ArticleProceedings of the National Academy of Sciences of the United States of America2022
Cotranslational folding and assembly of the dimeric
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Lipid-driven alignment and binding of p7 dimers in early oligomer assembly.PLoS computational biology · 2025Article
- Cotranslational membrane insertion of the voltage-sensitive KProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Single-residue effects on the behavior of a nascent polypeptide chain inside the ribosome exit tunnel.bioRxiv : the preprint server for biology · 2024Article
- Dominance analysis of competing protein assembly pathways.PloS one · 2023Article
- Still rocking in the structural era: A molecular overview of the small multidrug resistance (SMR) transporter family.The Journal of biological chemistry · 2022Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In recent years, it has become clear that many homo- and heterodimeric cytoplasmic proteins in both prokaryotic and eukaryotic cells start to dimerize cotranslationally (i.e., while at least one of the two chains is still attached to the ribosome). Whether this is also possible for integral membrane proteins is, however, unknown. Here, we apply force profile analysis (FPA)-a method where a translational arrest peptide (AP) engineered into the polypeptide chain is used to detect force generated on the nascent chain during membrane insertion-to demonstrate cotranslational interactions between a fully membrane-inserted monomer and a nascent, ribosome-tethered monomer of the
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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.