Evidence map›Paper›PMID 27323404›Full record

ArticleOncotarget2016

iPhos-PseEn: identifying phosphorylation sites in proteins by fusing different pseudo components into an ensemble classifier.

Wang-Ren Qiu, Xuan Xiao, Zhao-Chun Xu, Kuo-Chen Chou

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
21.1field-weighted citation impact, top 1% 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

31 citing papers in PubMed, 149 citations in OpenAlex.

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  5. iN6-methylat (5-step): identifying DNA NMolecular genetics and genomics : MGG · 2019
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  10. LAIPT: Lysine Acetylation Site Identification with Polynomial Tree.International journal of molecular sciences · 2018
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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 3 countries.

Wang-Ren QiuComputer Department, Jingdezhen Ceramic Institute, Jingdezhen, China.
Xuan XiaoComputer Department, Jingdezhen Ceramic Institute, Jingdezhen, China.
Zhao-Chun XuComputer Department, Jingdezhen Ceramic Institute, Jingdezhen, China.
Kuo-Chen ChouGordon Life Science Institute, Boston, MA, USA.
The Gordon Life Science Institute · USJingdezhen Ceramic Institute · CNUniversity of Missouri · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphorylation is a posttranslational modification (PTM or PTLM), where a phosphoryl group is added to the residue(s) of a protein molecule. The most commonly phosphorylated amino acids occur at serine (S), threonine (T), and tyrosine (Y). Protein phosphorylation plays a significant role in a wide range of cellular processes; meanwhile its dysregulation is also involved with many diseases. Therefore, from the angles of both basic research and drug development, we are facing a challenging problem: for an uncharacterized protein sequence containing many residues of S, T, or Y, which ones can be phosphorylated, and which ones cannot? To address this problem, we have developed a predictor called iPhos-PseEn by fusing four different pseudo component approaches (amino acids' disorder scores, nearest neighbor scores, occurrence frequencies, and position weights) into an ensemble classifier via a voting system. Rigorous cross-validations indicated that the proposed predictor remarkably outperformed its existing counterparts. For the convenience of most experimental scientists, a user-friendly web-server for iPhos-PseEn has been established at http://www.jci-bioinfo.cn/iPhos-PseEn, by which users can easily obtain their desired results without the need to go through the complicated mathematical equations involved.

Indexed as

AlgorithmsProtein Processing, Post-TranslationalAmino Acid SequenceBinding SitesComputational BiologyHumansLysinePhosphorylationProtein Interaction Domains and MotifsProtein KinasesProteinsSoftwareLysineProtein KinasesProteinsensemble classifierprotein phosphorylationpseudo componentsrandom forests

Identifiers

PMID27323404
PMCPMC5239474
OpenAlexW2420474086

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.