Evidence map›Paper›PMID 37047605›Full record

ArticleInternational journal of molecular sciences2023

The Crystal Structure of Engineered Nitroreductase NTR 2.0 and Impact of F70A and F108Y Substitutions on Substrate Specificity.

Abigail V Sharrock, Jeff S Mumm, Gintautas Bagdžiūnas, Narimantas Čėnas, Vickery L Arcus, David F Ackerley

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 50% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. The Catalysis Mechanism ofInternational journal of molecular sciences · 2024
    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

6 authors at 4 institutions in 3 countries.

Abigail V SharrockSchool of Biological Sciences, Victoria University of Wellington, Wellington 6012, New Zealand.
Jeff S MummWilmer Eye Institute, Johns Hopkins University, Baltimore, MD 21287, USA.
Gintautas BagdžiūnasInstitute of Biochemistry, University of Vilnius, Saulėtekio 7, LT-10257 Vilnius, Lithuania.ORCID 0000-0002-9924-6902
Narimantas ČėnasInstitute of Biochemistry, University of Vilnius, Saulėtekio 7, LT-10257 Vilnius, Lithuania.
Vickery L ArcusTe Aka Mātuatua-School of Science, University of Waikato, Hamilton 3240, New Zealand.
David F AckerleySchool of Biological Sciences, Victoria University of Wellington, Wellington 6012, New Zealand.ORCID 0000-0002-6188-9902
Victoria University of Wellington · NZVilnius University · LTJohns Hopkins University · USUniversity of Waikato · NZ

Funding

Novel models of Alzheimer's Disease and Related Disorders enabling systematic investigation of the therapeutic potential of transplanted hiPSC-derived cells and endogenous adult neural stem cellsR01OD020376 · OD · JOHNS HOPKINS UNIVERSITY · PI MUMM, JEFFREY · 2016 to 2020
$2.1M
Health Research Council of New Zealand 19/750NIH HHS R01 OD020376NIH HHS R01OD020376Royal Society of New Zealand VUW1902
6 · The paper itself

Abstract

Bacterial nitroreductase enzymes that convert prodrugs to cytotoxins are valuable tools for creating transgenic targeted ablation models to study cellular function and cell-specific regeneration paradigms. We recently engineered a nitroreductase ("NTR 2.0") for substantially enhanced reduction of the prodrug metronidazole, which permits faster cell ablation kinetics, cleaner interrogations of cell function, ablation of previously recalcitrant cell types, and extended ablation paradigms useful for modelling chronic diseases. To provide insight into the enhanced enzymatic mechanism of NTR 2.0, we have solved the X-ray crystal structure at 1.85 Angstroms resolution and compared it to the parental enzyme, NfsB from

Indexed as

ProdrugsAnimalsAnimals, Genetically ModifiedMetronidazoleNitroreductasesSubstrate SpecificityMetronidazoleNitroreductasesProdrugsCB1954crystal structuredinitrotoluenemetronidazoleNfsBprodrugtargeted cellular ablationtinidazoletype I nitroreductase

Identifiers

PMID37047605
PMCPMC10095097
OpenAlexW4362582651

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.