Evidence map›Paper›PMID 27782050›Full record

ArticleToxins2016

A Combinational Strategy upon RNA Sequencing and Peptidomics Unravels a Set of Novel Toxin Peptides in Scorpion Mesobuthus martensii.

Ning Luan, Wang Shen, Jie Liu, Bo Wen, Zhilong Lin, Shilong Yang, Ren Lai, Siqi Liu, Mingqiang Rong

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.8field-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

4 citing papers in PubMed, 9 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

9 authors at 5 institutions in 1 country.

Ning LuanLife Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China. 15996268076@163.com.
Wang ShenLife Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China. shenwangzs@163.com.
Jie LiuBGI-Shenzhen, Shenzhen 518083, China. liujie8@genomics.cn.
Bo WenBGI-Shenzhen, Shenzhen 518083, China. wenbo@genomics.cn.
Zhilong LinBGI-Shenzhen, Shenzhen 518083, China. linzhilong@genomics.cn.
Shilong YangKey Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences & Yunnan Province, Kunming Institute of Zoology, Kunming 650223, Yunnan, China. yslzoology@163.com.
Ren LaiLife Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China. rlai@mail.kiz.ac.cn.
Siqi LiuBGI-Shenzhen, Shenzhen 518083, China. siqiliu@genomics.cn.
Mingqiang RongKey Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences & Yunnan Province, Kunming Institute of Zoology, Kunming 650223, Yunnan, China. rongmingqiang@mail.kiz.ac.cn.
BGI Group (China) · CNChina National GeneBank · CNKunming Institute of Zoology · CNNanjing Agricultural University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Scorpion venom is deemed to contain many toxic peptides as an important source of natural compounds. Out of the two hundred proteins identified in Mesobuthus martensii (M. martensii), only a few peptide toxins have been found so far. Herein, a combinational approach based upon RNA sequencing and Liquid chromatography-mass spectrometry/mass spectrometry (LC MS/MS) was employed to explore the venom peptides in M. martensii. A total of 153 proteins were identified from the scorpion venom, 26 previously known and 127 newly identified. Of the novel toxins, 97 proteins exhibited sequence similarities to known toxins, and 30 were never reported. Combining peptidomic and transcriptomic analyses, the peptide sequence of BmKKx1 was reannotated and four disulfide bridges were confirmed within it. In light of the comparison of conservation and variety of toxin amino acid sequences, highly conserved and variable regions were perceived in 24 toxins that were parts of two sodium channel and two potassium channel toxins families. Taking all of this evidences together, the peptidomic analysis on M. martensii indeed identified numerous novel scorpion peptides, expanded our knowledge towards the venom diversity, and afforded a set of pharmaceutical candidates.

Indexed as

Amino Acid SequenceAnimalsArthropod ProteinsChromatography, LiquidPeptidesScorpionsScorpion VenomsSequence Analysis, RNASequence Homology, Amino AcidTandem Mass SpectrometryToxins, BiologicalArthropod ProteinsPeptidesScorpion VenomsToxins, Biologicaldiversitypeptidomicsscorpiontoxins

Identifiers

PMID27782050
PMCPMC5086646
OpenAlexW2527972735

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.