ArticleNature communications2018
Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Conformational changes of the baseplate regulating tail contraction of Staphylococcus phage 812.The EMBO journal · 2026Article
- Facilitating NMR Resonance Assignment with Metabolic Tampering.bioRxiv : the preprint server for biology · 2026Article
- Improving Protein Structure Determination by Integrating Ensemble-Driven Molecular Dynamics with Chemical Shift-Based Restraints.Journal of chemical information and modeling · 2026Article
- Elucidation of the Mechanisms of Inter-domain Coupling in the Monomeric State of Enzyme I by High-pressure NMR.Journal of molecular biology · 2024Article
- Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition.Nature communications · 2023Article
- Recognition and coacervation of G-quadruplexes by a multifunctional disordered region in RECQ4 helicase.Nature communications · 2023Article
- NMR-Chemical-Shift-Driven Protocol Reveals the Cofactor-Bound, Complete Structure of Dynamic Intermediates of the Catalytic Cycle of Oncogenic KRAS G12C Protein and the Significance of the MgInternational journal of molecular sciences · 2023Article
- Solution Structure Ensembles of the Open and Closed Forms of the ∼130 kDa Enzyme I via AlphaFold Modeling, Coarse Grained Simulations, and NMR.Journal of the American Chemical Society · 2023Article
- Linear discriminant analysis reveals hidden patterns in NMR chemical shifts of intrinsically disordered proteins.PLoS computational biology · 2022Article
- Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding.Nature communications · 2021Article
- Phosphorylation-induced changes in the PDZ domain of Dishevelled 3.Scientific reports · 2021Article
- A Single Point Mutation Controls the Rate of Interconversion Between theFrontiers in molecular biosciences · 2021Article
- Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I.Journal of molecular biology · 2020Article
- Macromolecular modeling and design in Rosetta: recent methods and frameworks.Nature methods · 2020Review
- A Practical Perspective on the Roles of Solution NMR Spectroscopy in Drug Discovery.Molecules (Basel, Switzerland) · 2020Review
- N-terminal fusion of the N-terminal domain of bacterial enzyme I facilitates recombinant expression and purification of the human RNA demethylases FTO and Alkbh5.Protein expression and purification · 2020Article
- Comparative phosphorylation map of Dishevelled 3 links phospho-signatures to biological outputs.Cell communication and signaling : CCS · 2019Article
- Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins.Current opinion in structural biology · 2019Review
- Dishevelled-3 conformation dynamics analyzed by FRET-based biosensors reveals a key role of casein kinase 1.Nature communications · 2019Article
- CS-ROSETTA.Methods in enzymology · 2019Article
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9 authors.
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Abstract
Automated methods for NMR structure determination of proteins are continuously becoming more robust. However, current methods addressing larger, more complex targets rely on analyzing 6-10 complementary spectra, suggesting the need for alternative approaches. Here, we describe 4D-CHAINS/autoNOE-Rosetta, a complete pipeline for NOE-driven structure determination of medium- to larger-sized proteins. The 4D-CHAINS algorithm analyzes two 4D spectra recorded using a single, fully protonated protein sample in an iterative ansatz where common NOEs between different spin systems supplement conventional through-bond connectivities to establish assignments of sidechain and backbone resonances at high levels of completeness and with a minimum error rate. The 4D-CHAINS assignments are then used to guide automated assignment of long-range NOEs and structure refinement in autoNOE-Rosetta. Our results on four targets ranging in size from 15.5 to 27.3 kDa illustrate that the structures of proteins can be determined accurately and in an unsupervised manner in a matter of days.
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