id stringlengths 13 16 | sentence stringlengths 46 809 | label stringclasses 6
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23347038.T13.T22 | The <C>mannose 6-phosphate</C>-binding sites of M6P/<P>IGF2R</P> determine its capacity to suppress matrix invasion by squamous cell carcinoma cells. | 0 |
23347038.T6.T16 | The <C>M6P</C> (mannose 6-phosphate)/<P>IGF2R</P> (insulin-like growth factor II receptor) interacts with a variety of factors that impinge on tumour invasion and metastasis. | 0 |
23347038.T6.T18 | The <C>M6P</C> (mannose 6-phosphate)/IGF2R (<P>insulin-like growth factor II receptor</P>) interacts with a variety of factors that impinge on tumour invasion and metastasis. | 0 |
23347038.T10.T16 | The M6P (<C>mannose 6-phosphate</C>)/<P>IGF2R</P> (insulin-like growth factor II receptor) interacts with a variety of factors that impinge on tumour invasion and metastasis. | 0 |
23347038.T10.T18 | The M6P (<C>mannose 6-phosphate</C>)/IGF2R (<P>insulin-like growth factor II receptor</P>) interacts with a variety of factors that impinge on tumour invasion and metastasis. | 0 |
23347038.T4.T15 | It has been shown that expression of wild-type <C>M6P</C>/<P>IGF2R</P> reduces the tumorigenic and invasive properties of receptor-deficient SCC-VII squamous cell carcinoma cells. | 0 |
23347038.T5.T17 | We have now used mutant forms of <C>M6P</C>/<P>IGF2R</P> to assess the relevance of the different ligand-binding sites of the receptor for its biological activities in this cellular system. | 0 |
23347038.T7.T19 | The results of the present study demonstrate that <C>M6P</C>/<P>IGF2R</P> does not require a functional binding site for insulin-like growth factor II for inhibition of anchorage-independent growth and matrix invasion by SCC-VII cells. | 0 |
23347038.T7.T20 | The results of the present study demonstrate that <C>M6P</C>/IGF2R does not require a functional binding site for <P>insulin-like growth factor II</P> for inhibition of anchorage-independent growth and matrix invasion by SCC-VII cells. | 0 |
23347038.T9.T21 | These findings highlight that the interaction between <C>M6P</C>/<P>IGF2R</P> and M6P-modified ligands is not only important for intracellular accumulation of lysosomal enzymes and formation of dense lysosomes, but is also crucial for the ability of the receptor to suppress SCC-VII growth and invasion. | 0 |
23347038.T21.T11 | These findings highlight that the interaction between M6P/<P>IGF2R</P> and <C>M6P</C>-modified ligands is not only important for intracellular accumulation of lysosomal enzymes and formation of dense lysosomes, but is also crucial for the ability of the receptor to suppress SCC-VII growth and invasion. | 0 |
23347038.T1.T14 | The present study also shows that some of the biological activities of <C>M6P</C>/<P>IGF2R</P> in SCC-VII cells strongly depend on a functional M6P-binding site within domain 3, thus providing further evidence for the non-redundant cellular functions of the individual carbohydrate-binding domains of the receptor. | 0 |
23347038.T14.T2 | The present study also shows that some of the biological activities of M6P/<P>IGF2R</P> in SCC-VII cells strongly depend on a functional <C>M6P</C>-binding site within domain 3, thus providing further evidence for the non-redundant cellular functions of the individual carbohydrate-binding domains of the receptor. | 0 |
23347038.T14.T3 | The present study also shows that some of the biological activities of M6P/<P>IGF2R</P> in SCC-VII cells strongly depend on a functional M6P-binding site within domain 3, thus providing further evidence for the non-redundant cellular functions of the individual <C>carbohydrate</C>-binding domains of the receptor. | 0 |
10730683.T10.T14 | <C>Orlistat</C>, a new <P>lipase</P> inhibitor for the management of obesity. | CPR:4 |
10730683.T3.T12 | <C>Orlistat</C> treatment also results in modest improvements in total cholesterol, <P>low-density lipoprotein</P>, blood pressure, and fasting glucose and insulin concentrations. | CPR:3 |
10730683.T3.T13 | <C>Orlistat</C> treatment also results in modest improvements in total cholesterol, low-density lipoprotein, blood pressure, and fasting glucose and <P>insulin</P> concentrations. | CPR:3 |
