Evidence map›Paper›PMID 15210958›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment.

Hanudatta S Atreya, Thomas Szyperski

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Article
  2. Article
  3. Simultaneous MQMAS NMR Experiments for Two Half-Integer Quadrupolar Nuclei.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    Article
  4. Review
  5. Article
  6. Article
  7. Facing and Overcoming Sensitivity Challenges in Biomolecular NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2015
    Review
  8. Article
  9. Computational de novo design of a four-helix bundle protein--DND_4HB.Protein science : a publication of the Protein Society · 2015
    Article
  10. Article
  11. Article
  12. Spatially selective heteronuclear multiple-quantum coherence spectroscopy for biomolecular NMR studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2014
    Article
  13. Article
  14. Article
  15. Article
  16. Fast automated protein NMR data collection and assignment by ADAPT-NMR on Bruker spectrometers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

2 authors.

Hanudatta S AtreyaDepartment of Chemistry, State University of New York, Northeast Structural Genomics Consortium, Buffalo, NY 14260, USA.
Thomas Szyperski

Funding

STRUCTURAL GENOMICS OF EUKARYOTIC MODEL ORGANISMSP50GM062413 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MONTELIONE, GAETANO T · 2000 to 2004
$33.5M
NIGMS NIH HHS P50 GM062413NIGMS NIH HHS P50 GM62413
6 · The paper itself

Abstract

A G-matrix Fourier transform (GFT) NMR spectroscopy-based strategy for resonance assignment of proteins is described. Each of the GFT NMR experiments presented here rapidly affords four-, five-, or six-dimensional spectral information in combination with precise measurements of chemical shifts. The resulting high information content enables one to obtain nearly complete assignments by using only four NMR experiments. For the backbone amide proton detected "out-and-back" experiments, data collection was further accelerated up to approximately 2.5-fold by use of longitudinal (1)H relaxation optimization. The GFT NMR experiments were acquired for three proteins with molecular masses ranging from 8.6 to 17 kDa, demonstrating that the proposed strategy is of key interest for automated resonance assignment in structural genomics.

Indexed as

Fourier AnalysisBacterial ProteinsMagnetic Resonance SpectroscopyMolecular WeightPeptidesSensitivity and SpecificityBacterial ProteinsPeptides

Identifiers

PMID15210958
PMCPMC470728

What OpenQuestion holds

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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.