ArticleJournal of biomolecular NMR2004
Backbone assignment of proteins with known structure using residual dipolar couplings.
Article in Journal of biomolecular NMR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed.
- Conformational diversity of human HP1α.Protein science : a publication of the Protein Society · 2024Article
- Juxtaposition of Bub1 and Cdc20 on phosphorylated Mad1 during catalytic mitotic checkpoint complex assembly.Nature communications · 2022Article
- Molecular mechanism of Mad1 kinetochore targeting by phosphorylated Bub1.EMBO reports · 2021Article
- Farseer-NMR: automatic treatment, analysis and plotting of large, multi-variable NMR data.Journal of biomolecular NMR · 2018Article
- Automated assignment of NMR chemical shifts based on a known structure and 4D spectra.Journal of biomolecular NMR · 2016Article
- Reliable resonance assignments of selected residues of proteins with known structure based on empirical NMR chemical shift prediction.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA.The Journal of biological chemistry · 2012Article
- AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2012Article
- Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins.Journal of biomolecular NMR · 2011Article
- Backbone resonance assignment and order tensor estimation using residual dipolar couplings.Journal of biomolecular NMR · 2011Article
- NVR-BIP: Nuclear Vector Replacement using Binary Integer Programming for NMR Structure-Based Assignments.The computer journal · 2011Article
- RDC derived protein backbone resonance assignment using fragment assembly.Journal of biomolecular NMR · 2011Article
- Structure-oriented methods for protein NMR data analysis.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.Molecular cell · 2009Article
- NMR resonance assignments of sparsely labeled proteins: amide proton exchange correlations in native and denatured states.Journal of the American Chemical Society · 2009Article
- Assignment-free solution NMR method reveals CesT as an unswapped homodimer.Protein science : a publication of the Protein Society · 2008Article
- Structure-based protein NMR assignments using native structural ensembles.Journal of biomolecular NMR · 2008Article
- J-Spectroscopy in the presence of residual dipolar couplings: determination of one-bond coupling constants and scalable resolution.Journal of biomolecular NMR · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A prerequisite for NMR studies of protein-ligand interactions or protein dynamics is the assignment of backbone resonances. Here we demonstrate that protein assignment can significantly be enhanced when experimental dipolar couplings (RDCs) are matched to values back-calculated from a known three-dimensional structure. In case of small proteins, the program MARS allows assignment of more than 90% of backbone resonances without the need for sequential connectivity information. For bigger proteins, we show that the combination of sequential connectivity information with RDC-matching enables more residues to be assigned reliably and backbone assignment to be more robust against missing data. Structural or dynamic deviations from the employed 3D coordinates do not lead to an increased error rate in RDC-supported assignment. RDC-enhanced assignment is particularly useful when chemical shifts and sequential connectivity only provide a few reliable assignments.
Indexed as
Identifiers
15452432What 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.