Evidence map›Paper›PMID 21161328›Full record

ArticleJournal of biomolecular NMR2011

A novel strategy for NMR resonance assignment and protein structure determination.

Alexander Lemak, Aleksandras Gutmanas, Seth Chitayat, Murthy Karra, Christophe Farès, Maria Sunnerhagen, Cheryl H Arrowsmith

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
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

34 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Heat-induced structural and chemical changes to a computationally designed miniprotein.Protein science : a publication of the Protein Society · 2024
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  19. Basic Tilted Helix Bundle - a new protein fold in human FKBP25/FKBP3 and HectD1.Biochemical and biophysical research communications · 2014
    Article
  20. Review
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

7 authors at 4 institutions in 4 countries.

Alexander LemakOntario Cancer Institute and The Campbell Family Cancer Research Institute, Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, ON M5G 1L7, Canada.
Aleksandras Gutmanas
Seth Chitayat
Murthy Karra
Christophe Farès
Maria Sunnerhagen
Cheryl H Arrowsmith
Ontario Institute for Cancer Research · CAStructural Genomics Consortium · CAUniversity of Toronto · CALinköping University · SE

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI MONTELIONE, GAETANO T · 2010 to 2014
$36.9M
STRUCTURAL GENOMICS OF EUKARYOTIC MODEL ORGANISMSP50GM062413 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MONTELIONE, GAETANO T · 2000 to 2004
$33.5M
CIHRNIGMS NIH HHS GM67965NIGMS NIH HHS P50 GM062413NIGMS NIH HHS P50-GM62413-01NIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

The quality of protein structures determined by nuclear magnetic resonance (NMR) spectroscopy is contingent on the number and quality of experimentally-derived resonance assignments, distance and angular restraints. Two key features of protein NMR data have posed challenges for the routine and automated structure determination of small to medium sized proteins; (1) spectral resolution - especially of crowded nuclear Overhauser effect spectroscopy (NOESY) spectra, and (2) the reliance on a continuous network of weak scalar couplings as part of most common assignment protocols. In order to facilitate NMR structure determination, we developed a semi-automated strategy that utilizes non-uniform sampling (NUS) and multidimensional decomposition (MDD) for optimal data collection and processing of selected, high resolution multidimensional NMR experiments, combined it with an ABACUS protocol for sequential and side chain resonance assignments, and streamlined this procedure to execute structure and refinement calculations in CYANA and CNS, respectively. Two graphical user interfaces (GUIs) were developed to facilitate efficient analysis and compilation of the data and to guide automated structure determination. This integrated method was implemented and refined on over 30 high quality structures of proteins ranging from 5.5 to 16.5 kDa in size.

Indexed as

Models, MolecularAlgorithmsNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsSoftwareProteins

Identifiers

PMID21161328
PMCPMC3715383
OpenAlexW2026609572

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.