Evidence map›Paper›PMID 30737614›Full record

ArticleJournal of biomolecular NMR2019

The NMR signature of gluconoylation: a frequent N-terminal modification of isotope-labeled proteins.

David Schweida, Pierre Barraud, Christof Regl, Fionna E Loughlin, Christian G Huber, Chiara Cabrele, Mario Schubert

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

7 authors.

David SchweidaDepartment of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria.
Pierre BarraudInstitute of Molecular Biology and Biophysics, ETH Zürich, 8093, Zurich, Switzerland.
Christof ReglDepartment of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria.
Fionna E LoughlinInstitute of Molecular Biology and Biophysics, ETH Zürich, 8093, Zurich, Switzerland.
Christian G HuberDepartment of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria.
Chiara CabreleDepartment of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria.
Mario SchubertDepartment of Biosciences, University of Salzburg, Billrothstr. 11, 5020, Salzburg, Austria. mario.schubert@sbg.ac.at.ORCID http://orcid.org/0000-0003-0278-4091

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-terminal gluconoylation is a moderately widespread modification in recombinant proteins expressed in Escherichia coli, in particular in proteins bearing an N-terminal histidine-tag. This post-translational modification has been investigated mainly by mass spectrometry. Although its NMR signals must have been observed earlier in spectra of

Indexed as

Protein Processing, Post-TranslationalGluconatesIsotope LabelingNuclear Magnetic Resonance, BiomolecularRecombinant ProteinsGluconatesgluconic acidRecombinant ProteinsE. coliGluconic acidGluconoylationNMR spectroscopyN-terminusPost-translational protein modificationRecombinant protein

Identifiers

PMID30737614
PMCPMC6441400

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.