Evidence map›Paper›PMID 22689779›Full record

ArticleBioinformatics (Oxford, England)2012

A conditional neural fields model for protein threading.

Jianzhu Ma, Jian Peng, Sheng Wang, Jinbo Xu

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Protein Structure Prediction Methods.Advances in experimental medicine and biology · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Contact-Assisted Threading in Low-Homology Protein Modeling.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
  9. Article
  10. ProALIGN: Directly Learning Alignments for Protein Structure Prediction via Exploiting Context-Specific Alignment Motifs.Journal of computational biology : a journal of computational molecular cell biology · 2022
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Deep template-based protein structure prediction.PLoS computational biology · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors.

Jianzhu MaToyota Technological Institute at Chicago, IL 60637, USA.
Jian Peng
Sheng Wang
Jinbo Xu

Funding

New Computational Methods for Data-driven Protein Structure PredictionR01GM089753 · NIGMS · TOYOTA TECHNOLOGICAL INSTITUTE / CHICAGO · PI XU, JINBO · 2010 to 2023
$3.8M
NIGMS NIH HHS R01 GM089753NIGMS NIH HHS R01GM0897532
6 · The paper itself

Abstract

motivationAlignment errors are still the main bottleneck for current template-based protein modeling (TM) methods, including protein threading and homology modeling, especially when the sequence identity between two proteins under consideration is low (<30%).

resultsWe present a novel protein threading method, CNFpred, which achieves much more accurate sequence-template alignment by employing a probabilistic graphical model called a Conditional Neural Field (CNF), which aligns one protein sequence to its remote template using a non-linear scoring function. This scoring function accounts for correlation among a variety of protein sequence and structure features, makes use of information in the neighborhood of two residues to be aligned, and is thus much more sensitive than the widely used linear or profile-based scoring function. To train this CNF threading model, we employ a novel quality-sensitive method, instead of the standard maximum-likelihood method, to maximize directly the expected quality of the training set. Experimental results show that CNFpred generates significantly better alignments than the best profile-based and threading methods on several public (but small) benchmarks as well as our own large dataset. CNFpred outperforms others regardless of the lengths or classes of proteins, and works particularly well for proteins with sparse sequence profiles due to the effective utilization of structure information. Our methodology can also be adapted to protein sequence alignment.

Indexed as

AlgorithmsAmino Acid SequenceAmino Acid SubstitutionComputational BiologyLikelihood FunctionsProteinsProtein Structure, SecondarySequence AlignmentSoftwareProteins

Identifiers

PMID22689779
PMCPMC3371845

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.