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. 2020 Jun 22;11:3162. doi: 10.1038/s41467-020-16966-3

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a The secondary structure of the J6f1 aptamer predicted by MFold (http://unafold.rna.albany.edu/). b In vitro binding of HULC-J6f1 to tobramycin-conjugated agarose beads. HULC-J6f1 was synthesized by in vitro transcription. Data represent mean ± s.d. of triplicate independent analyses. c The levels of HULC in HepG2 cells overexpressing HULC or HULC-J6f1 were measured by qRT-PCR. HepG2 cells expressing empty vector or J6f1 vector were used as controls. Data represent mean ± s.d. (n = 3 independent experiments, ***P < 0.001, n.s., not significant, by two-sided Student’s t test). d The proliferation of HepG2 cells expressing HULC or HULC-J6f1 was measured by CCK8 assay at the indicated time points. Data represent mean ± s.d. of triplicate independent experiments. e The cellular localizations of HULC and HULC-J6f1 were analyzed by RNA-FISH. The scale bar was 20 μm. f The workflow of tobramycin affinity purification mass spectrometry (TOBAP-MS). See also Supplementary Fig. 1. Source data are provided as a Source data file.