10730683.T4.T12 | Orlistat treatment also results in modest improvements in total <C>cholesterol</C>, <P>low-density lipoprotein</P>, blood pressure, and fasting glucose and insulin concentrations. | 0 |
10730683.T4.T13 | Orlistat treatment also results in modest improvements in total <C>cholesterol</C>, low-density lipoprotein, blood pressure, and fasting glucose and <P>insulin</P> concentrations. | 0 |
10730683.T12.T5 | Orlistat treatment also results in modest improvements in total cholesterol, <P>low-density lipoprotein</P>, blood pressure, and fasting <C>glucose</C> and insulin concentrations. | 0 |
10730683.T5.T13 | Orlistat treatment also results in modest improvements in total cholesterol, low-density lipoprotein, blood pressure, and fasting <C>glucose</C> and <P>insulin</P> concentrations. | 0 |
23637347.T10.T1 | In the AG+GG group, males with <P>HDL</P> <C>cholesterol</C> levels <40 mg/dL are less frequent (P = 0.05) and obesity tends to be less prevalent (P = 0.07). | 0 |
1663395.T6.T4 | Evidence has accumulated in the last few years that the expression of the microsomal/peroxidase antigen (<P>M/TPO-Ag</P>) in thyroid cells is induced by TSH, through pathways which involve intracellular <C>cAMP</C> accumulation and protein synthesis. | CPR:3 |
1663395.T14.T4 | Evidence has accumulated in the last few years that the expression of the microsomal/peroxidase antigen (M/TPO-Ag) in thyroid cells is induced by <P>TSH</P>, through pathways which involve intracellular <C>cAMP</C> accumulation and protein synthesis. | 0 |
1663395.T24.T4 | Evidence has accumulated in the last few years that the expression of the <P>microsomal/peroxidase antigen</P> (M/TPO-Ag) in thyroid cells is induced by TSH, through pathways which involve intracellular <C>cAMP</C> accumulation and protein synthesis. | CPR:3 |
1663395.T20.T5 | <P>TSH</P> and <C>cAMP</C> also increase the levels of the specific mRNA for TPO in thyroid cells from different species. | 0 |
1663395.T5.T21 | TSH and <C>cAMP</C> also increase the levels of the specific mRNA for <P>TPO</P> in thyroid cells from different species. | CPR:3 |
1663395.T7.T1 | The modulation of <P>M/TPO-Ag</P> surface expression by TSH can explain the decrease of circulating anti-MAb observed during <C>L-thyroxine</C> therapy in hypothyroid patients with Hashimoto's thyroiditis. | 0 |
1663395.T8.T1 | The modulation of M/TPO-Ag surface expression by <P>TSH</P> can explain the decrease of circulating anti-MAb observed during <C>L-thyroxine</C> therapy in hypothyroid patients with Hashimoto's thyroiditis. | 0 |
1663395.T2.T9 | Other agents, such as <C>methimazole</C> and sodium iodide, which influence thyroid cell function, do not directly interfere with the expression of <P>M/TPO-Ag</P>. | 0 |
1663395.T3.T9 | Other agents, such as methimazole and <C>sodium iodide</C>, which influence thyroid cell function, do not directly interfere with the expression of <P>M/TPO-Ag</P>. | 0 |
23569204.T6.T1 | <P>Saccharomyces cerevisiae τ55</P>, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an <C>N</C>-terminal histidine phosphatase domain (τ55-HPD) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T7.T1 | Saccharomyces cerevisiae τ55, a subunit of the RNA polymerase III-specific general transcription factor <P>TFIIIC</P>, comprises an <C>N</C>-terminal histidine phosphatase domain (τ55-HPD) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T1.T9 | Saccharomyces cerevisiae τ55, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an <C>N</C>-terminal histidine phosphatase domain (<P>τ55</P>-HPD) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T1.T10 | Saccharomyces cerevisiae τ55, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an <C>N</C>-terminal histidine phosphatase domain (τ55-<P>HPD</P>) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T14.T1 | Saccharomyces cerevisiae τ55, a subunit of the <P>RNA polymerase III</P>-specific general transcription factor TFIIIC, comprises an <C>N</C>-terminal histidine phosphatase domain (τ55-HPD) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T6.T2 | <P>Saccharomyces cerevisiae τ55</P>, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an N-terminal <C>histidine</C> phosphatase domain (τ55-HPD) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T7.T2 | Saccharomyces cerevisiae τ55, a subunit of the RNA polymerase III-specific general transcription factor <P>TFIIIC</P>, comprises an N-terminal <C>histidine</C> phosphatase domain (τ55-HPD) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T2.T9 | Saccharomyces cerevisiae τ55, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an N-terminal <C>histidine</C> phosphatase domain (<P>τ55</P>-HPD) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T2.T10 | Saccharomyces cerevisiae τ55, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an N-terminal <C>histidine</C> phosphatase domain (τ55-<P>HPD</P>) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T14.T2 | Saccharomyces cerevisiae τ55, a subunit of the <P>RNA polymerase III</P>-specific general transcription factor TFIIIC, comprises an N-terminal <C>histidine</C> phosphatase domain (τ55-HPD) whose catalytic activity and cellular function is poorly understood. | 0 |
23569204.T11.T3 | We solved the crystal structures of <P>τ55</P>-HPD and its closely related paralogue Huf and used in silico docking methods to identify <C>phospho-serine</C> and phospho-tyrosine containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. | 0 |
23569204.T12.T3 | We solved the crystal structures of τ55-<P>HPD</P> and its closely related paralogue Huf and used in silico docking methods to identify <C>phospho-serine</C> and phospho-tyrosine containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. | 0 |
23569204.T13.T3 | We solved the crystal structures of τ55-HPD and its closely related paralogue <P>Huf</P> and used in silico docking methods to identify <C>phospho-serine</C> and phospho-tyrosine containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. | 0 |
23569204.T3.T15 | We solved the crystal structures of τ55-HPD and its closely related paralogue Huf and used in silico docking methods to identify <C>phospho-serine</C> and phospho-tyrosine containing peptides as possible substrates that were subsequently validated using in vitro <P>phosphatase</P> assays. | 0 |
23569204.T11.T4 | We solved the crystal structures of <P>τ55</P>-HPD and its closely related paralogue Huf and used in silico docking methods to identify phospho-serine and <C>phospho-tyrosine</C> containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. | 0 |
23569204.T12.T4 | We solved the crystal structures of τ55-<P>HPD</P> and its closely related paralogue Huf and used in silico docking methods to identify phospho-serine and <C>phospho-tyrosine</C> containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. | 0 |
23569204.T13.T4 | We solved the crystal structures of τ55-HPD and its closely related paralogue <P>Huf</P> and used in silico docking methods to identify phospho-serine and <C>phospho-tyrosine</C> containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. | 0 |
23569204.T4.T15 | We solved the crystal structures of τ55-HPD and its closely related paralogue Huf and used in silico docking methods to identify phospho-serine and <C>phospho-tyrosine</C> containing peptides as possible substrates that were subsequently validated using in vitro <P>phosphatase</P> assays. | 0 |
23569204.T5.T16 | A comparative <C>phospho</C>-proteomic study identified additional phosphopeptides as possible targets, which show the involvement of these two <P>phosphatases</P> in the regulation of a variety of cellular functions. | 0 |
23506741.T10.T27 | A novel benzo[d]imidazole derivate prevents the development of dextran sulfate <C>sodium</C>-induced murine experimental colitis via inhibition of <P>NLRP3</P> inflammasome. | 0 |
23506741.T11.T27 | A novel <C>benzo[d]imidazole</C> derivate prevents the development of dextran sulfate sodium-induced murine experimental colitis via inhibition of <P>NLRP3</P> inflammasome. | CPR:4 |
23506741.T4.T19 | In the present study, we aimed at examining the effect of <C>1-ethyl-5-methyl-2-phenyl-1H-benzo[d]imidazole</C>, a synthetic small molecular compound also named Fc11a-2, for the treatment of dextran sulfate sodium (DSS)-induced experimental colitis in mice via targeting <P>NLRP3</P> inflammasome. | 0 |
