Evidence map›Paper›PMID 12766417›Full record

ArticleJournal of biomolecular NMR2003

A rapid method to attain isotope labeled small soluble peptides for NMR studies.

Bernd W Koenig, Marco Rogowski, John M Louis

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. The Polycystin-1, Lipoxygenase, and α-Toxin Domain Regulates Polycystin-1 Trafficking.Journal of the American Society of Nephrology : JASN · 2016
    Article
  4. Article
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  8. Article
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  10. Structural basis of RNA binding by leucine zipper GCN4.Protein science : a publication of the Protein Society · 2012
    Article
  11. Article
  12. Dynamics of antibody domains studied by solution NMR.Methods in molecular biology (Clifton, N.J.) · 2009
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Protein-Inhibitor Interaction Studies Using NMR.Applications of NMR spectroscopy
    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

3 authors.

Bernd W KoenigStructural Biology Institute, IBI-2, Research Centre Jülich, D-52425 Jülich, Germany. b.koenig@fz-juelich.de
Marco Rogowski
John M Louis

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A widely applicable strategy is presented for efficient and rapid production of small water soluble peptides expressed as fusion proteins with the immunoglobulin-binding domain of streptococcal protein G. A simple extraction and purification scheme that includes a protease cleavage step to release the target peptide is described. The yield of authentic target peptide exceeds 10 mg per liter of culture. Production of U-13C, 15N and highly deuterated U-13C, 15N isotope labeled peptide is demonstrated for the 11 residue S2 peptide, corresponding to the C-terminus of the alpha-subunit of transducin, and the coiled coil trimerization domain from cartilage matrix protein (CMPcc), respectively. Heteronuclear two-dimensional NMR spectra are used for initial peptide characterization.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAnimalsBacterial ProteinsGene ExpressionGenetic VectorsIsotope LabelingPeptidesPlasmidsRecombinant Fusion ProteinsSolubilityBacterial ProteinsIgG Fc-binding protein, StreptococcusPeptidesRecombinant Fusion Proteins

Identifiers

What OpenQuestion holds

Textmetadata
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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.