ReviewThe FEBS journal2011
Transient RNA-protein interactions in RNA folding.
Review in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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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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
40 citing papers in PubMed, 61 citations in OpenAlex.
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- Isolation of nucleic acids using liquid-liquid phase separation of pH-sensitive elastin-like polypeptides.Scientific reports · 2024Article
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- Structural Impact of the Interaction of the Influenza A Virus Nucleoprotein with Genomic RNA Segments.Viruses · 2024Article
- Alu RNA fold links splicing with signal recognition particle proteins.Nucleic acids research · 2023Article
- c-di-GMP regulates activity of the PlzA RNA chaperone from the Lyme disease spirochete.Molecular microbiology · 2023Article
- In vivo architecture of the telomerase RNA catalytic core in Trypanosoma brucei.Nucleic acids research · 2021Article
- Kinetics of protein-assisted nucleic acid interconversion monitored by transient time resolved fluorescence in microfluidic droplets.Nucleic acids research · 2021Article
- The RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements.Nucleic acids research · 2021Article
- Formation of frameshift-stimulating RNA pseudoknots is facilitated by remodeling of their folding intermediates.Nucleic acids research · 2021Article
- Dengue virus 2 capsid protein chaperones the strand displacement of 5'-3' cyclization sequences.Nucleic acids research · 2021Article
- Probing Transcriptome-Wide RNA Structural Changes Dependent on the DEAD-box Helicase Dbp2.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Complexome Profiling-Exploring Mitochondrial Protein Complexes in Health and Disease.Frontiers in cell and developmental biology · 2021Review
- A combined NMR and EPR investigation on the effect of the disordered RGG regions in the structure and the activity of the RRM domain of FUS.Scientific reports · 2020Article
- αβDCA method identifies unspecific binding but specific disruption of the group I intron by the StpA chaperone.RNA (New York, N.Y.) · 2020Article
- Mechanisms and Regulation of RNA Condensation in RNP Granule Formation.Trends in biochemical sciences · 2020Review
- Intrinsic Regulatory Role of RNA Structural Arrangement in Alternative Splicing Control.International journal of molecular sciences · 2020Review
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA folding trajectory features numerous off-pathway folding traps, which represent conformations that are often equally as stable as the native functional ones. Therefore, the conversion between these off-pathway structures and the native correctly folded ones is the critical step in RNA folding. This process, referred to as RNA refolding, is slow, and is represented by a transition state that has a characteristic high free energy. Because this kinetically limiting process occurs in vivo, proteins (called RNA chaperones) have evolved that facilitate the (re)folding of RNA molecules. Here, we present an overview of how proteins interact with RNA molecules in order to achieve properly folded states. In this respect, the discrimination between static and transient interactions is crucial, as different proteins have evolved a multitude of mechanisms for RNA remodeling. For RNA chaperones that act in a sequence-unspecific manner and without the use of external sources of energy, such as ATP, transient RNA-protein interactions represent the basis of the mode of action. By presenting stretches of positively charged amino acids that are positioned in defined spatial configurations, RNA chaperones enable the RNA backbone, via transient electrostatic interactions, to sample a wider conformational space that opens the route for efficient refolding reactions.
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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.