Evidence map›Paper›PMID 23719418›Full record

ArticleScientific reports2013

Ab Initio structure prediction for Escherichia coli: towards genome-wide protein structure modeling and fold assignment.

Dong Xu, Yang Zhang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Recent Progress of Protein Tertiary Structure Prediction.Molecules (Basel, Switzerland) · 2024
    Review
  2. Article
  3. Article
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  6. Toward the solution of the protein structure prediction problem.The Journal of biological chemistry · 2021
    Review
  7. Article
  8. Selenoprotein N is an endoplasmic reticulum calcium sensor that links luminal calcium levels to a redox activity.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Molecular Modeling of ClonedIndian journal of microbiology · 2017
    Article
  14. Approaches to ab initio molecular replacement of α-helical transmembrane proteins.Acta crystallographica. Section D, Structural biology · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. General overview on structure prediction of twilight-zone proteins.Theoretical biology & medical modelling · 2015
    Review
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 at 2 institutions in 1 country.

Dong XuDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109, USA.
Yang Zhang
University of Michigan–Ann Arbor · USWashtenaw Community College · US

Funding

I-TASSER based atomic-level protein structure predictionR01GM083107 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2008 to 2019
$3.5M
Atomic-level, large-scale structure prediction of G protein-coupled receptorsR01GM084222 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2009 to 2012
$1.3M
NIGMS NIH HHS GM083107NIGMS NIH HHS GM084222NIGMS NIH HHS R01 GM083107NIGMS NIH HHS R01 GM084222
6 · The paper itself

Abstract

Genome-wide protein structure prediction and structure-based function annotation have been a long-term goal in molecular biology but not yet become possible due to difficulties in modeling distant-homology targets. We developed a hybrid pipeline combining ab initio folding and template-based modeling for genome-wide structure prediction applied to the Escherichia coli genome. The pipeline was tested on 43 known sequences, where QUARK-based ab initio folding simulation generated models with TM-score 17% higher than that by traditional comparative modeling methods. For 495 unknown hard sequences, 72 are predicted to have a correct fold (TM-score > 0.5) and 321 have a substantial portion of structure correctly modeled (TM-score > 0.35). 317 sequences can be reliably assigned to a SCOP fold family based on structural analogy to existing proteins in PDB. The presented results, as a case study of E. coli, represent promising progress towards genome-wide structure modeling and fold family assignment using state-of-the-art ab initio folding algorithms.

Indexed as

Escherichia coliModels, MolecularProtein ConformationProtein FoldingSoftwareAlgorithmsBacterial ProteinsBase SequenceComputational BiologyGenome, BacterialInternetMolecular Sequence DataBacterial Proteins

Identifiers

PMID23719418
PMCPMC3667494
OpenAlexW1998728673

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.