Evidence map›Paper›PMID 18227427›Full record

ArticleProtein science : a publication of the Protein Society2008

Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy.

Ying Li, Deborah A Berthold, Robert B Gennis, Chad M Rienstra

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

41 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Helical membrane protein conformations and their environment.European biophysics journal : EBJ · 2013
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structure determination of a membrane protein in proteoliposomes.Journal of the American Chemical Society · 2012
    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

4 authors at 1 institution in 1 country.

Ying LiCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Deborah A Berthold
Robert B Gennis
Chad M Rienstra
University of Illinois Urbana-Champaign · US

Funding

Structure and Function of Membrane Protein Complexes(RMI)R01GM075937 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RIENSTRA, CHAD M · 2005 to 2009
$1.4M
NIGMS NIH HHS R01 GM075937NIGMS NIH HHS R01GM075937
6 · The paper itself

Abstract

The Escherichia coli inner membrane enzyme DsbB catalyzes disulfide bond formation in periplasmic proteins, by transferring electrons to ubiquinone from DsbA, which in turn directly oxidizes cysteines in substrate proteins. We have previously shown that DsbB can be prepared in a state that gives highly resolved magic-angle spinning (MAS) NMR spectra. Here we report sequential 13C and 15N chemical shift assignments for the majority of the residues in the transmembrane helices, achieved by three-dimensional (3D) correlation experiments on a uniformly 13C, 15N-labeled sample at 750-MHz 1H frequency. We also present a four-dimensional (4D) correlation spectrum, which confirms assignments in some highly congested regions of the 3D spectra. Overall, our results show the potential to assign larger membrane proteins using 3D and 4D correlation experiments and form the basis of further structural and dynamical studies of DsbB by MAS NMR.

Indexed as

Bacterial ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsMembrane ProteinsNuclear Magnetic Resonance, BiomolecularOxidoreductasesProtein FoldingProtein Structure, SecondaryBacterial ProteinsDsbB protein, BacteriaEscherichia coli ProteinsMembrane ProteinsOxidoreductases

Identifiers

PMID18227427
PMCPMC2222720
OpenAlexW1994609929

What OpenQuestion holds

Textmetadata
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.