ReviewAnnual review of biophysics2011
Protein folding at the exit tunnel.
Review in Annual review of biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
55 citing papers in PubMed.
- Role of Hsp70 chaperone in client-protein folding elucidated by Markov state modeling and NMR restraint-assisted molecular dynamics simulations.Biophysical journal · 2026Article
- Mechanical forces regulate the composition and fate of stalled nascent chains.Molecular cell · 2026Article
- Chloroplast ATP synthase: From structure to engineering.The Plant cell · 2024Review
- Chloroplast biogenesis involves spatial coordination of nuclear and organellar gene expression in Chlamydomonas.Plant physiology · 2024Article
- Nascent chains derived from a foldable protein sequence interact with specific ribosomal surface sites near the exit tunnel.Scientific reports · 2024Article
- Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex.ACS central science · 2024Article
- Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-TerminalMolecules (Basel, Switzerland) · 2023Article
- Molecular Chaperones' Potential against Defective Proteostasis of Amyotrophic Lateral Sclerosis.Cells · 2023Review
- Reversible protein assemblies in the proteostasis network in health and disease.Frontiers in molecular biosciences · 2023Review
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Modulating co-translational protein folding by rational design and ribosome engineering.Nature communications · 2022Article
- Co-translational assembly orchestrates competing biogenesis pathways.Nature communications · 2022Article
- Hydrophobic and electrostatic interactions modulate protein escape at the ribosomal exit tunnel.Biophysical journal · 2021Article
- Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins.The journal of physical chemistry. B · 2021Article
- The ribosome modulates folding inside the ribosomal exit tunnel.Communications biology · 2021Article
- Statistical Evidence for a Helical Nascent Chain.Biomolecules · 2021Article
- Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding.Genome biology · 2021Article
- An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics.Journal of visualized experiments : JoVE · 2020Article
- Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Transmembrane protein rotaxanes reveal kinetic traps in the refolding of translocated substrates.Communications biology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Over five decades of research have yielded a large body of information on how purified proteins attain their native state when refolded in the test tube, starting from a chemically or thermally denatured state. Nevertheless, we still know little about how proteins fold and unfold in their natural biological habitat: the living cell. Indeed, a variety of cellular components, including molecular chaperones, the ribosome, and crowding of the intracellular medium, modulate folding mechanisms in physiologically relevant environments. This review focuses on the current state of knowledge in protein folding in the cell with emphasis on the early stage of a protein's life, as the nascent polypeptide traverses and emerges from the ribosomal tunnel. Given the vectorial nature of ribosome-assisted translation, the transient degree of chain elongation becomes a relevant variable expected to affect nascent protein foldability, aggregation propensity and extent of interaction with chaperones and the ribosome.
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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.