23506741.T5.T19 | In the present study, we aimed at examining the effect of 1-ethyl-5-methyl-2-phenyl-1H-benzo[d]imidazole, a synthetic small molecular compound also named <C>Fc11a-2</C>, for the treatment of dextran sulfate sodium (DSS)-induced experimental colitis in mice via targeting <P>NLRP3</P> inflammasome. | 0 |
23506741.T6.T19 | In the present study, we aimed at examining the effect of 1-ethyl-5-methyl-2-phenyl-1H-benzo[d]imidazole, a synthetic small molecular compound also named Fc11a-2, for the treatment of dextran <C>sulfate</C> sodium (DSS)-induced experimental colitis in mice via targeting <P>NLRP3</P> inflammasome. | 0 |
23506741.T7.T19 | In the present study, we aimed at examining the effect of 1-ethyl-5-methyl-2-phenyl-1H-benzo[d]imidazole, a synthetic small molecular compound also named Fc11a-2, for the treatment of dextran sulfate <C>sodium</C> (DSS)-induced experimental colitis in mice via targeting <P>NLRP3</P> inflammasome. | 0 |
23506741.T20.T8 | In addition, the disease activity index, histopathologic scores and <P>myeloperoxidase</P> activity were also significantly reduced by <C>Fc11a-2</C> treatment. | CPR:4 |
23506741.T21.T9 | Moreover, protein and mRNA levels of DSS-induced proinflammatory <P>cytokines</P> in colon, including TNF-α, IL-1β, IL-18, IL-17A and IFN-γ, were markedly suppressed by <C>Fc11a-2</C>. | CPR:4 |
23506741.T22.T9 | Moreover, protein and mRNA levels of DSS-induced proinflammatory cytokines in colon, including <P>TNF-α</P>, IL-1β, IL-18, IL-17A and IFN-γ, were markedly suppressed by <C>Fc11a-2</C>. | CPR:4 |
23506741.T23.T9 | Moreover, protein and mRNA levels of DSS-induced proinflammatory cytokines in colon, including TNF-α, <P>IL-1β</P>, IL-18, IL-17A and IFN-γ, were markedly suppressed by <C>Fc11a-2</C>. | CPR:4 |
23506741.T24.T9 | Moreover, protein and mRNA levels of DSS-induced proinflammatory cytokines in colon, including TNF-α, IL-1β, <P>IL-18</P>, IL-17A and IFN-γ, were markedly suppressed by <C>Fc11a-2</C>. | CPR:4 |
23506741.T25.T9 | Moreover, protein and mRNA levels of DSS-induced proinflammatory cytokines in colon, including TNF-α, IL-1β, IL-18, <P>IL-17A</P> and IFN-γ, were markedly suppressed by <C>Fc11a-2</C>. | CPR:4 |
23506741.T26.T9 | Moreover, protein and mRNA levels of DSS-induced proinflammatory cytokines in colon, including TNF-α, IL-1β, IL-18, IL-17A and <P>IFN-γ</P>, were markedly suppressed by <C>Fc11a-2</C>. | CPR:4 |
23506741.T13.T1 | Furthermore, a decreased CD11c(+) macrophage infiltration in colons and inactivation of <P>caspase-1</P> in peritoneal macrophages were detected in <C>Fc11a</C>-2-treated mice. | CPR:4 |
23506741.T2.T14 | The mechanism of action of <C>Fc11a-2</C> was related to the inhibition of the cleavage of <P>pro-caspase-1</P>, pro-IL-1β and pro-IL-18 which in turn suppressed the activation of NLRP3 inflammasome. | CPR:4 |
23506741.T2.T15 | The mechanism of action of <C>Fc11a-2</C> was related to the inhibition of the cleavage of pro-caspase-1, <P>pro-IL-1β</P> and pro-IL-18 which in turn suppressed the activation of NLRP3 inflammasome. | CPR:4 |
23506741.T2.T16 | The mechanism of action of <C>Fc11a-2</C> was related to the inhibition of the cleavage of pro-caspase-1, pro-IL-1β and <P>pro-IL-18</P> which in turn suppressed the activation of NLRP3 inflammasome. | CPR:4 |
23506741.T2.T17 | The mechanism of action of <C>Fc11a-2</C> was related to the inhibition of the cleavage of pro-caspase-1, pro-IL-1β and pro-IL-18 which in turn suppressed the activation of <P>NLRP3</P> inflammasome. | CPR:4 |
23506741.T3.T18 | Taken together, our results demonstrate the ability of <C>Fc11a-2</C> to inhibit <P>NLRP3</P> inflammasome activation and its potential use in the treatment of inflammatory bowel diseases. | CPR:4 |
17611273.T12.T22 | At PND35, the medial prefrontal cortex (mPFC) of rats given <C>MPH</C> showed 55% greater immunoreactivity (-ir) for the catecholamine marker <P>tyrosine hydroxylase</P> (TH), 60% more Nissl-stained cells, and 40% less norepinephrine transporter (NET)-ir density. | CPR:3 |
17611273.T12.T23 | At PND35, the medial prefrontal cortex (mPFC) of rats given <C>MPH</C> showed 55% greater immunoreactivity (-ir) for the catecholamine marker tyrosine hydroxylase (<P>TH</P>), 60% more Nissl-stained cells, and 40% less norepinephrine transporter (NET)-ir density. | CPR:3 |
