Evidence map›Paper›PMID 38066344›Full record

ArticleNature methods2024

DeepMainmast: integrated protocol of protein structure modeling for cryo-EM with deep learning and structure prediction.

Genki Terashi, Xiao Wang, Devashish Prasad, Tsukasa Nakamura, Daisuke Kihara

Abstract read
In one paragraph

Article in Nature methods, 2024. 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. Article
  2. Article
  3. Article
  4. AI-Physics-Experiment Trinity for Integrated Protein Dynamics Modeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Article
  6. Article
  7. Accurate Macromolecular Complex Modeling for Cryo-EM with CryoZeta.bioRxiv : the preprint server for biology · 2026
    Article
  8. When cryo-EM modeling meets structure prediction.Nature structural & molecular biology · 2026
    Article
  9. CryoAtom improves model building for cryo-EM.Nature structural & molecular biology · 2026
    Article
  10. EMProt improves structure determination from cryo-EM maps.Nature structural & molecular biology · 2026
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Genki TerashiDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0000-0002-5339-909X
Xiao WangDepartment of Computer Science, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0000-0003-4435-7098
Devashish PrasadDepartment of Computer Science, Purdue University, West Lafayette, IN, USA.
Tsukasa NakamuraDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA.ORCID http://orcid.org/0000-0002-6312-3070
Daisuke KiharaDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA. dkihara@purdue.edu.ORCID http://orcid.org/0000-0003-4091-6614

Funding

Building protein structure models for intermediate resolution cryo-electron microscopy mapsR01GM133840 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2020 to 2023
$1.6M
National Science Foundation (NSF) CMMI1825941National Science Foundation (NSF) DBI2003635National Science Foundation (NSF) DBI2146026National Science Foundation (NSF) DMS2151678National Science Foundation (NSF) IIS2211598National Science Foundation (NSF) MCB1925643NIGMS NIH HHS R01 GM133840U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM133840
6 · The paper itself

Abstract

Three-dimensional structure modeling from maps is an indispensable step for studying proteins and their complexes with cryogenic electron microscopy. Although the resolution of determined cryogenic electron microscopy maps has generally improved, there are still many cases where tracing protein main chains is difficult, even in maps determined at a near-atomic resolution. Here we developed a protein structure modeling method, DeepMainmast, which employs deep learning to capture the local map features of amino acids and atoms to assist main-chain tracing. Moreover, we integrated AlphaFold2 with the de novo density tracing protocol to combine their complementary strengths and achieved even higher accuracy than each method alone. Additionally, the protocol is able to accurately assign the chain identity to the structure models of homo-multimers, which is not a trivial task for existing methods.

Indexed as

Deep LearningCryoelectron MicroscopyMicroscopy, ElectronModels, MolecularProtein ConformationProteinsProteins

Identifiers

PMID38066344
PMCPMC12815591

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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.