Evidence map›Paper›PMID 29142737›Full record

ArticleCell & bioscience2017

Cloning, expression and identification of KTX-Sp4, a selective Kv1.3 peptidic blocker from

Yan Zou, Feng Zhang, Yaxian Li, Yuanfang Wang, Yi Li, Zhengtao Long, Shujuan Shi, Li Shuai, Jiukai Liu, Zhiyong Di and 1 more

Open access · goldAbstract read
In one paragraph

Article in Cell & bioscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Article
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

11 authors at 2 institutions in 1 country.

Yan Zou *School of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Feng Zhang *School of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Yaxian LiSchool of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Yuanfang WangSchool of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Yi LiSchool of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Zhengtao LongSchool of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Shujuan ShiSchool of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Li ShuaiSchool of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Jiukai LiuSchool of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
Zhiyong DiSchool of Life Sciences, University of Science and Technology of China, Hefei, 230027 People's Republic of China.
Shijin YinSchool of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, 430074 People's Republic of China.
South Central University for Nationalities · CNUniversity of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSpecific and selective peptidic blockers of Kv1.3 channels can serve as a valuable drug lead for treating T cell-mediated autoimmune diseases, and scorpion venom is an important source of kv1.3 channel inhibitors. Through conducting transcriptomic sequencing for the venom gland of

resultsWe screened out a new peptide toxin KTX-Sp4 which had 43 amino acids including six cysteine residues. Electrophysiological experiments indicated that recombinant expression products of KTX-Sp4 blocked both endogenous and exogenous Kv1.3 channel concentration-dependently, and exhibited good selectivity on Kv1.3 over Kv1.1, Kv1.2, respectively. Mutation experiments showed that the Kv1 turret region was responsible for the selectivity of KTX-Sp4 peptide on Kv1.3 over Kv1.1.

conclusionsThis work not only provided a novel lead compound for the development of anti autoimmune disease drugs, but also enriched the molecular basis for the interaction between scorpion toxins and potassium channels, serving as an important theoretical basis for designing high selective Kv1.3 peptide inhibitors.

Indexed as

Channel turretKv1.3Peptide KTX-Sp4Scorpiops pocockiSelectivity

Identifiers

PMID29142737
PMCPMC5674823
OpenAlexW2767655768

What OpenQuestion holds

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Registered trials

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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.