ReviewRNA biology2021
The La-related proteins: structures and interactions of a versatile superfamily of RNA-binding proteins.
Review in RNA biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 48 citations in OpenAlex.
- RNA-binding proteins in the mouse lens: Functional classifications, expression profiling, and interaction studies of Carhsp1 with crystallin mRNAs.Developmental biology · 2026Article
- Long-Term Salt Exposure Reprograms the Nicotiana tabacum BY-2 Suspension Proteome and Metabolome Toward Stabilization of the Core Metabolic Pathways, Protein Turnover Machinery Modifications, and Protective Metabolome Adjustments.Plant, cell & environment · 2026Article
- Mechanisms of LARP7 in regulating the progression of non-small cell lung cancer.Journal of thoracic disease · 2026Article
- Prime editing for precise genome engineering and modulation of fungal metabolism.Nature biotechnology · 2026Article
- LARP7 enhances the potential of dental pulp stem cells to promote peripheral nerve repair.Stem cells (Dayton, Ohio) · 2026Article
- The Mechanistic Review of the Molecular Interface of RNA-Loaded Extracellular Vesicles: Redefining Targeted Therapy for Autoimmune Disorders.International journal of molecular sciences · 2026Review
- An intrinsically disordered region mediates RNA-binding selectivity and cellular activities of LARP6.Nature communications · 2026Article
- Article
- The LARP6 La module fromRNA biology · 2025Article
- Mitochondria-associated condensates maintain mitochondrial homeostasis and promote lifespan.Nature aging · 2025Article
- Phase separation meets energy generation to boost longevity.Nature aging · 2025Article
- Deciphering the RNA recognition by Musashi-1 to design protein and RNA variants for in vitro and in vivo applications.Nucleic acids research · 2025Article
- SSB cooperates with METTL16-mediated mCell reports · 2025Article
- Noncanonical RNA binding of human La-related protein 6.Nucleic acids research · 2025Article
- Key RNA-binding domains in the La protein establish tRNA modification levels in Trypanosoma brucei.Nucleic acids research · 2025Article
- The dual role of RNA-binding proteins: promotion of tumorigenesis, drug resistance, and emerging therapeutic targets.Acta biochimica et biophysica Sinica · 2025Article
- Article
- The short conserved region-2 of LARP4 interacts with ribosome-associated RACK1 and promotes translation.Nucleic acids research · 2025Article
- The short conserved region-2 of LARP4 interacts with ribosome-associated RACK1 and promotes translation.bioRxiv : the preprint server for biology · 2024Article
- Molecular and Evolutionary Analysis of RNA-Protein Interactions in Telomerase Regulation.Non-coding RNA · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
Abstract
The La-related proteins (LaRPs) are an ancient superfamily of RNA-binding proteins orchestrating the major fates of RNA, from processing and maturation to regulation of mRNA translation. LaRPs are instrumental in modulating complex assemblies where the RNA is bound, folded, processed, escorted and presented to the functional effectors often through recruitment of protein partners. This intricate web of protein-RNA and protein-protein interactions is enabled by the modular nature of the LaRPs, comprising several structured domains connected by flexible linkers, and other sequences lacking recognizable folded motifs. Recent structures, together with biochemical and biophysical studies, have provided insights into how each LaRP family has evolved unique mechanisms of RNA recognition, not only through the conserved RNA-binding unit, the La-module, but also mediated by other family-specific motifs. Furthermore, in a series of unexpected twists and turns, they have revealed that the dynamic and conformational interplay of multi-structured domains and disordered regions operate in unison to achieve RNA substrate discrimination. This review proposes a perspective of our current knowledge of the structure-function relationship of the LaRP superfamily.
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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.