Evidence map›Paper›PMID 24865376›Full record

ArticleScientific reports2014

Investigating the impact of Asp181 point mutations on interactions between PTP1B and phosphotyrosine substrate.

Mengyuan Liu, Lushan Wang, Xun Sun, Xian Zhao

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 48 citations in OpenAlex.

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  12. Impact of point mutation P29S in RAC1 on tumorigenesis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
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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

4 authors at 3 institutions in 1 country.

Mengyuan LiuState Key Laboratory of Crystal Materials, Shandong University, Jinan 250100, China.
Lushan WangState Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China.
Xun SunState Key Laboratory of Crystal Materials, Shandong University, Jinan 250100, China.
Xian ZhaoState Key Laboratory of Crystal Materials, Shandong University, Jinan 250100, China.
Shandong University · CNState Key Laboratory of Crystal MaterialsState Key Laboratory of Microbial Technology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein tyrosine phosphatase 1B (PTP1B) is a key negative regulator of insulin and leptin signaling, which suggests that it is an attractive therapeutic target in type II diabetes and obesity. The aim of this research is to explore residues which interact with phosphotyrosine substrate can be affected by D181 point mutations and lead to increased substrate binding. To achieve this goal, molecular dynamics simulations were performed on wild type (WT) and two mutated PTP1B/substrate complexes. The cross-correlation and principal component analyses show that point mutations can affect the motions of some residues in the active site of PTP1B. Moreover, the hydrogen bond and energy decomposition analyses indicate that apart from residue 181, point mutations have influence on the interactions of substrate with several residues in the active site of PTP1B.

Indexed as

Binding SitesCatalytic DomainDiabetes Mellitus, Type 2HumansHydrogen BondingInsulinLeptinMolecular Dynamics SimulationPhosphotyrosinePoint MutationProtein Tyrosine Phosphatase, Non-Receptor Type 1Signal TransductionSubstrate SpecificityInsulinLeptinPhosphotyrosineProtein Tyrosine Phosphatase, Non-Receptor Type 1PTPN1 protein, human

Identifiers

PMID24865376
PMCPMC4035576
OpenAlexW2075803307

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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.