Evidence map›Paper›PMID 29936543›Full record

ArticleExtremophiles : life under extreme conditions2018

Molecular cloning, expression, and biochemical characterization of a novel cold-active α-amylase from Bacillus sp. dsh19-1.

Shaohua Dou, Naiyu Chi, Xinshang Zhou, Qingfang Zhang, Fei Pang, Zhilong Xiu

Abstract read
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In one paragraph

Article in Extremophiles : life under extreme conditions, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Purification and Characterization of α-Amylase fromCurrent issues in molecular biology · 2026
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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.

Shaohua DouSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, 116024, China.
Naiyu ChiSchool of Life Science and Biotechnology, Dalian University, Dalian, 116622, China. cny7566@126.com.
Xinshang ZhouSchool of Life Science and Biotechnology, Dalian University, Dalian, 116622, China.
Qingfang ZhangSchool of Life Science and Biotechnology, Dalian University, Dalian, 116622, China.
Fei PangSchool of Life Science and Biotechnology, Dalian University, Dalian, 116622, China.
Zhilong XiuSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, 116024, China. zhlxiu@dlut.edu.cn.

Funding

The Natural Science Foundation of Liaoning Province 2014020134
6 · The paper itself

Abstract

A novel gene (ANK58566) encoding a cold-active α-amylase was cloned from marine bacterium Bacillus sp. dsh19-1 (CCTCC AB 2015426), and the protein was expressed in Escherichia coli. The gene had a length of 1302 bp and encoded an α-amylase of 433 amino acids with an estimated molecular mass of 50.1 kDa. The recombinant α-amylase (AmyD-1) showed maximum activity at 20 °C and pH 6.0, and retained about 35.7% of activity at 4 °C. The AmyD-1 activity was stimulated by Ca

Indexed as

alpha-AmylasesCold TemperatureBacillusCalcium Chelating AgentsCloning, MolecularEdetic AcidEnzyme ActivationEnzyme StabilityEscherichia coliGene ExpressionHydrogen-Ion ConcentrationHydrolysisMicrobiological TechniquesProtein EngineeringRecombinant Proteinsalpha-AmylasesCalcium Chelating AgentsEdetic AcidRecombinant ProteinsBacillusBiochemical characterizationCloningCold-activeExpressionα-Amylase

Identifiers

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.