Evidence map›Paper›PMID 29691408›Full record

ArticleNature communications2018

De novo main-chain modeling for EM maps using MAINMAST.

Genki Terashi, Daisuke Kihara

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
9.7field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 148 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Accurate Macromolecular Complex Modeling for Cryo-EM with CryoZeta.bioRxiv : the preprint server for biology · 2026
    Article
  5. CryoAtom improves model building for cryo-EM.Nature structural & molecular biology · 2026
    Article
  6. EMProt improves structure determination from cryo-EM maps.Nature structural & molecular biology · 2026
    Article
  7. Article
  8. Article
  9. Recognizing amino acid sidechains in a medium-resolution cryo-electron density map.Protein science : a publication of the Protein Society · 2025
    Article
  10. Article
  11. Article
  12. A Labeled Dataset for AI-based Cryo-EM Map Enhancement.bioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. MELD in Action: Harnessing Data to Accelerate Molecular Dynamics.Journal of chemical information and modeling · 2025
    Review
  15. Review
  16. AI-based methods for biomolecular structure modeling for Cryo-EM.Current opinion in structural biology · 2025
    Review
  17. Article
  18. Review
  19. Secondary Structure Detection and Structure Modeling for Cryo-EM.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  20. A labeled dataset for AI-based cryo-EM map enhancement.Computational and structural biotechnology journal · 2025
    Article

16 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 at 1 institution in 1 country.

Genki TerashiDepartment of Biological Sciences, Purdue University, 249S. Martin Jischke Dr., West Lafayette, IN, 47907, USA.ORCID http://orcid.org/0000-0002-5339-909X
Daisuke KiharaDepartment of Biological Sciences, Purdue University, 249S. Martin Jischke Dr., West Lafayette, IN, 47907, USA. dkihara@purdue.edu.ORCID http://orcid.org/0000-0003-4091-6614
Purdue University West Lafayette · US

Funding

Structural Modeling of Multifarious Protein ComplexesR01GM123055 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2017 to 2020
$1.2M
Identification of protein-metabolite interactome.R01GM097528 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM097528NIGMS NIH HHS R01 GM123055
6 · The paper itself

Abstract

An increasing number of protein structures are determined by cryo-electron microscopy (cryo-EM) at near atomic resolution. However, tracing the main-chains and building full-atom models from EM maps of ~4-5 Å is still not trivial and remains a time-consuming task. Here, we introduce a fully automated de novo structure modeling method, MAINMAST, which builds three-dimensional models of a protein from a near-atomic resolution EM map. The method directly traces the protein's main-chain and identifies Cα positions as tree-graph structures in the EM map. MAINMAST performs significantly better than existing software in building global protein structure models on data sets of 40 simulated density maps at 5 Å resolution and 30 experimentally determined maps at 2.6-4.8 Å resolution. In another benchmark of building missing fragments in protein models for EM maps, MAINMAST builds fragments of 11-161 residues long with an average RMSD of 2.68 Å.

Indexed as

Models, MolecularAlgorithmsCryoelectron MicroscopyProtein ConformationProteinsSoftwareProteins

Identifiers

PMID29691408
PMCPMC5915429
OpenAlexW2802061004

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.