ArticleCell2016
Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery.
Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 248 papers, 1 of them a synthesis that pooled it.
What it found
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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
248 citing papers in PubMed, 1 synthesis or guideline pooled it, 512 citations in OpenAlex.
- A 10-year meta-analysis of membrane protein structural biology: Detergents, membrane mimetics, and structure determination techniques.Biochimica et biophysica acta. Biomembranes · 2021Pooled it
- Cryo-EM sample preparation with soft-landing and laser flash melting.Nature communications · 2026Article
- Protein-DNA Binding Sites Prediction via Integrating Pretrained Large Language Models and Contrastive Learning.Interdisciplinary sciences, computational life sciences · 2026Article
- PCIPG: A comprehensive framework for protein complex identification based on a probabilistic graphical model.PLoS computational biology · 2026Article
- Two datasets are better than one: method of double moments for 3D reconstruction in cryo-EM.Inverse problems · 2026Article
- Cryo-EM: the revolution continues.IUCrJ · 2026Review
- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
- Benchmarking deep learning methods for Cα atom prediction in cryo-EM density maps.Bioinformatics (Oxford, England) · 2026Article
- Harnessing artificial intelligence for antimicrobial discovery and optimization.Current opinion in microbiology · 2026Review
- An improved dataset for predicting mammal infecting viruses from genetic sequence information.PLoS computational biology · 2026Article
- Energy-resolved EBSD using a monolithic direct electron detector.Ultramicroscopy · 2026Article
- Advantages and Limitations of AlphaFold in Structural Biology: Insights from Recent Studies.The protein journal · 2026Review
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Advances in cryo-electron microscopy (cryoEM) for structure-based drug discovery.Expert opinion on drug discovery · 2025Review
- Article
- Improvement in positional accuracy of neural-network predicted hydration sites of proteins by incorporating atomic details of water-protein interactions and site-searching algorithm.Biophysics and physicobiology · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Protein-small molecule binding site prediction based on a pre-trained protein language model with contrastive learning.Journal of cheminformatics · 2024Article
- A head-to-head comparison of MM/PBSA and MM/GBSA in predicting binding affinities for the CBJournal of molecular modeling · 2024Article
- Protein complex structure modeling by cross-modal alignment between cryo-EM maps and protein sequences.Nature communications · 2024Article
188 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
11 authors at 3 institutions in 1 country.
Funding
Abstract
Recent advances in single-particle cryoelecton microscopy (cryo-EM) are enabling generation of numerous near-atomic resolution structures for well-ordered protein complexes with sizes ≥ ∼200 kDa. Whether cryo-EM methods are equally useful for high-resolution structural analysis of smaller, dynamic protein complexes such as those involved in cellular metabolism remains an important question. Here, we present 3.8 Å resolution cryo-EM structures of the cancer target isocitrate dehydrogenase (93 kDa) and identify the nature of conformational changes induced by binding of the allosteric small-molecule inhibitor ML309. We also report 2.8-Å- and 1.8-Å-resolution structures of lactate dehydrogenase (145 kDa) and glutamate dehydrogenase (334 kDa), respectively. With these results, two perceived barriers in single-particle cryo-EM are overcome: (1) crossing 2 Å resolution and (2) obtaining structures of proteins with sizes < 100 kDa, demonstrating that cryo-EM can be used to investigate a broad spectrum of drug-target interactions and dynamic conformational states.
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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.