Evidence map›Paper›PMID 15126668›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Automated structure prediction of weakly homologous proteins on a genomic scale.

Yang Zhang, Jeffrey Skolnick

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 158 papers.

0numbers the graph read from it
0cells of the map it votes in
158citing 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

158 citing papers in PubMed.

  1. Article
  2. Review
  3. The physics-AI dialogue in drug design.RSC medicinal chemistry · 2025
    Review
  4. Review
  5. Article
  6. Recent Progress of Protein Tertiary Structure Prediction.Molecules (Basel, Switzerland) · 2024
    Review
  7. De novo protein fold design through sequence-independent fragment assembly simulations.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Toward the solution of the protein structure prediction problem.The Journal of biological chemistry · 2021
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

98 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

2 authors.

Yang ZhangCenter of Excellence in Bioinformatics, University at Buffalo, 901 Washington Street, Buffalo, NY 14203, USA.
Jeffrey Skolnick

Funding

Interaction Pattern Based Predictor of Protein StruturesR01GM048835 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SKOLNICK, JEFFREY · 1994 to 2015
$4.0M
THEORY OF FOLDING TRANSITIONS IN A-HELICAL PROTEINSR01GM037408 · NIGMS · WASHINGTON UNIVERSITY · PI SKOLNICK, JEFFREY · 1987 to 2014
$3.9M
NIGMS NIH HHS GM-37408NIGMS NIH HHS GM-48835NIGMS NIH HHS R01 GM037408NIGMS NIH HHS R01 GM048835
6 · The paper itself

Abstract

We have developed TASSER, a hierarchical approach to protein structure prediction that consists of template identification by threading, followed by tertiary structure assembly via the rearrangement of continuous template fragments guided by an optimized C(alpha) and side-chain-based potential driven by threading-based, predicted tertiary restraints. TASSER was applied to a comprehensive benchmark set of 1,489 medium-sized proteins in the Protein Data Bank. With homologues excluded, in 927 cases, the templates identified by our threading algorithm PROSPECTOR_3 have a rms deviation from native <6.5 A with approximately 80% alignment coverage. After template reassembly, this number increases to 1,172. This shows significant and systematic improvement of the final models with respect to the initial template alignments. Furthermore, significant improvements in loop modeling are demonstrated. We then apply TASSER to the 1,360 medium-sized ORFs in the Escherichia coli genome; approximately 920 can be predicted with high accuracy based on confidence criteria established in the Protein Data Bank benchmark. These results from our unprecedented comprehensive folding benchmark on all protein categories provide a reliable basis for the application of TASSER to structural genomics, especially to proteins of low sequence identity to solved protein structures.

Indexed as

Structural Homology, ProteinAlgorithmsElectronic Data ProcessingEscherichia coliModels, MolecularMonte Carlo MethodProtein ConformationProtein FoldingProteinsProteins

Identifiers

PMID15126668
PMCPMC419651

What OpenQuestion holds

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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.