ArticleProceedings of the National Academy of Sciences of the United States of America2020
A nanobody targeting the LIN28:let-7 interaction fragment of TUT4 blocks uridylation of let-7.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- A Simple and Cost-Effective Electrochemical Assay for Heart Failure Prognosis Using Soluble Suppression of Tumorigenicity 2‑Specific Nanobodies.ACS pharmacology & translational science · 2026Article
- Covalently constrained 'Di-Gembodies' enable parallel structure solutions by cryo-EM.Nature chemical biology · 2026Article
- Regulating Protein-RNA Interactions: Advances in Targeting the LIN28/Let-7 Pathway.International journal of molecular sciences · 2024Review
- Dynamic RBM47 ISGylation confers broad immunoprotection against lung injury and tumorigenesis via TSC22D3 downregulation.Cell death discovery · 2023Article
- Evolution of nanobodies specific for BCL11A.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- LIN28A: A multifunctional versatile molecule with future therapeutic potential.World journal of biological chemistry · 2022Review
- The distinct roles of zinc finger CCHC-type (ZCCHC) superfamily proteins in the regulation of RNA metabolism.RNA biology · 2021Review
- MicroRNA let-7b downregulates AML1-ETO oncogene expression in t(8;21) AML by targeting its 3'UTR.Experimental hematology & oncology · 2021Article
- Article
- Polymorphisms in Pepsinogen C and miRNA Genes Associate with High Serum Pepsinogen II in Gastric Cancer Patients.Microorganisms · 2021Article
- Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020Review
- Prospect of SARS-CoV-2 spike protein: Potential role in vaccine and therapeutic development.Virus research · 2020Review
Corrections and comments
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
Abstract
The LIN28:pre-let-7:TUTase ternary complex regulates pluripotency and oncogenesis by controlling processing of the let-7 family of microRNAs. The complex oligouridylates the 3' ends of pre-let-7 molecules, leading to their degradation via the DIS3L2 exonuclease. Previous studies suggest that components of this complex are potential therapeutic targets in malignancies that aberrantly express LIN28. In this study we developed a functional epitope selection approach to identify nanobody inhibitors of the LIN28:pre-let-7:TUT4 complex. We demonstrate that one of the identified nanobodies, Nb-S2A4, targets the 106-residue LIN28:let-7 interaction (LLI) fragment of TUT4. Nb-S2A4 can effectively inhibit oligouridylation and monouridylation of pre-let-7g in vitro. Expressing Nb-S2A4 allows maturation of the let-7 species in cells expressing LIN28, highlighting the therapeutic potential of targeting the LLI fragment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.