ReviewBiochemistry2007
Interactions that drive Sec-dependent bacterial protein transport.
Review in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed, 78 citations in OpenAlex.
- Article
- Lipoprotein Signal Peptide as Adjuvants: Leveraging Lipobox-Driven TLR2 Activation in Modern Vaccine Design.Vaccines · 2025Review
- Comparative Secretory Efficiency of Two Chitosanase Signal Peptides from Bacillus subtilis in Escherichia coli.Journal of microbiology (Seoul, Korea) · 2024Article
- Analysis of protein secretion in Bacillus subtilis by combining a secretion stress biosensor strain with an in vivo split GFP assay.Microbial cell factories · 2023Article
- Bioengineering of Antibody Fragments: Challenges and Opportunities.Bioengineering (Basel, Switzerland) · 2023Review
- Functional annotation of rhizospheric phageome of the wild plant speciesFrontiers in microbiology · 2023Article
- Insights into the Influence of Signal Peptide on the Enzymatic Properties of Alginate Lyase AlyI1 with Removal Effect onMarine drugs · 2022Article
- The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.FEMS microbiology reviews · 2022Review
- TISIGNER.com: web services for improving recombinant protein production.Nucleic acids research · 2021Article
- Article
- Biosensor-Based Optimization of Cutinase Secretion byFrontiers in microbiology · 2021Article
- Plastid chaperone HSP90C guides precursor proteins to the SEC translocase for thylakoid transport.Journal of experimental botany · 2020Article
- Analyzing Signal Peptides for Secretory Production of Recombinant Diagnostic Antigen B8/1 fromMolecular biology research communications · 2020Article
- A secretion biosensor for monitoring Sec-dependent protein export in Corynebacterium glutamicum.Microbial cell factories · 2020Article
- Article
- Exploitation of Bacillus subtilis as a robust workhorse for production of heterologous proteins and beyond.World journal of microbiology & biotechnology · 2018Review
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- Signal peptides for recombinant protein secretion in bacterial expression systems.Microbial cell factories · 2018Review
- Site-saturation mutagenesis of mutant L-asparaginase II signal peptide hydrophobic region for improved excretion of cyclodextrin glucanotransferase.Journal of industrial microbiology & biotechnology · 2017Article
- Comparative Transcriptome Analysis of Vibrio splendidus JZ6 Reveals the Mechanism of Its Pathogenicity at Low Temperatures.Applied and environmental microbiology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Understanding the transport of hydrophilic proteins across biological membranes continues to be an important undertaking. The general secretory (Sec) pathway in Escherichia coli transports the majority of E. coli proteins from their point of synthesis in the cytoplasm to their sites of final localization, associating sequentially with a number of protein components of the transport machinery. The targeting signals for these substrates must be discriminated from those of proteins transported via other pathways. While targeting signals for each route have common overall characteristics, individual signal peptides vary greatly in their amino acid sequences. How do these diverse signals interact specifically with the proteins that comprise the appropriate transport machinery and, at the same time, avoid targeting to an alternate route? The recent publication of the crystal structures of components of the Sec transport machinery now allows a more thorough consideration of the interactions of signal sequences with these components.
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.