Evidence map›Paper›PMID 24961398›Full record

ArticleBMC systems biology2014

Genome-scale analysis of the high-efficient protein secretion system of Aspergillus oryzae.

Lifang Liu, Amir Feizi, Tobias Österlund, Carsten Hjort, Jens Nielsen

Open access · diamondAbstract read
In one paragraph

Article in BMC systems biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Two-Step Engineering of Food-GradeJournal of fungi (Basel, Switzerland) · 2026
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  6. Reconstruction of a Genome-Scale Metabolic Model forInternational journal of molecular sciences · 2025
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  7. Improving recombinant protein secretion inMetabolic engineering communications · 2025
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Silencing ofJournal of fungi (Basel, Switzerland) · 2022
    Article
  15. Membrane Traffic inJournal of fungi (Basel, Switzerland) · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Heterologous expression and functional characterization of the ligand-binding domain of oxysterol-binding protein from Aspergillus oryzae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2019
    Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Lifang Liu
Amir Feizi
Tobias Österlund
Carsten Hjort
Jens NielsenNovo Nordisk Foundation Center for Biosustainability, Department of Chemical and Biologicl Engineering, Chalmers University of Technology, SE-41296 Göteborg, Sweden. nielsenj@chalmers.se.
Chalmers University of Technology · SENovozymes (Denmark) · DKTechnical University of Denmark · DK

Funding

European Research Council 247013
6 · The paper itself

Abstract

backgroundThe koji mold, Aspergillus oryzae is widely used for the production of industrial enzymes due to its particularly high protein secretion capacity and ability to perform post-translational modifications. However, systemic analysis of its secretion system is lacking, generally due to the poorly annotated proteome.

resultsHere we defined a functional protein secretory component list of A. oryzae using a previously reported secretory model of S. cerevisiae as scaffold. Additional secretory components were obtained by blast search with the functional components reported in other closely related fungal species such as Aspergillus nidulans and Aspergillus niger. To evaluate the defined component list, we performed transcriptome analysis on three α-amylase over-producing strains with varying levels of secretion capacities. Specifically, secretory components involved in the ER-associated processes (including components involved in the regulation of transport between ER and Golgi) were significantly up-regulated, with many of them never been identified for A. oryzae before. Furthermore, we defined a complete list of the putative A. oryzae secretome and monitored how it was affected by overproducing amylase.

conclusionIn combination with the transcriptome data, the most complete secretory component list and the putative secretome, we improved the systemic understanding of the secretory machinery of A. oryzae in response to high levels of protein secretion. The roles of many newly predicted secretory components were experimentally validated and the enriched component list provides a better platform for driving more mechanistic studies of the protein secretory pathway in this industrially important fungus.

Indexed as

Genomicsalpha-AmylasesAspergillus oryzaeBatch Cell Culture TechniquesFungal ProteinsGenome, FungalTranscription, Geneticalpha-AmylasesFungal Proteins

Identifiers

PMID24961398
PMCPMC4086290
OpenAlexW2146529013

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.