ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2015
Channel crossing: how are proteins shipped across the bacterial plasma membrane?
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 67 citations in OpenAlex.
- Charge Neutralization During Peptide Transport in the Bacterial SecYEG Translocon.Biomolecules · 2025Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Highly multiplexed spatial transcriptomics in bacteria.Science (New York, N.Y.) · 2025Article
- Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.Biophysical journal · 2025Article
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- Highly Multiplexed Spatial Transcriptomics in Bacteria.bioRxiv : the preprint server for biology · 2024Article
- A unifying mechanism for protein transport through the core bacterial Sec machinery.Open biology · 2023Review
- Article
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Refined measurement of SecA-driven protein secretion reveals that translocation is indirectly coupled to ATP turnover.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Iron is a ligand of SecA-like metal-binding domainsThe Journal of biological chemistry · 2020Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism.Journal of bacteriology · 2020Article
- Novel Sequence Feature of SecA Translocase Protein Unique to the Thermophilic Bacteria: Bioinformatics Analyses to Investigate Their Potential Roles.Microorganisms · 2019Article
- Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome inThe Journal of biological chemistry · 2019Article
- Structure of the substrate-engaged SecA-SecY protein translocation machine.Nature communications · 2019Article
- Article
- Investigating the stability of the SecA-SecYEG complex during protein translocation across the bacterial membrane.The Journal of biological chemistry · 2019Article
- Two paths diverged in the stroma: targeting to dual SEC translocase systems in chloroplasts.Photosynthesis research · 2018Review
- A positive positive to negative.Nature chemistry · 2018Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The structure of the first protein-conducting channel was determined more than a decade ago. Today, we are still puzzled by the outstanding problem of protein translocation--the dynamic mechanism underlying the consignment of proteins across and into membranes. This review is an attempt to summarize and understand the energy transducing capabilities of protein-translocating machines, with emphasis on bacterial systems: how polypeptides make headway against the lipid bilayer and how the process is coupled to the free energy associated with ATP hydrolysis and the transmembrane protein motive force. In order to explore how cargo is driven across the membrane, the known structures of the protein-translocation machines are set out against the background of the historic literature, and in the light of experiments conducted in their wake. The paper will focus on the bacterial general secretory (Sec) pathway (SecY-complex), and its eukaryotic counterpart (Sec61-complex), which ferry proteins across the membrane in an unfolded state, as well as the unrelated Tat system that assembles bespoke channels for the export of folded proteins.
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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.