Evidence map›Paper›PMID 29871927›Full record

ArticleThe Journal of biological chemistry2018

Structural insights into the catalytic mechanism of a novel glycoside hydrolase family 113 β-1,4-mannanase from

Xin You, Zhen Qin, Qiaojuan Yan, Shaoqing Yang, Yanxiao Li, Zhengqiang Jiang

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 18 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Xin YouFrom the Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Engineering, China Agricultural University, Beijing 100083.
Zhen Qinthe School of Biotechnology, State Key Laboratory of Bioreactor Engineering, R&D Center of Separation and Extraction Technology in Fermentation Industry, East China University of Science and Technology, Shanghai 200237, and.
Qiaojuan YanFrom the Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Engineering, China Agricultural University, Beijing 100083.
Shaoqing Yangthe College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
Yanxiao LiFrom the Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Engineering, China Agricultural University, Beijing 100083.
Zhengqiang Jiangthe College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China zhqjiang@cau.edu.cn.
China Agricultural University · CNEast China University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-1,4-Mannanase degrades β-1,4-mannan polymers into manno-oligosaccharides with a low degree of polymerization. To date, only one glycoside hydrolase (GH) family 113 β-1,4-mannanase, from

Indexed as

Amino Acid SequenceBacillaceaebeta-MannosidaseCatalytic DomainCrystallography, X-RayMannansModels, MolecularOligosaccharidesProtein ConformationSequence AlignmentSubstrate SpecificityTrisaccharidesbeta-MannosidaseMannansmannobiosemannopentaosemannotrioseOligosaccharidesTrisaccharidesComplex structureendo-β-1,4-mannanaseenzyme catalysisenzyme mechanismenzyme structureGH family 113 catalytic mechanismprotein designRational designX-ray crystallography

Identifiers

PMID29871927
PMCPMC6066303
OpenAlexW2806378002

What OpenQuestion holds

Textmetadata
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.