Evidence map›Paper›PMID 30005661›Full record

ArticleBMC biotechnology2018

Construction of a trifunctional cellulase and expression in Saccharomyces cerevisiae using a fusion protein.

Zi-Lu Liu, Hua-Nan Li, Hui-Ting Song, Wen-Jing Xiao, Wu-Cheng Xia, Xiao-Peng Liu, Zheng-Bing Jiang

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

8 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Engineering non-P450 3-hydroxylase forSynthetic and systems biotechnology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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

7 authors at 2 institutions in 1 country.

Zi-Lu LiuHubei Key Laboratory of Industrial Biotechnology College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
Hua-Nan LiHubei Key Laboratory of Industrial Biotechnology College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
Hui-Ting SongHubei Key Laboratory of Industrial Biotechnology College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
Wen-Jing XiaoHubei Key Laboratory of Industrial Biotechnology College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
Wu-Cheng XiaHubei Key Laboratory of Industrial Biotechnology College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China.
Xiao-Peng LiuDepartment of Biological Science and Technology, Hubei University for Nationalities, Ensi, 445000, People's Republic of China.
Zheng-Bing JiangHubei Key Laboratory of Industrial Biotechnology College of Life Science, Hubei University, Wuhan, 430062, People's Republic of China. zhbjiang@hubu.edu.cn.ORCID 0000-0002-2089-6401
Hubei University · CNHubei University for Nationalities · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCellulose is the most important component of lignocellulose, and its degradation requires three different types of enzymes to act synergistically. There have been reports of single gene duality, but no gene has been described to have more than two functions. Cloning and expression of fusion cellulases containing more than two kinds of catalytic domains has not been reported thus far.

resultsWe synthesized three different cellulase genes and linked the three catalytic domains with a (G

conclusionsThe trifunctional cellulase BCE was designed based on β-glucosidase BG, endoglucanase EG and exoglucanase CBH, and it possessed β-glucosidase activity, endoglucanase activity and exoglucanase activity simultaneously. The BCE has better filter paper activity, it means the potential practical application.

Indexed as

beta-GlucosidaseCellulaseRecombinant Fusion ProteinsSaccharomyces cerevisiaeCatalytic DomainCelluloseLigninbeta-GlucosidaseCellulaseCelluloseLigninlignocelluloseRecombinant Fusion ProteinsFilter paper enzyme activityLignocelluloseTrifunctional cellulase

Identifiers

PMID30005661
PMCPMC6044064
OpenAlexW2883172530

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.