ArticleeLife2014
Sequence co-evolution gives 3D contacts and structures of protein complexes.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 265 papers, 1 of them a synthesis that pooled 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.
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
265 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Meta-analysis defines principles for the design and analysis of co-fractionation mass spectrometry experiments.Nature methods · 2021Pooled it
- Structures of the Xcp and Hxc T2SS endopili provide new insights into type IV pili subfamilies.Structure (London, England : 1993) · 2026Article
- Pocket restraints guided by B-cell epitope prediction improve Chai-1 antibody-antigen structure modeling.Protein science : a publication of the Protein Society · 2026Article
- Structure and evolution-guided design of minimal RNA-guided nucleases.Science (New York, N.Y.) · 2026Article
- Evolutionary and molecular characteristics of high-Shannon entropy codons in VP1 of Coxsackievirus A6.The Journal of general virology · 2026Article
- Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles.Nature biotechnology · 2026Article
- Allostery is a widespread cause of loss-of-function variant pathogenicity.Nature communications · 2026Article
- Caveat emptor: predicting and modeling protein-DNA recognition and binding via machine-learning computational approaches.Nucleic acids research · 2026Review
- Phase diagrams for biophysical fitness landscape design.bioRxiv : the preprint server for biology · 2026Article
- Global genomic diversity of temperate P2-like viruses.Communications biology · 2026Article
- Comparative evaluation of the prediction accuracy of AlphaFold and ESMFold for monomeric and dimeric proteins.NAR genomics and bioinformatics · 2026Article
- Structural ontogeny of protein-protein interactions.Science (New York, N.Y.) · 2026Article
- Co-Var, a Measure to Determine Intra-protein, Inter-protein, Protein-DNA, or Protein-RNA Coevolution.Methods in molecular biology (Clifton, N.J.) · 2026Article
- NEMO recruitment at single cytokine-receptor complexes shows quantized dynamics independent of ligand affinity.Cell reports · 2025Article
- Cryo-EM structures of plant Augmin reveal coiled-coil assembly, antiparallel dimerization, and NEDD1 binding.Nature communications · 2025Article
- Two-Component Systems inVeterinary sciences · 2025Review
- PlasmoFP: leveraging deep learning to predict protein function of uncharacterized proteins across the malaria parasite genus.bioRxiv : the preprint server for biology · 2025Article
- State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025Review
- Effect of Mutations on the Evolution of Extended Spectrum β-lactamases (ESBL).The protein journal · 2025Review
- Long-range coupling regulates stator dynamics in the bacterial flagellar motor.bioRxiv : the preprint server for biology · 2025Article
205 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
8 authors.
Funding
Abstract
Protein-protein interactions are fundamental to many biological processes. Experimental screens have identified tens of thousands of interactions, and structural biology has provided detailed functional insight for select 3D protein complexes. An alternative rich source of information about protein interactions is the evolutionary sequence record. Building on earlier work, we show that analysis of correlated evolutionary sequence changes across proteins identifies residues that are close in space with sufficient accuracy to determine the three-dimensional structure of the protein complexes. We evaluate prediction performance in blinded tests on 76 complexes of known 3D structure, predict protein-protein contacts in 32 complexes of unknown structure, and demonstrate how evolutionary couplings can be used to distinguish between interacting and non-interacting protein pairs in a large complex. With the current growth of sequences, we expect that the method can be generalized to genome-wide elucidation of protein-protein interaction networks and used for interaction predictions at residue resolution.
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.