ArticleProtein expression and purification2017
Recombinant expression and purification of the RNA-binding LARP6 proteins from fish genetic model organisms.
Article in Protein expression and purification, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- The LARP6 La module fromRNA biology · 2025Article
- RNA aptamers as tools for the purification and analysis of in vivo assembled ribonucleoproteins.RNA (New York, N.Y.) · 2025Review
- A Robust Expression and Purification Protocol for the Production of the La Domain of Human LARP6.ACS omega · 2025Article
- Characterization of Sequence-Specific Binding of LARP6 to the 5' Stem-Loop of Type I Collagen mRNAs and Implications for Rational Design of Antifibrotic Drugs.Journal of molecular biology · 2022Article
- The La-related proteins: structures and interactions of a versatile superfamily of RNA-binding proteins.RNA biology · 2021Review
- Maternal Larp6 controls oocyte development, chorion formation and elevation.Development (Cambridge, England) · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The RNA-binding proteins that comprise the La-related protein (LARP) superfamily have been implicated in a wide range of cellular functions, from tRNA maturation to regulation of protein synthesis. To more expansively characterize the biological function of the LARP6 subfamily, we have recombinantly expressed the full-length LARP6 proteins from two teleost fish, platyfish (Xiphophorus maculatus) and zebrafish (Danio rerio). The yields of the recombinant proteins were enhanced to >2 mg/L using a tandem approach of an N-terminal His
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Registered trials
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