Evidence map›Paper›PMID 37884796›Full record

ArticleNature methods2023

nextPYP: a comprehensive and scalable platform for characterizing protein variability in situ using single-particle cryo-electron tomography.

Hsuan-Fu Liu, Ye Zhou, Qinwen Huang, Jonathan Piland, Weisheng Jin, Justin Mandel, Xiaochen Du, Jeffrey Martin, Alberto Bartesaghi

Abstract read
In one paragraph

Article in Nature methods, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. CoCryoViS: Collaborative online cryo-electron tomography visualization system.Protein science : a publication of the Protein Society · 2026
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  16. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
    Review
  17. Review
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  19. Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025
    Article
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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

9 authors.

Hsuan-Fu Liu *Department of Biochemistry, Duke University, Durham, NC, USA.ORCID 0000-0001-9302-7648
Ye Zhou *Department of Computer Science, Duke University, Durham, NC, USA.ORCID 0000-0002-0489-3614
Qinwen HuangDepartment of Computer Science, Duke University, Durham, NC, USA.ORCID 0000-0002-7082-5257
Jonathan PilandDepartment of Electrical and Computer Engineering, Duke University, Durham, NC, USA.ORCID 0009-0001-1718-9861
Weisheng JinDepartment of Computer Science, Duke University, Durham, NC, USA.
Justin MandelDepartment of Computer Science, Duke University, Durham, NC, USA.
Xiaochen DuDepartment of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.ORCID 0000-0001-6228-0907
Jeffrey MartinDepartment of Computer Science, Duke University, Durham, NC, USA.
Alberto BartesaghiDepartment of Biochemistry, Duke University, Durham, NC, USA. alberto.bartesaghi@duke.edu.ORCID 0000-0002-7360-1523

Funding

Project 3 - Dynamics of latent HIV-1 reservoirs: High resolution antigenic mapping and strategies to block reboundU54AI170752 · NIAID · DUKE UNIVERSITY · PI Derek Wilson Cain · 2022 to 2026
$32.0M
A Computational Platform for In-Situ Structure Determination at Near-Atomic Resolution using Cryo-Electron TomographyR01GM141223 · NIGMS · DUKE UNIVERSITY · PI BARTESAGHI, ALBERTO · 2021 to 2024
$1.5M
NIAID NIH HHS U54 AI170752NIGMS NIH HHS R01 GM141223
6 · The paper itself

Abstract

Single-particle cryo-electron tomography is an emerging technique capable of determining the structure of proteins imaged within the native context of cells at molecular resolution. While high-throughput techniques for sample preparation and tilt-series acquisition are beginning to provide sufficient data to allow structural studies of proteins at physiological concentrations, the complex data analysis pipeline and the demanding storage and computational requirements pose major barriers for the development and broader adoption of this technology. Here, we present a scalable, end-to-end framework for single-particle cryo-electron tomography data analysis from on-the-fly pre-processing of tilt series to high-resolution refinement and classification, which allows efficient analysis and visualization of datasets with hundreds of tilt series and hundreds of thousands of particles. We validate our approach using in vitro and cellular datasets, demonstrating its effectiveness at achieving high-resolution and revealing conformational heterogeneity in situ. The framework is made available through an intuitive and easy-to-use computer application, nextPYP ( http://nextpyp.app ).

Indexed as

Electron Microscope TomographySoftwareCryoelectron MicroscopyImage Processing, Computer-AssistedProteinsProteins

Identifiers

PMID37884796
PMCPMC10703682

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LicenceCC BY
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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.