROT:Q6ZMZ3	inhibits		CHEBI:28744	Chemical	3221fbce-f58e-11eb-8d1f-001a4a160175	30419187	Another lncRNA named LINC00341 could act as a pro-inflammatory inhibitor to prevent the ECs from inflammatory lesions by repressing the vascular cell adhesion molecule 1(VCAM1) [28].
1	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0016477	Phenotype	87a033fc-351e-11e9-87c2-001a4a160175	PMC6072301	Previous studies have revealed that Nesprin3 silencing reduces both the cell migration velocity and the directionality of migration (19).
1	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0010467	Phenotype	ba3e175a-bc38-11e5-ac4e-001a4ae51246	PMC3425586	The gene expression signature associated with high microglia/macrophage number was most strongly driven by two genes: KCNN2 and C14orf139.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0051179	Phenotype	e4e9c978-bc05-11e5-8abe-001a4ae51246	10.1016/j.yexcr.2008.06.021	This suggests that nesprin-3α promotes the NE localization of the dystonin fusion proteins.
1	SYNE3	UNIPROT:Q6ZMZ3	inhibits		MESH:D009362	Phenotype	05406db0-5c34-11e7-8e96-001a4ae51246	PMC5362486	We proposed that LINC00341 might suppress cancer metastasis through mediating these genes expression.
1	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0007050	Phenotype	bdf34ee2-8282-11ee-9572-0050569a1f61	10.1007/s10565-022-09709-1	The lncRNA LINC00341 may contribute to PM2.5-mediated cell cycle arrest in bronchial epithelial cells (Xu et al.2017).
1	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0007050	Phenotype	e9ca1888-f588-11eb-942d-001a4a160176	30384309	Just as reported before, lncRNA LINC00341 mediates cell cycle arrest at the G2/M phase in human bronchial epithelial cells induced by PM2.5, and it may be through the regulation of cycle inhibitor gene p21 (Xu et al., 2017).
1	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0007165	Phenotype	fdd2fa80-f53a-11eb-ba38-001a4a160176	29655896	Tse-Shun Huang's study have shown that LINC00341 mediates PI3K-AKT signaling pathway and inhibits VCAM1 to play an anti-inflammatory effect on vascular endothelial cells (Huang et al., 2017).
1	SYNE3	UNIPROT:Q6ZMZ3	activates		GO:0030225	Phenotype	99a2adaa-bbd7-11e5-9b9d-001a4ae51247	PMC2671807	This immunoblot data is consistent with, but does not firmly establish, an increased expression of human nesprin 3 during TPA-induced macrophage differentiation of HL-60/S4 cells.
1		UNIPROT:Q8WXH0	inhibits	SYNE3	UNIPROT:Q6ZMZ3	Protein	61a41858-bc13-11e5-9b9d-001a4ae51247	PMC3388469	Interestingly, the depletion of Nesprin 2 giant seemed to induce a higher density of Nesprin 3 at the nuclear envelope (Fig. 4H; bottom right panel).
1		UNIPROT:Q15149	activates	SYNE3	UNIPROT:Q6ZMZ3	Protein	fcb4f08a-c739-11ee-9aaa-0050569a1f61	10.1016/j.cub.2023.08.008	Disrupting the plectin-mediated link between nuclear envelope components and keratins by knocking down the nuclear envelope protein nesprin-3 resulted in cytoskeletal collapse, cell rounding and low levels of nuclear YAP.
1		UNIPROT:P61586	inhibits	SYNE3	UNIPROT:Q6ZMZ3	Protein	2e9b704a-c46b-11e5-85e4-001a4ae51246	25170155	Overall actomyosin contractile function remained unaffected in nesprin-3 knockdown cells, because RhoA activation by lysophosphatidic acid still increased 2D focal adhesion size in nesprin-3 siRNA-treated cells on glass (Fig. 4Band fig.
1		MESH:D051379	inhibits	SYNE3	UNIPROT:Q6ZMZ3	Phenotype	d2b749e0-bc3e-11e5-8d2d-001a4ae51247	PMC3727937	Despite the absence of gross abnormalities, the knockout mice allowed us to investigate the function of nesprin-3 in Sertoli cells.
1		UNIPROT:Q9NPE6	increases	SYNE3	UNIPROT:Q6ZMZ3	Protein	87a033fc-351e-11e9-87c2-001a4a160175	PMC6072301	6B and C, SPAG4 silencing significantly reduced the expression of Nesprin3.
1		UNIPROT:P04591	inhibits	SYNE3	UNIPROT:Q6ZMZ3	Protein	ac18b242-3a8b-11e8-9192-001a4a160175	28366736	siRNA transfection LINC00341-specific siRNAs and negative control siRNAs were synthesized by Invitrogen (Waltham, MA, USA).