ReviewMolecular microbiology2020
Targeting of proteins to the twin-arginine translocation pathway.
Review in Molecular microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 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
46 citing papers in PubMed, 79 citations in OpenAlex.
- Enhancing the Secretion Systems: Genetic Engineering of Super Bioagents for Effective Plant Disease Control.Biotechnology and bioengineering · 2026Review
- Adaptations in electron transport chain complexes of clinical Rhodococcus equi revealed through comparative genomics.World journal of microbiology & biotechnology · 2026Article
- Molecular basis of type VI secretion system effector loading.Nature microbiology · 2026Article
- Twin-arginine transport complex plays an essential role inMolecular biology of the cell · 2026Article
- Repurposing the bacterial surface display technology for drug delivery.Advanced drug delivery reviews · 2025Review
- Article
- Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025Article
- Phylogenomics Untangles the Metabolic Potential of Picochlorum tauri, a New Picoalgal Species Causing a Winter Bloom in the Mediterranean Thau Lagoon.Environmental microbiology · 2025Article
- Bacterial Systems as a Precision Delivery Platform of Therapeutic Peptides for Cancer Therapy.Polymer science & technology (Washington, D.C.) · 2025Review
- Signal Peptides: From Molecular Mechanisms to Applications in Protein and Vaccine Engineering.Biomolecules · 2025Review
- Cleavage cascade of the sigma regulator FecR orchestrates TonB-dependent signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Advancements in Escherichia coli secretion systems for enhanced recombinant protein production.World journal of microbiology & biotechnology · 2025Review
- Isolation of PCSK9-specific nanobodies from synthetic libraries using a combined protein selection strategy.Scientific reports · 2025Article
- The Glycoworld: Glycoproteins in Nature: A General Overview of the Different Roles That Glycoproteins Exert in Living Organism.Methods in molecular biology (Clifton, N.J.) · 2025Review
- The twin-arginine translocation system is vital for cell adhesion and uptake of iron in the cystic fibrosis pathogenVirulence · 2024Article
- Parameter-efficient fine-tuning on large protein language models improves signal peptide prediction.Genome research · 2024Article
- The Freshwater CyanobacteriumPlants (Basel, Switzerland) · 2024Article
- N-Terminal Sequences of Signal Peptides Assuming Critical Roles in Expression of Heterologous Proteins inMicroorganisms · 2024Article
- Bacillus subtilis: current and future modification strategies as a protein secreting factory.World journal of microbiology & biotechnology · 2024Review
- An essential and highly selective protein import pathway encoded by nucleus-forming phage.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The twin-arginine protein transport (Tat pathway) is found in prokaryotes and plant organelles and transports folded proteins across membranes. Targeting of substrates to the Tat system is mediated by the presence of an N-terminal signal sequence containing a highly conserved twin-arginine motif. The Tat machinery comprises membrane proteins from the TatA and TatC families. Assembly of the Tat translocon is dynamic and is triggered by the interaction of a Tat substrate with the Tat receptor complex. This review will summarise recent advances in our understanding of Tat transport, focusing in particular on the roles played by Tat signal peptides in protein targeting and translocation.
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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.