ReviewThe FEBS journal2013
Cryo-electron microscopy--a primer for the non-microscopist.
Review in The FEBS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 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
92 citing papers in PubMed, 259 citations in OpenAlex.
- Beyond spherical vesicles: morphological diversity of extracellular vesicles in health and disease.Annals of medicine · 2026Review
- The (r)evolution of chemical space and molecular modeling: a time-resolved perspective.Journal of computer-aided molecular design · 2026Review
- CryoPromptSeg: prompt-guided segmentation with integrated denoising for cryo-EM particle picking.Bioinformatics (Oxford, England) · 2026Article
- CryoFSL: an annotation-efficient, few-shot learning framework for robust protein particle picking in cryo-electron microscopy micrographs.Briefings in bioinformatics · 2026Article
- "Green-path": planting seeds for environmental sustainability in diagnostic and research surgical pathology.Virchows Archiv : an international journal of pathology · 2026Review
- Review
- Systematic scale-up and enhanced purification of marine cyanophage P-SSP7.Frontiers in microbiology · 2026Article
- From structural code to immunomodulation: the structure-activity relationship, molecular mechanisms, and translational medicine challenges of yam (Frontiers in immunology · 2026Review
- Exploring the Frontiers of Computational NMR: Methods, Applications, and Challenges.Chemical reviews · 2025Review
- CryoFSL: An Annotation-Efficient, Few-Shot Learning Framework for Robust Protein Particle Picking in Cryo-EM Micrographs.bioRxiv : the preprint server for biology · 2025Article
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- Self-supervised learning for generalizable particle picking in cryo-EM micrographs.Cell reports methods · 2025Article
- Accurate and fast segmentation of filaments and membranes in micrographs and tomograms with TARDIS.bioRxiv : the preprint server for biology · 2025Article
- Unraveling atomic complexity from frozen samples.Structural dynamics (Melville, N.Y.) · 2025Article
- Structure Bioinformatics of Six Human Integral Transmembrane Enzymes and their AlphaFold3 Predicted Water-Soluble QTY Analogs: Insights into FACE1 and STEA4 Binding Mechanisms.Pharmaceutical research · 2025Article
- Balancing speed and precision in protein folding: a comparison of AlphaFold2, ESMFold, and OmegaFold.Frontiers in genetics · 2025Article
- Structural bioinformatic study of human mitochondrial respiratory integral membrane megacomplex and its AlphaFold3 predicted water-soluble QTY megacomplex analog.QRB discovery · 2025Article
- Protein-membrane interactions: sensing and generating curvature.Trends in biochemical sciences · 2024Review
- Article
- Simcryocluster: a semantic similarity clustering method of cryo-EM images by adopting contrastive learning.BMC bioinformatics · 2024Article
32 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
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Cryo-electron microscopy (cryo-EM) is increasingly becoming a mainstream technology for studying the architecture of cells, viruses and protein assemblies at molecular resolution. Recent developments in microscope design and imaging hardware, paired with enhanced image processing and automation capabilities, are poised to further advance the effectiveness of cryo-EM methods. These developments promise to increase the speed and extent of automation, and to improve the resolutions that may be achieved, making this technology useful to determine a wide variety of biological structures. Additionally, established modalities for structure determination, such as X-ray crystallography and nuclear magnetic resonance spectroscopy, are being routinely integrated with cryo-EM density maps to achieve atomic-resolution models of complex, dynamic molecular assemblies. In this review, which is directed towards readers who are not experts in cryo-EM methodology, we provide an overview of emerging themes in the application of this technology to investigate diverse questions in biology and medicine. We discuss the ways in which these methods are being used to study structures of macromolecular assemblies that range in size from whole cells to small proteins. Finally, we include a description of how the structural information obtained by cryo-EM is deposited and archived in a publicly accessible database.
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.