Evidence map›Paper›PMID 26616824›Full record

ArticleJournal of the American Chemical Society2015

Single Amino Acid Switch between a Flavin-Dependent Dehalogenase and Nitroreductase.

Arnab Mukherjee, Steven E Rokita

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Biochemistry · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Evolutionary aspects of the Viridiplantae nitroreductases.Journal, genetic engineering & biotechnology · 2020
    Article
  9. Article
  10. Redox control of iodotyrosine deiodinase.Protein science : a publication of the Protein Society · 2019
    Article
  11. Article
  12. Article
  13. Evolutionary and molecular foundations of multiple contemporary functions of the nitroreductase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Review
  15. Article
  16. Functional analysis of iodotyrosine deiodinase from drosophila melanogaster.Protein science : a publication of the Protein Society · 2016
    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.

Arnab MukherjeeDepartment of Chemistry, Johns Hopkins University , Baltimore, Maryland 21218, United States.
Steven E RokitaDepartment of Chemistry, Johns Hopkins University , Baltimore, Maryland 21218, United States.

Funding

Reductive Dehalogenation in Mammals by Iodotyrosine DeiodinaseR01DK084186 · NIDDK · UNIV OF MARYLAND, COLLEGE PARK · PI ROKITA, STEVEN E · 2009 to 2012
$1.3M
NIDDK NIH HHS DK084186NIDDK NIH HHS R01 DK084186
6 · The paper itself

Abstract

A single mutation within a flavoprotein is capable of switching the catalytic activity of a dehalogenase into a nitroreductase. This change in function correlates with a destabilization of the one-electron-reduced flavin semiquinone that is differentially expressed in the nitro-FMN reductase superfamily during redox cycling. The diversity of function within such a superfamily therefore has the potential to arise from rapid evolution, and its members should provide a convenient basis for developing new catalysts with an altered specificity of choice.

Indexed as

Amino AcidsFlavinsGene Expression Regulation, EnzymologicMolecular StructureMutationNitroreductasesOxidoreductasesAmino AcidsFlavinsNitroreductasesOxidoreductases

Identifiers

PMID26616824
PMCPMC4684082

What OpenQuestion holds

Textmetadata
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.