Evidence map›Paper›PMID 26121406›Full record

ArticleNature methods2015

Protein structure determination by combining sparse NMR data with evolutionary couplings.

Yuefeng Tang, Yuanpeng Janet Huang, Thomas A Hopf, Chris Sander, Debora S Marks, Gaetano T Montelione

Abstract read
In one paragraph

Article in Nature methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

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  18. CS-ROSETTA.Methods in enzymology · 2019
    Article
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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

6 authors.

Yuefeng Tang1] Center for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [2] Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA.
Yuanpeng Janet Huang1] Center for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [2] Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA.
Thomas A Hopf1] Department of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA. [2] Department of Informatics, Technische Universität München, Garching, Germany.
Chris SanderComputational Biology Center, Memorial Sloan Kettering Cancer Center, New York, New York, USA.
Debora S MarksDepartment of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA.
Gaetano T Montelione1] Center for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [2] Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA. [3] Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, The State University of New Jersey, Piscataway, New Jersey, USA.

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Elisa de Stanchina · 1985 to 2026
$347.4M
University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI MONTELIONE, GAETANO T · 2010 to 2014
$36.9M
Accelerated Determination of 3D Structures of Proteins and ComplexesR01GM106303 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI SANDER, CHRIS · 2013 to 2016
$1.7M
NCI NIH HHS P30 CA008748NIGMS NIH HHS 1R01-GM106303NIGMS NIH HHS R01 GM106303NIGMS NIH HHS U54 GM094597NIGMS NIH HHS U54-GM094597
6 · The paper itself

Abstract

Accurate determination of protein structure by NMR spectroscopy is challenging for larger proteins, for which experimental data are often incomplete and ambiguous. Evolutionary sequence information together with advances in maximum entropy statistical methods provide a rich complementary source of structural constraints. We have developed a hybrid approach (evolutionary coupling-NMR spectroscopy; EC-NMR) combining sparse NMR data with evolutionary residue-residue couplings and demonstrate accurate structure determination for several proteins 6-41 kDa in size.

Indexed as

AlgorithmsComputational BiologyCrystallography, X-RayEvolution, MolecularHumansHydrodynamicsImaging, Three-DimensionalMagnetic Resonance SpectroscopyModels, StatisticalMolecular ConformationProtein ConformationProteinsProto-Oncogene ProteinsProto-Oncogene Proteins p21(ras)ras ProteinsKRAS protein, humanProteinsProto-Oncogene ProteinsProto-Oncogene Proteins p21(ras)ras Proteins

Identifiers

PMID26121406
PMCPMC4521990

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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.