Evidence map›Paper›PMID 32850115›Full record

ArticleToxicology research2020

Exploring the influence of silver and lead on structure and function of xylanase: spectroscopic and calorimetric methods.

Mingyang Jing, Rui Tang, Guangye Han, Shansheng Zhang, Rutao Liu

Open access · bronzeAbstract read
In one paragraph

Article in Toxicology research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 56% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 1 country.

Mingyang JingSchool of Environmental Science and Engineering, Shandong University, America CRC for Environment & Health, 72# Jimo Binhai Road, Qingdao, Shandong 266237, P.R. China.
Rui TangSchool of Environmental Science and Engineering, Shandong University, America CRC for Environment & Health, 72# Jimo Binhai Road, Qingdao, Shandong 266237, P.R. China.
Guangye HanShandong Academy of Environmental Sciences Co., Ltd, Lixia, 50# Lishan Road, Jinan, Shandong 250100, P.R. China.
Shansheng ZhangPenglai Jiaxin Dye Chemical Co., Ltd, 1#Jiaxin Road, Yantai, Shandong 265601, P.R. China.
Rutao LiuSchool of Environmental Science and Engineering, Shandong University, America CRC for Environment & Health, 72# Jimo Binhai Road, Qingdao, Shandong 266237, P.R. China.
Shandong University · CNShandong Academy of Environmental Science · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Soil contamination with heavy metal could induce the alteration of soil ecological environments, and soil enzyme activities are sensitive indicators for the soil toxicology. Xylanase is one of predominant soil enzymes related to carbon nitrogen cycle. In this work, we explored the underlying mechanisms for conformational and enzymatic activity alterations of xylanase after silver and lead exposure at molecular level with systematical measurements including multiple spectroscopic methods, isothermal titration calorimetry, and enzymatic activity. Both silver and lead could loosen and unfold the skeleton of xylanase with the quenching of endogenous fluorescence. Silver interacted with xylanase forming larger-size aggregations through Van der Waals forces and hydrogen bonding, while lead interacted with xylanase forming larger-size aggregations through hydrophobic force. Silver and lead induced an obvious loss (67.1 and 56.31%) of the xylanase enzymatic activity, but silver has a greater impact on xylanase than that of lead. The xylanase enzymatic activity significantly decreased due to the conformational alterations. The negative effect of silver exposure on xylanase structure and function was more prominent than that of lead.

Indexed as

calorimetryleadsilverspectroscopic methodsxylanase

Identifiers

PMID32850115
PMCPMC7438702
OpenAlexW3022370481

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.