Evidence map›Paper›PMID 27547920›Full record

ArticleNature chemical biology2016

Oxidation increases the strength of the methionine-aromatic interaction.

Andrew K Lewis, Katie M Dunleavy, Tiffany L Senkow, Cheng Her, Benjamin T Horn, Mark A Jersett, Ryan Mahling, Megan R McCarthy, Gabriella T Perell, Christopher C Valley and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Styrylquinazoline derivatives as ABL inhibitors selective for different DFG orientations.Journal of enzyme inhibition and medicinal chemistry · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Methionine in proteins: The Cinderella of the proteinogenic amino acids.Protein science : a publication of the Protein Society · 2019
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Andrew K LewisDepartment of Biomedical Engineering, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
Katie M DunleavyDepartment of Chemistry and Biochemistry, University of Minnesota-Duluth, Duluth, Minnesota, USA.
Tiffany L SenkowDepartment of Biomedical Engineering, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
Cheng HerDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
Benjamin T HornDepartment of Chemistry and Biochemistry, University of Minnesota-Duluth, Duluth, Minnesota, USA.
Mark A JersettDepartment of Chemistry and Biochemistry, University of Minnesota-Duluth, Duluth, Minnesota, USA.
Ryan MahlingDepartment of Chemistry and Biochemistry, University of Minnesota-Duluth, Duluth, Minnesota, USA.
Megan R McCarthyDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
Gabriella T PerellDepartment of Chemistry, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
Christopher C ValleyDepartment of Biomedical Engineering, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
Christine B KarimDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
Jiali GaoDepartment of Chemistry, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
William C K PomerantzDepartment of Chemistry, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
David D ThomasDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.
Alessandro CembranDepartment of Chemistry and Biochemistry, University of Minnesota-Duluth, Duluth, Minnesota, USA.
Anne HinderliterDepartment of Chemistry and Biochemistry, University of Minnesota-Duluth, Duluth, Minnesota, USA.
Jonathan N SachsDepartment of Biomedical Engineering, University of Minnesota-Twin Cities, Minneapolis, Minnesota, USA.

Funding

TRAINING PROGRAM IN MUSCLE RESEARCHT32AR007612 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI JAMES M ERVASTI, DAWN A LOWE · 2001 to 2026
$11.3M
Site-Directed Oxidative Modification of Muscle Protein Structural DynamicsR37AG026160 · NIA · UNIVERSITY OF MINNESOTA · PI THOMAS, DAVID D · 2011 to 2020
$4.5M
Protein Oxidation, Structure, &Function in Aging MuscleR01AG026160 · NIA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 2004 to 2008
$2.2M
Dynamics of transmembrane dimers in TNF-Receptors by EPR and molecular simulationR01GM107175 · NIGMS · UNIVERSITY OF MINNESOTA · PI SACHS, JONATHAN N · 2014 to 2017
$1.3M
NIAMS NIH HHS T32 AR007612NIA NIH HHS R01 AG026160NIA NIH HHS R37 AG026160NIGMS NIH HHS R01 GM107175
6 · The paper itself

Abstract

Oxidation of methionine disrupts the structure and function of a range of proteins, but little is understood about the chemistry that underlies these perturbations. Using quantum mechanical calculations, we found that oxidation increased the strength of the methionine-aromatic interaction motif, a driving force for protein folding and protein-protein interaction, by 0.5-1.4 kcal/mol. We found that non-hydrogen-bonded interactions between dimethyl sulfoxide (a methionine analog) and aromatic groups were enriched in both the Protein Data Bank and Cambridge Structural Database. Thermal denaturation and NMR spectroscopy experiments on model peptides demonstrated that oxidation of methionine stabilized the interaction by 0.5-0.6 kcal/mol. We confirmed the biological relevance of these findings through a combination of cell biology, electron paramagnetic resonance spectroscopy and molecular dynamics simulations on (i) calmodulin structure and dynamics, and (ii) lymphotoxin-α binding toTNFR1. Thus, the methionine-aromatic motif was a determinant of protein structural and functional sensitivity to oxidative stress.

Indexed as

Hydrocarbons, AromaticMethionineModels, MolecularOxidation-ReductionQuantum TheoryHydrocarbons, AromaticMethionine

Identifiers

PMID27547920
PMCPMC5060120

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.