Evidence map›Paper›PMID 39251798›Full record

ArticleNature methods2024

MiLoPYP: self-supervised molecular pattern mining and particle localization in situ.

Qinwen Huang, Ye Zhou, Alberto Bartesaghi

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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. In situ cryo-ET visualization of mitochondrial depolarization and mitophagic engulfment.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. bioRxiv : the preprint server for biology · 2025
    Article
  12. Article
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

3 authors.

Qinwen Huang *Department of Computer Science, Duke University, Durham, NC, USA.ORCID http://orcid.org/0000-0002-7082-5257
Ye Zhou *Department of Computer Science, Duke University, Durham, NC, USA.ORCID http://orcid.org/0000-0002-0489-3614
Alberto BartesaghiDepartment of Computer Science, Duke University, Durham, NC, USA. alberto.bartesaghi@duke.edu.ORCID http://orcid.org/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 GM141223Silicon Valley Community Foundation (SVCF) DAF2021-234602U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) U54-AI170752U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM141223
6 · The paper itself

Abstract

Cryo-electron tomography allows the routine visualization of cellular landscapes in three dimensions at nanometer-range resolutions. When combined with single-particle tomography, it is possible to obtain near-atomic resolution structures of frequently occurring macromolecules within their native environment. Two outstanding challenges associated with cryo-electron tomography/single-particle tomography are the automatic identification and localization of proteins, tasks that are hindered by the molecular crowding inside cells, imaging distortions characteristic of cryo-electron tomography tomograms and the sheer size of tomographic datasets. Current methods suffer from low accuracy, demand extensive and time-consuming manual labeling or are limited to the detection of specific types of proteins. Here, we present MiLoPYP, a two-step dataset-specific contrastive learning-based framework that enables fast molecular pattern mining followed by accurate protein localization. MiLoPYP's ability to effectively detect and localize a wide range of targets including globular and tubular complexes as well as large membrane proteins, will contribute to streamline and broaden the applicability of high-resolution workflows for in situ structure determination.

Indexed as

Cryoelectron MicroscopyElectron Microscope TomographyAlgorithmsImage Processing, Computer-AssistedProteinsSoftwareProteins

Identifiers

PMID39251798
PMCPMC11468773

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.