Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine."@en ?g. }

• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• NP468867.RARVlmKMwVHN5TbHqRo_lH2WSV70tDbuueTR90xvl1l14130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP468867.RARVlmKMwVHN5TbHqRo_lH2WSV70tDbuueTR90xvl1l14130_provenance.
• NP812370.RASD33YdSmpHEOstFlS1Tx0WO3Lu0eFAVpqJf4iQcRA3g130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP812370.RASD33YdSmpHEOstFlS1Tx0WO3Lu0eFAVpqJf4iQcRA3g130_provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." provenance.
• NP809886.RAQ7DfOv3JQ-lEuMOQmvKa66RfBAjOsiVW0aqADVZshZk130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP809886.RAQ7DfOv3JQ-lEuMOQmvKa66RfBAjOsiVW0aqADVZshZk130_provenance.
• NP809879.RAB-m7nEtwtTaxloyEkTGP8idEMuus-RnyxhVzLG191Yc130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP809879.RAB-m7nEtwtTaxloyEkTGP8idEMuus-RnyxhVzLG191Yc130_provenance.
• NP809882.RAAadI5Azox1liMgGR4J_ALR1tlmvyeau4wlDTL7D0ox4130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP809882.RAAadI5Azox1liMgGR4J_ALR1tlmvyeau4wlDTL7D0ox4130_provenance.
• NP468538.RApERf572mvpR9OsAz3UlGlxBo1yJuZzGqeLSZq16cLSw130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP468538.RApERf572mvpR9OsAz3UlGlxBo1yJuZzGqeLSZq16cLSw130_provenance.
• NP468669.RAuW3rSzBroyJthROl-H3onB1tILCtTkZ4UHNQruBSXa8130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP468669.RAuW3rSzBroyJthROl-H3onB1tILCtTkZ4UHNQruBSXa8130_provenance.
• NP468286.RACAHfcPitmaJ8fVqN09jRcrDU_tpiqLkUCNdgFv4b8UQ130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP468286.RACAHfcPitmaJ8fVqN09jRcrDU_tpiqLkUCNdgFv4b8UQ130_provenance.
• NP809881.RAr_lYtgZLKqKuHcq-tgTfTy1-DE3cNhF0iop5L5mBRgU130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP809881.RAr_lYtgZLKqKuHcq-tgTfTy1-DE3cNhF0iop5L5mBRgU130_provenance.
• NP809883.RArkBwowviljPaAvLP8kK1V_cgJ-Napv2R6icQofq52Jw130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP809883.RArkBwowviljPaAvLP8kK1V_cgJ-Napv2R6icQofq52Jw130_provenance.
• NP809885.RAhRywNh6NVue0EqqqyVyhjLGucBD0Bp74-dmhLpfZw30130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP809885.RAhRywNh6NVue0EqqqyVyhjLGucBD0Bp74-dmhLpfZw30130_provenance.
• NP809884.RANln4GvD_n7YLyKapt6TSQZulkafuc00kd8Klx7czTWY130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP809884.RANln4GvD_n7YLyKapt6TSQZulkafuc00kd8Klx7czTWY130_provenance.
• NP812099.RA3UnVlSXj3dx444YHuFNrws06vxBNUOuTt1NHduBGD_Y130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP812099.RA3UnVlSXj3dx444YHuFNrws06vxBNUOuTt1NHduBGD_Y130_provenance.
• NP809876.RA9-NPS5puumOdKizxq-KTKi4yePsCYxMvcKNMPpYZGos130_assertion description "[Initially using a proteomic approach, we identified that heat shock protein 27 (Hsp27) binds to a motif in estrogen receptor alpha (ERalpha) and promotes palmitoylation of the SR. Hsp27-induced acylation occurred on the ERalpha monomer and augmented caveolin-1 interactions with ERalpha, resulting in membrane localization, kinase activation, and DNA synthesis in breast cancer cells.]. Sentence from MEDLINE/PubMed, a database of the U.S. National Library of Medicine." NP809876.RA9-NPS5puumOdKizxq-KTKi4yePsCYxMvcKNMPpYZGos130_provenance.