ArticleeLife2016
Assembling the Tat protein translocase.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 70 citations in OpenAlex.
- Structure and substrate recognition by the bacterial twin-arginine translocation (Tat) core complex.Nature microbiology · 2026Article
- Review
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- Aberrant Topologies of Bacterial Membrane Proteins Revealed by High Sensitivity Fluorescence Labelling.Journal of molecular biology · 2024Article
- Defining Assembly Pathways by Fluorescence Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Length matters: Functional flip of the short TatA transmembrane helix.Biophysical journal · 2023Article
- Characterization of a TatA/TatB binding site on the TatC component of theMicrobiology (Reading, England) · 2023Article
- New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon.Molecular microbiology · 2022Article
- Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria.Microbial cell (Graz, Austria) · 2022Review
- Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex.Communications biology · 2022Article
- What have molecular simulations contributed to understanding of Gram-negative bacterial cell envelopes?Microbiology (Reading, England) · 2022Review
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Fates of Sec, Tat, and YidC Translocases in Mitochondria and Other Eukaryotic Compartments.Molecular biology and evolution · 2021Review
- Influence of the TorD signal peptide chaperone on Tat-dependent protein translocation.PloS one · 2021Article
- The Tat system and its dependent cell division proteins are critical for virulence of extra-intestinal pathogenicVirulence · 2020Article
- Targeting of proteins to the twin-arginine translocation pathway.Molecular microbiology · 2020Review
- Surface-exposed domains of TatB involved in the structural and functional assembly of the Tat translocase inThe Journal of biological chemistry · 2019Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- Analysis of haloarchaeal twin-arginine translocase pathway reveals the diversity of the machineries.Heliyon · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The twin-arginine protein translocation system (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membranes of plant chloroplasts. The Tat transporter is assembled from multiple copies of the membrane proteins TatA, TatB, and TatC. We combine sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of
Indexed as
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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.