Evidence map›Paper›PMID 19113834›Full record

ArticleBiochemistry2009

Protein nuclear magnetic resonance under physiological conditions.

Gary J Pielak, Conggang Li, Andrew C Miklos, Alexander P Schlesinger, Kristin M Slade, Gui-Fang Wang, Imola G Zigoneanu

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
  2. Selective [9-Chembiochem : a European journal of chemical biology · 2025
    Article
  3. Review
  4. Article
  5. In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells.Journal of the American Chemical Society · 2021
    Article
  6. Article
  7. Article
  8. Controlling and quantifying protein concentration in Escherichia coli.Protein science : a publication of the Protein Society · 2019
    Article
  9. Review
  10. Applications of In-Cell NMR in Structural Biology and Drug Discovery.International journal of molecular sciences · 2019
    Review
  11. Article
  12. Enhancing fluorescent protein photostability through robot-assisted photobleaching.Integrative biology : quantitative biosciences from nano to macro · 2018
    Article
  13. Article
  14. Intracellular pH modulates quinary structure.Protein science : a publication of the Protein Society · 2015
    Article
  15. Article
  16. Specific ion effects on macromolecular interactions in Escherichia coli extracts.Protein science : a publication of the Protein Society · 2015
    Article
  17. Intrinsic site-selectivity of ubiquitin dimer formation.Protein science : a publication of the Protein Society · 2015
    Article
  18. Article
  19. Review
  20. Impact of reconstituted cytosol on protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Gary J PielakDepartment of Chemistry, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599, USA. gary_pielak@unc.edu
Conggang Li
Andrew C Miklos
Alexander P Schlesinger
Kristin M Slade
Gui-Fang Wang
Imola G Zigoneanu
UNC Lineberger Comprehensive Cancer CenterUniversity of North Carolina at Chapel Hill · US

Funding

NIH Director's Pioneer AwardDP1OD000783 · OD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PIELAK, GARY JOSEPH · 2006 to 2010
$3.7M
NIH HHS 5DP1OD783NIH HHS DP1 OD000783
6 · The paper itself

Abstract

Almost everything we know about protein biophysics comes from studies on purified proteins in dilute solution. Most proteins, however, operate inside cells where the concentration of macromolecules can be >300 mg/mL. Although reductionism-based approaches have served protein science well for more than a century, biochemists now have the tools to study proteins under these more physiologically relevant conditions. We review a part of this burgeoning postreductionist landscape by focusing on high-resolution protein nuclear magnetic resonance (NMR) spectroscopy, the only method that provides atomic-level information over an entire protein under the crowded conditions found in cells.

Indexed as

CarbonDeuteriumDiffusionNitrogenNuclear Magnetic Resonance, BiomolecularProteinsCarbonDeuteriumNitrogenProteins

Identifiers

PMID19113834
PMCPMC2645539
OpenAlexW2047774685

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.