Evidence map›Paper›PMID 22045506›Full record

ArticleJournal of computational chemistry2012

SPINE X: improving protein secondary structure prediction by multistep learning coupled with prediction of solvent accessible surface area and backbone torsion angles.

Eshel Faraggi, Tuo Zhang, Yuedong Yang, Lukasz Kurgan, Yaoqi Zhou

Abstract readValidation Study
In one paragraph

Article in Journal of computational chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed, 1 pooled it
–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

104 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Sequence-Based Prediction for Protein Solvent Accessibility.International journal of molecular sciences · 2025
    Article
  3. AlphaFold2, SPINE-X, and Seder on Four Hard CASP Targets.Methods in molecular biology (Clifton, N.J.) · 2025
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  5. Review
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  10. ProFeatX: A parallelized protein feature extraction suite for machine learning.Computational and structural biotechnology journal · 2023
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44 more citing papers are in PubMed but not listed here.

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.

Eshel FaraggiSchool of Informatics, Indiana University Purdue University, Indianapolis, Indiana, USA.
Tuo Zhang
Yuedong Yang
Lukasz Kurgan
Yaoqi Zhou

Funding

Toward experimental quality protein structures: a synergistic approachR01GM067168 · NIGMS · UNIVERSITY OF DELAWARE · PI DUAN, YONG, ZHOU, YAOQI · 2003 to 2012
$2.4M
Statistical Energy Functions: a Fragment-based ApproachR01GM085003 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI ZHOU, YAOQI · 2008 to 2011
$1.1M
NIGMS NIH HHS GM 067168NIGMS NIH HHS GM 085003NIGMS NIH HHS R01 GM067168NIGMS NIH HHS R01 GM085003
6 · The paper itself

Abstract

Accurate prediction of protein secondary structure is essential for accurate sequence alignment, three-dimensional structure modeling, and function prediction. The accuracy of ab initio secondary structure prediction from sequence, however, has only increased from around 77 to 80% over the past decade. Here, we developed a multistep neural-network algorithm by coupling secondary structure prediction with prediction of solvent accessibility and backbone torsion angles in an iterative manner. Our method called SPINE X was applied to a dataset of 2640 proteins (25% sequence identity cutoff) previously built for the first version of SPINE and achieved a 82.0% accuracy based on 10-fold cross validation (Q(3)). Surpassing 81% accuracy by SPINE X is further confirmed by employing an independently built test dataset of 1833 protein chains, a recently built dataset of 1975 proteins and 117 CASP 9 targets (critical assessment of structure prediction techniques) with an accuracy of 81.3%, 82.3% and 81.8%, respectively. The prediction accuracy is further improved to 83.8% for the dataset of 2640 proteins if the DSSP assignment used above is replaced by a more consistent consensus secondary structure assignment method. Comparison to the popular PSIPRED and CASP-winning structure-prediction techniques is made. SPINE X predicts number of helices and sheets correctly for 21.0% of 1833 proteins, compared to 17.6% by PSIPRED. It further shows that SPINE X consistently makes more accurate prediction in helical residues (6%) without over prediction while PSIPRED makes more accurate prediction in coil residues (3-5%) and over predicts them by 7%. SPINE X Server and its training/test datasets are available at http://sparks.informatics.iupui.edu/

Indexed as

Neural Networks, ComputerProteinsProtein Structure, SecondarySolventsProteinsSolvents

Identifiers

PMID22045506
PMCPMC3240697

What OpenQuestion holds

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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.