Evidence map›Paper›PMID 31878333›Full record

ReviewMolecules (Basel, Switzerland)2019

Advances in Structure Modeling Methods for Cryo-Electron Microscopy Maps.

Eman Alnabati, Daisuke Kihara

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Secondary Structure Detection and Structure Modeling for Cryo-EM.Methods in molecular biology (Clifton, N.J.) · 2025
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  17. Deep Learning-Based Advances in Protein Structure Prediction.International journal of molecular sciences · 2021
    Review
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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.

Eman AlnabatiDepartment of Computer Science, Purdue University, West Lafayette, IN 47907, USA.
Daisuke KiharaDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.

Funding

Structural Modeling of Multifarious Protein ComplexesR01GM123055 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2017 to 2020
$1.2M
National Science Foundation CMMI1825941National Science Foundation DMS1614777National Science Foundation MCB1925643NIGMS NIH HHS R01 GM123055NIH HHS R01GM123055
6 · The paper itself

Abstract

Cryo-electron microscopy (cryo-EM) has now become a widely used technique for structure determination of macromolecular complexes. For modeling molecular structures from density maps of different resolutions, many algorithms have been developed. These algorithms can be categorized into rigid fitting, flexible fitting, and de novo modeling methods. It is also observed that machine learning (ML) techniques have been increasingly applied following the rapid progress of the ML field. Here, we review these different categories of macromolecule structure modeling methods and discuss their advances over time.

Indexed as

Cryoelectron MicroscopyModels, MolecularAlgorithmsMachine Learningcryo-electron microscopycryo-EMde novo modelingdensity mapmachine learning methodsprotein modelingstructure fitting algorithms

Identifiers

PMID31878333
PMCPMC6982917

What OpenQuestion holds

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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.