ArticleNature methods2020
Bottom-up structural proteomics: cryoEM of protein complexes enriched from the cellular milieu.
Article in Nature methods, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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.
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.
Who cites it
87 citing papers in PubMed.
- Ghost Neuron preparation unlocks high-resolution structural mapping of intracellular architecture in axons.Nature communications · 2026Article
- Article
- Article
- Article
- Confidence-guided cryo-EM map optimisation with LocScale-2.0.Nature communications · 2026Article
- Visual exoproteomics ofbioRxiv : the preprint server for biology · 2026Article
- Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Discovery and cryoEM structure of FPM13, a periplasmic metalloprotein unique to Francisella.PLoS pathogens · 2026Article
- Structure first - exploration and discovery with cryo-electron microscopy.Journal of cell science · 2026Review
- Cytochrome nanowires under electron microscopy.Emerging topics in life sciences · 2026Review
- A dramatic protein fold switch powers a bactericidal nanomachine.bioRxiv : the preprint server for biology · 2026Article
- Serendipity and the Slime Mold: A Visual Survey of High-Molecular-Weight Protein Assemblies Reveals the Structure of the Polyketide Synthase Pks16.Molecular & cellular proteomics : MCP · 2026Article
- Integrating multi-omics data to reveal the host-microbiota interactome in inflammatory bowel disease.Gut microbes · 2025Review
- Structure, identification, and characterization of the RibD-enolase complex in Francisella.Protein & cell · 2025Article
- Visualizing the translation landscape in human cells at high resolution.Nature communications · 2025Article
- Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025Review
- The CAGE complex: a hollow, megadalton, protein assembly in prokaryotic and eukaryotic microbes.bioRxiv : the preprint server for biology · 2025Article
- CryoDataBot: a pipeline to curate cryoEM datasets for AI-driven structural biology.bioRxiv : the preprint server for biology · 2025Article
- CryoEM-enabled visual proteomics reveals de novo structures of oligomeric protein complexes.Structure (London, England : 1993) · 2025Article
- Review
27 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
X-ray crystallography often requires non-native constructs involving mutations or truncations, and is challenged by membrane proteins and large multicomponent complexes. We present here a bottom-up endogenous structural proteomics approach whereby near-atomic-resolution cryo electron microscopy (cryoEM) maps are reconstructed ab initio from unidentified protein complexes enriched directly from the endogenous cellular milieu, followed by identification and atomic modeling of the proteins. The proteins in each complex are identified using cryoID, a program we developed to identify proteins in ab initio cryoEM maps. As a proof of principle, we applied this approach to the malaria-causing parasite Plasmodium falciparum, an organism that has resisted conventional structural-biology approaches, to obtain atomic models of multiple protein complexes implicated in intraerythrocytic survival of the parasite. Our approach is broadly applicable for determining structures of undiscovered protein complexes enriched directly from endogenous sources.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.