ReviewActa crystallographica. Section D, Structural biology2017
The ribosome and its role in protein folding: looking through a magnifying glass.
Review in Acta crystallographica. Section D, Structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Proinsulin regulators identified with CRISPR screen and in vivo mouse QTL mapping.Nature communications · 2026Article
- How Does Genetic Information Enable Life?Bulletin of mathematical biology · 2026Article
- Correction of VWF multimerization in type 2A/IIC von Willebrand disease by exogenous VWF propeptide supplementation.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Integration of text mining and biological network analysis: Identification of essential genes in sulfate-reducing bacteria.Frontiers in microbiology · 2023Article
- The role of cellular proteostasis in antitumor immunity.The Journal of biological chemistry · 2022Review
- Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?International journal of molecular sciences · 2022Review
- Hydrophobic and electrostatic interactions modulate protein escape at the ribosomal exit tunnel.Biophysical journal · 2021Article
- Conserved residues Glu37 and Trp229 play an essential role in protein folding of β-lactamase.The FEBS journal · 2021Article
- Translational control in aging and neurodegeneration.Wiley interdisciplinary reviews. RNA · 2021Review
- Article
- Gradual compaction of the nascent peptide during cotranslational folding on the ribosome.eLife · 2020Article
- Insights Into Translatomics in the Nervous System.Frontiers in genetics · 2020Review
- Network theory of the bacterial ribosome.PloS one · 2020Article
- Differences in the path to exit the ribosome across the three domains of life.Nucleic acids research · 2019Article
- OSTRFPD: Multifunctional Tool for Genome-Wide Short Tandem Repeat Analysis for DNA, Transcripts, and Amino Acid Sequences with Integrated Primer Designer.Evolutionary bioinformatics online · 2019Article
- Modulating long-range energetics via helix stabilization: A case study using T4 lysozyme.Protein science : a publication of the Protein Society · 2018Article
- A small single-domain protein folds through the same pathway on and off the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Codon usage clusters correlation: towards protein solubility prediction in heterologous expression systems in E. coli.Scientific reports · 2018Article
- How Messenger RNA and Nascent Chain Sequences Regulate Translation Elongation.Annual review of biochemistry · 2018Review
- Unraveling co-translational protein folding: Concepts and methods.Methods (San Diego, Calif.) · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Protein folding, a process that underpins cellular activity, begins co-translationally on the ribosome. During translation, a newly synthesized polypeptide chain enters the ribosomal exit tunnel and actively interacts with the ribosome elements - the r-proteins and rRNA that line the tunnel - prior to emerging into the cellular milieu. While understanding of the structure and function of the ribosome has advanced significantly, little is known about the process of folding of the emerging nascent chain (NC). Advances in cryo-electron microscopy are enabling visualization of NCs within the exit tunnel, allowing early glimpses of the interplay between the NC and the ribosome. Once it has emerged from the exit tunnel into the cytosol, the NC (still attached to its parent ribosome) can acquire a range of conformations, which can be characterized by NMR spectroscopy. Using experimental restraints within molecular-dynamics simulations, the ensemble of NC structures can be described. In order to delineate the process of co-translational protein folding, a hybrid structural biology approach is foreseeable, potentially offering a complete atomic description of protein folding as it occurs on the ribosome.
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What OpenQuestion holds
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.