Evidence map›Paper›PMID 26934646›Full record

ArticleOncotarget2016

Predicting hot spots in protein interfaces based on protrusion index, pseudo hydrophobicity and electron-ion interaction pseudopotential features.

Junfeng Xia, Zhenyu Yue, Yunqiang Di, Xiaolei Zhu, Chun-Hou Zheng

Abstract 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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Nabe: an energetic database of amino acid mutations in protein-nucleic acid binding interfaces.Database : the journal of biological databases and curation · 2021
    Article
  5. Article
  6. Article
  7. Predicting Hot Spot Residues at Protein-DNA Binding Interfaces Based on Sequence Information.Interdisciplinary sciences, computational life sciences · 2021
    Article
  8. Article
  9. Article
  10. Review
  11. 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

5 authors.

Junfeng XiaKey Laboratory of Intelligent Computing and Signal Processing of Ministry of Education, Institute of Health Sciences, Anhui University, Hefei, Anhui 230601, China.
Zhenyu YueSchool of Life Sciences, Anhui University, Hefei, Anhui 230601, China.
Yunqiang DiCollege of Electrical Engineering and Automation, Anhui University, Hefei, Anhui 230601, China.
Xiaolei ZhuSchool of Life Sciences, Anhui University, Hefei, Anhui 230601, China.
Chun-Hou ZhengCo-Innovation Center for Information Supply and Assurance Technology, School of Computer Science and Technology, Anhui University, Hefei, Anhui 230601, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The identification of hot spots, a small subset of protein interfaces that accounts for the majority of binding free energy, is becoming more important for the research of drug design and cancer development. Based on our previous methods (APIS and KFC2), here we proposed a novel hot spot prediction method. For each hot spot residue, we firstly constructed a wide variety of 108 sequence, structural, and neighborhood features to characterize potential hot spot residues, including conventional ones and new one (pseudo hydrophobicity) exploited in this study. We then selected 3 top-ranking features that contribute the most in the classification by a two-step feature selection process consisting of minimal-redundancy-maximal-relevance algorithm and an exhaustive search method. We used support vector machines to build our final prediction model. When testing our model on an independent test set, our method showed the highest F1-score of 0.70 and MCC of 0.46 comparing with the existing state-of-the-art hot spot prediction methods. Our results indicate that these features are more effective than the conventional features considered previously, and that the combination of our and traditional features may support the creation of a discriminative feature set for efficient prediction of hot spots in protein interfaces.

Indexed as

Databases, ProteinProtein Interaction MapsAdenomatous Polyposis Coli ProteinAlgorithmsbeta CateninBinding SitesElectronsErythropoietinHydrophobic and Hydrophilic InteractionsModels, MolecularProtein BindingProtein Interaction Domains and MotifsReceptors, ErythropoietinAdenomatous Polyposis Coli ProteinAPC protein, humanbeta CateninErythropoietinReceptors, Erythropoietincancer driver mutationelectron-ion interaction pseudopotentialhot spotprotrusion indexpseudo hydrophobicity

Identifiers

PMID26934646
PMCPMC4951271

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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.