Evidence map›Paper›PMID 30626119›Full record

ArticleInternational journal of molecular sciences2019

Molecular Dynamics Simulations of Wild Type and Mutants of SAPAP in Complexed with Shank3.

Lianhua Piao, Zhou Chen, Qiuye Li, Ranran Liu, Wei Song, Ren Kong, Shan Chang

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 63 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

7 authors at 1 institution in 1 country.

Lianhua PiaoInstitute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, Changzhou 213001, China. lianhuapiao@jsut.edu.cn.
Zhou ChenInstitute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, Changzhou 213001, China. chenzhou@jsut.edu.cn.
Qiuye LiInstitute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, Changzhou 213001, China. youer99311216@jsut.edu.cn.
Ranran LiuInstitute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, Changzhou 213001, China. lrr@jsut.edu.cn.
Wei SongInstitute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, Changzhou 213001, China. dxxsw@jsut.edu.cn.
Ren KongInstitute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, Changzhou 213001, China. rkong@jsut.edu.cn.ORCID 0000-0001-9010-1750
Shan ChangInstitute of Bioinformatics and Medical Engineering, School of Electrical and Information Engineering, Jiangsu University of Technology, Changzhou 213001, China. schang@jsut.edu.cn.ORCID 0000-0001-7169-9398
Jiangsu University of Technology · CN

Funding

Jiangsu Education Department 16KJD310001National Natural Science Foundation of China 81603152Six Talent Peaks Project in Jiangsu Province 2016-XYDXXJS-020
6 · The paper itself

Abstract

Specific interactions between scaffold protein SH3 and multiple ankyrin repeat domains protein 3 (Shank3) and synapse-associated protein 90/postsynaptic density-95⁻associated protein (SAPAP) are essential for excitatory synapse development and plasticity. In a bunch of human neurological diseases, mutations on Shank3 or SAPAP are detected. To investigate the dynamical and thermodynamic properties of the specific binding between the N-terminal extended PDZ (Post-synaptic density-95/Discs large/Zonaoccludens-1) domain (N-PDZ) of Shank3 and the extended PDZ binding motif (E-PBM) of SAPAP, molecular dynamics simulation approaches were used to study the complex of N-PDZ with wild type and mutated E-PBM peptides. To compare with the experimental data,

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceDisks Large Homolog 4 ProteinHydrogen BondingMutant ProteinsNerve Tissue ProteinsPDZ DomainsProtein BindingThermodynamicsDisks Large Homolog 4 ProteinMutant ProteinsNerve Tissue Proteinsconformational changefree energy calculationmolecular dynamics simulationShank3 and SAPAP interactions

Identifiers

PMID30626119
PMCPMC6337207
OpenAlexW2910882956

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.