Evidence map›Paper›PMID 30403347›Full record

ArticleJournal of the American Chemical Society2018

n→π* Interactions Modulate the Properties of Cysteine Residues and Disulfide Bonds in Proteins.

Henry R Kilgore, Ronald T Raines

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Context-Dependence of the Reactivity of Cysteine and Lysine Residues.Chembiochem : a European journal of chemical biology · 2022
    Article
  10. Article
  11. Article
  12. Journal of the American Chemical Society · 2020
    Article
  13. Article
  14. Disulfide Chromophores Arise from Stereoelectronic Effects.The journal of physical chemistry. B · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Secondary Forces in Protein Folding.ACS chemical biology · 2019
    Review
  20. AnACS catalysis · 2019
    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

2 authors at 1 institution in 1 country.

Henry R KilgoreDepartment of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States.
Ronald T RainesDepartment of Chemistry , Massachusetts Institute of Technology , Cambridge , Massachusetts 02139 , United States.ORCID 0000-0001-7164-1719
Massachusetts Institute of Technology · US

Funding

STRUCTURE--FUNCTION ANALYSIS OF RIBONUCLEASE AR01GM044783 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RAINES, RONALD T · 1990 to 2021
$7.1M
High Performance Computing Cluster for Public Health Driven Molecular Science - Core FacilityS10OD023532 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI DURKIN, KATHLEEN A · 2017 to 2017
$434k
NIGMS NIH HHS R01 GM044783NIH HHS S10 OD023532
6 · The paper itself

Abstract

Noncovalent interactions are ubiquitous in biology, taking on roles that include stabilizing the conformation of and assembling biomolecules, and providing an optimal environment for enzymatic catalysis. Here, we describe a noncovalent interaction that engages the sulfur atoms of cysteine residues and disulfide bonds in proteins-their donation of electron density into an antibonding orbital of proximal amide carbonyl groups. This n→ π* interaction tunes the reactivity of the CXXC motif, which is the critical feature of thioredoxin and other enzymes involved in redox homeostasis. In particular, an n→ π* interaction lowers the p K

Indexed as

Amino Acid MotifsAnimalsAspergillusBacteriaBacterial ProteinsCatalytic DomainComputational BiologyComputer SimulationCysteineDisulfidesDrosophila melanogasterEnzymesFungal ProteinsHumansHydrogen BondingModels, ChemicalBacterial ProteinsCysteineDisulfidesEnzymesFungal ProteinsProteins

Identifiers

PMID30403347
PMCPMC6527516
OpenAlexW2900400590

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.