Evidence map›Paper›PMID 20041641›Full record

ArticleJournal of the American Chemical Society2010

High-resolution solid-state NMR structure of a 17.6 kDa protein.

Ivano Bertini, Anusarka Bhaumik, Gaël De Paëpe, Robert G Griffin, Moreno Lelli, Józef R Lewandowski, Claudio Luchinat

Open access · greenAbstract 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 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
6.1field-weighted citation impact, top 3% 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, 124 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Strategies for RNA Resonance Assignment byFrontiers in molecular biosciences · 2021
    Review
  5. Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021
    Article
  6. Adiabatic Solid Effect.The journal of physical chemistry letters · 2020
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Proton-Assisted Recoupling (PAR) in Peptides and Proteins.The journal of physical chemistry. B · 2017
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Biosilica-Entrapped Enzymes Studied by Using Dynamic Nuclear-Polarization-Enhanced High-Field NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2015
    Article
  18. Facing and Overcoming Sensitivity Challenges in Biomolecular NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2015
    Review
  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

7 authors at 1 institution in 1 country.

Ivano BertiniMagnetic Resonance Center, CERM, University of Florence, Via L. Sacconi, 6-50019 Sesto Fiorentino, Italy. bertini@cerm.unifi.it
Anusarka Bhaumik
Gaël De Paëpe
Robert G Griffin
Moreno Lelli
Józef R Lewandowski
Claudio Luchinat
University of Florence · IT

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Solid State NMR Studies of Peptides and ProteinsR01EB003151 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2004 to 2015
$6.5M
NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB003151
6 · The paper itself

Abstract

The use of pseudocontact shifts arising from paramagnetic metal ions in a microcrystalline protein sample is proposed as a strategy to obtain unambiguous signal assignments in solid-state NMR spectra enabling distance extraction for protein structure calculation. With this strategy, 777 unambiguous (281 sequential, 217 medium-range, and 279 long-range) distance restraints could be obtained from PDSD, DARR, CHHC, and the recently introduced PAR and PAIN-CP solid-state experiments for the cobalt(II)-substituted catalytic domain of matrix metalloproteinase 12 (159 amino acids, 17.6 kDa). The obtained structure is a high resolution one, with backbone rmsd of 1.0 +/- 0.2 A, and is in good agreement with the X-ray structure (rmsd to X-ray 1.3 A). The proposed strategy, which may be generalized for nonmetalloproteins with the use of paramagnetic tags, represents a significant step ahead in protein structure determination using solid-state NMR.

Indexed as

Crystallography, X-RayMagnetic Resonance SpectroscopyMatrix Metalloproteinase 12Models, MolecularProtein ConformationMatrix Metalloproteinase 12

Identifiers

PMID20041641
PMCPMC4437541
OpenAlexW2057913703

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.