Evidence map›Paper›PMID 20509649›Full record

ArticleJournal of the American Chemical Society2010

A resonance assignment method for oriented-sample solid-state NMR of proteins.

Robert W Knox, George J Lu, Stanley J Opella, Alexander A Nevzorov

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
  3. Article
  4. Spatial reorientation experiments for NMR of solids and partially oriented liquids.Progress in nuclear magnetic resonance spectroscopy · 2015
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Mechanism of dilute-spin-exchange in solid-state NMR.The Journal of chemical physics · 2014
    Article
  10. Covariance spectroscopy in high-resolution multi-dimensional solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Membrane protein structure determination: back to the membrane.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  17. Structure determination of membrane proteins by nuclear magnetic resonance spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2013
    Review
  18. Review
  19. 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

4 authors at 2 institutions in 1 country.

Robert W KnoxDepartment of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, North Carolina 27695-8204, USA.
George J Lu
Stanley J Opella
Alexander A Nevzorov
North Carolina State University · USUniversity of California, San Diego · US

Funding

RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
Molecular Imaging of G-Protein-Coupled Receptors for Drug DevelopmentR01EB005161 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2006 to 2014
$6.8M
Membrane Protein Structures:Phospholipid Bilayers (RMI)R01GM075877 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2005 to 2009
$1.4M
NIBIB NIH HHS P41 EB002031NIBIB NIH HHS P41EB002031NIBIB NIH HHS R01 EB005161NIGMS NIH HHS R01 GM075877
6 · The paper itself

Abstract

A general sequential assignment strategy for uniformly (15)N-labeled uniaxially aligned membrane proteins is proposed. Mismatched Hartmann-Hahn magnetization transfer is employed to establish proton-mediated correlations among the neighboring (15)N backbone spins. Magnetically aligned Pf1 phage coat protein was used to illustrate the method. Exchanged and nonexchanged separated local field spectra were acquired and overlaid to distinguish the cross-peaks from the main peaks. Most of the original assignments from the literature were confirmed without selectively labeled samples. This method is applicable to proteins with arbitrary topology and will find use in assigning solid-state NMR spectra of oriented membrane proteins for their subsequent structure determination.

Indexed as

Bacteriophage Pf1Nuclear Magnetic Resonance, BiomolecularProteinsProteins

Identifiers

PMID20509649
PMCPMC2909040
OpenAlexW2005395842

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.