17611273.T12.T24 | At PND35, the medial prefrontal cortex (mPFC) of rats given <C>MPH</C> showed 55% greater immunoreactivity (-ir) for the catecholamine marker tyrosine hydroxylase (TH), 60% more Nissl-stained cells, and 40% less <P>norepinephrine transporter</P> (NET)-ir density. | CPR:4 |
17611273.T12.T25 | At PND35, the medial prefrontal cortex (mPFC) of rats given <C>MPH</C> showed 55% greater immunoreactivity (-ir) for the catecholamine marker tyrosine hydroxylase (TH), 60% more Nissl-stained cells, and 40% less norepinephrine transporter (<P>NET</P>)-ir density. | CPR:4 |
17611273.T13.T22 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the <C>catecholamine</C> marker <P>tyrosine hydroxylase</P> (TH), 60% more Nissl-stained cells, and 40% less norepinephrine transporter (NET)-ir density. | 0 |
17611273.T13.T23 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the <C>catecholamine</C> marker tyrosine hydroxylase (<P>TH</P>), 60% more Nissl-stained cells, and 40% less norepinephrine transporter (NET)-ir density. | 0 |
17611273.T13.T24 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the <C>catecholamine</C> marker tyrosine hydroxylase (TH), 60% more Nissl-stained cells, and 40% less <P>norepinephrine transporter</P> (NET)-ir density. | 0 |
17611273.T13.T25 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the <C>catecholamine</C> marker tyrosine hydroxylase (TH), 60% more Nissl-stained cells, and 40% less norepinephrine transporter (<P>NET</P>)-ir density. | 0 |
17611273.T14.T23 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the catecholamine marker <C>tyrosine</C> hydroxylase (<P>TH</P>), 60% more Nissl-stained cells, and 40% less norepinephrine transporter (NET)-ir density. | 0 |
17611273.T14.T24 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the catecholamine marker <C>tyrosine</C> hydroxylase (TH), 60% more Nissl-stained cells, and 40% less <P>norepinephrine transporter</P> (NET)-ir density. | 0 |
17611273.T14.T25 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the catecholamine marker <C>tyrosine</C> hydroxylase (TH), 60% more Nissl-stained cells, and 40% less norepinephrine transporter (<P>NET</P>)-ir density. | 0 |
17611273.T22.T15 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the catecholamine marker <P>tyrosine hydroxylase</P> (TH), 60% more Nissl-stained cells, and 40% less <C>norepinephrine</C> transporter (NET)-ir density. | 0 |
17611273.T23.T15 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the catecholamine marker tyrosine hydroxylase (<P>TH</P>), 60% more Nissl-stained cells, and 40% less <C>norepinephrine</C> transporter (NET)-ir density. | 0 |
17611273.T15.T25 | At PND35, the medial prefrontal cortex (mPFC) of rats given MPH showed 55% greater immunoreactivity (-ir) for the catecholamine marker tyrosine hydroxylase (TH), 60% more Nissl-stained cells, and 40% less <C>norepinephrine</C> transporter (<P>NET</P>)-ir density. | 0 |
17611273.T16.T18 | In hippocampal dentate gyrus, <C>MPH</C>-receiving rats showed a 51% decrease in NET-ir density and a 61% expanded distribution of the new-cell marker PSA-NCAM (polysialylated form of <P>neural cell adhesion molecule</P>). | CPR:3 |
17611273.T16.T26 | In hippocampal dentate gyrus, <C>MPH</C>-receiving rats showed a 51% decrease in <P>NET</P>-ir density and a 61% expanded distribution of the new-cell marker PSA-NCAM (polysialylated form of neural cell adhesion molecule). | CPR:4 |
17611273.T16.T27 | In hippocampal dentate gyrus, <C>MPH</C>-receiving rats showed a 51% decrease in NET-ir density and a 61% expanded distribution of the new-cell marker PSA-<P>NCAM</P> (polysialylated form of neural cell adhesion molecule). | CPR:3 |
17611273.T19.T1 | In medial striatum, <P>TH</P>-ir decreased by 21%, and in hypothalamus neuropeptide Y-ir increased by 10% in <C>MPH</C>-exposed rats. | CPR:4 |
17611273.T20.T1 | In medial striatum, TH-ir decreased by 21%, and in hypothalamus <P>neuropeptide Y</P>-ir increased by 10% in <C>MPH</C>-exposed rats. | CPR:3 |
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