ArticleProceedings of the National Academy of Sciences of the United States of America2011
Probing the SecYEG translocation pore size with preproteins conjugated with sizable rigid spherical molecules.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. 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
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
38 citing papers in PubMed, 73 citations in OpenAlex.
- Outer membrane proteins mediate unconventional secretion of Pseudomonas peroxidase through crosstalk between the Sec pathway and outer membrane vesicles.PLoS genetics · 2026Article
- Investigating the applicability of HEPES-AuNPs for SERS measurements on individual functional red blood cells in saline.RSC advances · 2025Article
- A widespread family of ribosomal peptide metallophores involved in bacterial adaptation to metal stress.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Ribosome profiling reveals multiple roles of SecA in cotranslational protein export.Nature communications · 2022Article
- Conformational Control of [2]Rotaxane by Hydrogen Bond.The Journal of organic chemistry · 2022Article
- Biogenesis of hepatitis B virus e antigen is driven by translocon-associated protein complex and regulated by conserved cysteine residues within its signal peptide sequence.The FEBS journal · 2022Article
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Spatial organization of Clostridium difficile S-layer biogenesis.Scientific reports · 2020Article
- The SecA motor generates mechanical force during protein translocation.Nature communications · 2020Article
- Transmembrane protein rotaxanes reveal kinetic traps in the refolding of translocated substrates.Communications biology · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- The Two Distinct Types of SecA2-Dependent Export Systems.Microbiology spectrum · 2019Review
- ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery.eLife · 2019Article
- Substrate Proteins Take Shape at an Improved Bacterial Translocon.Journal of bacteriology · 2019Article
- Evaluating the Functional Pore Size of Chloroplast TOC and TIC Protein Translocons: Import of Folded Proteins.The Plant cell · 2018Article
- Driving Forces of Translocation Through Bacterial Translocon SecYEG.The Journal of membrane biology · 2018Article
- The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.FEMS microbiology letters · 2018Review
- Palladium-Catalyzed Triarylation of spAdvanced synthesis & catalysis · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein translocation in Escherichia coli is mediated by the translocase that in its minimal form consists of the protein-conducting channel SecYEG, and the motor protein, SecA. SecYEG forms a narrow pore in the membrane that allows passage of unfolded proteins only. Molecular dynamics simulations suggest that the maximal width of the central pore of SecYEG is limited to . To access the functional size of the SecYEG pore, the precursor of outer membrane protein A was modified with rigid spherical tetraarylmethane derivatives of different diameters at a unique cysteine residue. SecYEG allowed the unrestricted passage of the precursor of outer membrane protein A conjugates carrying tetraarylmethanes with diameters up to , whereas a sized molecule blocked the translocation pore. Translocation of the protein-organic molecule hybrids was strictly proton motive force-dependent and occurred at a single pore. With an average diameter of an unfolded polypeptide chain of , the pore accommodates structures of at least , which is vastly larger than the predicted maximal width of a single pore by molecular dynamics simulations.
Indexed as
Identifiers
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.