Evidence map›Paper›PMID 10427742›Full record

ArticleJournal of biomolecular NMR1999

Refinement of the structure of protein-RNA complexes by residual dipolar coupling analysis.

P Bayer, L Varani, G Varani

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

P BayerMRC Laboratory of Molecular Biology, Cambridge, U.K.
L Varani
G Varani

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The main limitation in NMR-determined structures of nucleic acids and their complexes with proteins derives from the elongated, non-globular nature of physiologically important DNA and RNA molecules. Since it is generally not possible to obtain long-range distance constraints between distinct regions of the structure, long-range properties such as bending or kinking at sites of protein recognition cannot be determined accurately nor precisely. Here we show that use of residual dipolar couplings in the refinement of the structure of a protein-RNA complex improves the definition of the long-range properties of the RNA. These features are often an important aspect of molecular recognition and biological function; therefore, their improved definition is of significant value in RNA structural biology.

Indexed as

Cloning, MolecularDimyristoylphosphatidylcholineEscherichia coliHumansLipid BilayersModels, MolecularNuclear Magnetic Resonance, BiomolecularPhospholipid EthersProtein ConformationProtein Structure, SecondaryRecombinant ProteinsRibonucleoprotein, U1 Small NuclearRNARNA-Binding ProteinsThermodynamics1,2-dihexadecyl-sn-glycero-3-phosphocholineDimyristoylphosphatidylcholineLipid BilayersPhospholipid EthersRecombinant ProteinsRibonucleoprotein, U1 Small NuclearRNARNA-Binding ProteinsU1A protein

Identifiers

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Registered trials

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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.