ArticleProceedings of the National Academy of Sciences of the United States of America2005
NMR data collection and analysis protocol for high-throughput protein structure determination.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 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
64 citing papers in PubMed, 117 citations in OpenAlex.
- Label-Free Measurement of Ligand Interactions Using SABRE Hyperpolarization at Low Magnetic Fields.Analytical chemistry · 2026Article
- Top-Down Scoring of Spectral Fitness by Image Analysis for Protein Structure Validation.Journal of chemical information and modeling · 2026Article
- AlphaFold Models of Small Proteins Rival the Accuracy of Solution NMR Structures.Frontiers in molecular biosciences · 2022Article
- Role of backbone strain in de novo design of complex α/β protein structures.Nature communications · 2021Article
- Article
- Synthesis and Solution-Phase Characterization of Sulfonated Oligothioetheramides.Macromolecules · 2017Article
- Structural/Functional Properties of Human NFU1, an Intermediate [4Fe-4S] Carrier in Human Mitochondrial Iron-Sulfur Cluster Biogenesis.Structure (London, England : 1993) · 2016Article
- Observation selection bias in contact prediction and its implications for structural bioinformatics.Scientific reports · 2016Article
- Article
- Introduction of a polar core into the de novo designed protein Top7.Protein science : a publication of the Protein Society · 2016Article
- The impact of structural genomics: the first quindecennial.Journal of structural and functional genomics · 2016Review
- A community resource of experimental data for NMR / X-ray crystal structure pairs.Protein science : a publication of the Protein Society · 2016Review
- Enhanced biosynthetically directed fractional carbon-13 enrichment of proteins for backbone NMR assignments.Protein expression and purification · 2015Article
- Control over overall shape and size in de novo designed proteins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A hybrid NMR/SAXS-based approach for discriminating oligomeric protein interfaces using Rosetta.Proteins · 2015Article
- Structure calculation, refinement and validation using CcpNmr Analysis.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network.Journal of structural and functional genomics · 2014Article
- Solution NMR structures of immunoglobulin-like domains 7 and 12 from obscurin-like protein 1 contribute to the structural coverage of the Human Cancer Protein Interaction Network.Journal of structural and functional genomics · 2014Article
- Nonuniform sampling and non-Fourier signal processing methods in multidimensional NMR.Progress in nuclear magnetic resonance spectroscopy · 2014Review
- High-quality NMR structure of human anti-apoptotic protein domain Mcl-1(171-327) for cancer drug design.PloS one · 2014Article
4 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
14 authors at 3 institutions in 2 countries.
Funding
Abstract
A standardized protocol enabling rapid NMR data collection for high-quality protein structure determination is presented that allows one to capitalize on high spectrometer sensitivity: a set of five G-matrix Fourier transform NMR experiments for resonance assignment based on highly resolved 4D and 5D spectral information is acquired in conjunction with a single simultaneous 3D 15N,13C(aliphatic),13C(aromatic)-resolved [1H,1H]-NOESY spectrum providing 1H-1H upper distance limit constraints. The protocol was integrated with methodology for semiautomated data analysis and used to solve eight NMR protein structures of the Northeast Structural Genomics Consortium pipeline. The molecular masses of the hypothetical target proteins ranged from 9 to 20 kDa with an average of approximately 14 kDa. Between 1 and 9 days of instrument time were invested per structure, which is less than approximately 10-25% of the measurement time routinely required to date with conventional approaches. The protocol presented here effectively removes data collection as a bottleneck for high-throughput solution structure determination of proteins up to at least approximately 20 kDa, while concurrently providing spectra that are highly amenable to fast and robust analysis.
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.