Evidence map›Paper›PMID 21782785›Full record

ArticleArchives of biochemistry and biophysics2011

The Escherichia coli alkylation response protein AidB is a redox partner of flavodoxin and binds RNA and acyl carrier protein.

Scott B Mulrooney, Michael J Howard, Robert P Hausinger

Abstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 24% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Scott B MulrooneyDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, USA. mulroon2@msu.edu
Michael J Howard
Robert P Hausinger
Michigan State University · US

Funding

Study of alpha-ketoglutarate-dependent dioxygenasesR01GM063584 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HAUSINGER, ROBERT P · 2002 to 2014
$3.8M
NIGMS NIH HHS GM063584NIGMS NIH HHS R01 GM063584
6 · The paper itself

Abstract

Microorganisms are exposed to a wide variety of exogenous and endogenous chemical agents that alkylate DNA. Escherichia coli cells exhibit an adaptive response that recognizes and repairs alkylated DNA lesions using Ada, AlkA, and AlkB enzymes. Another alkylation response protein, the DNA-binding flavoprotein AidB, was proposed to repair DNA or protect it from chemical alkylating agents, but direct evidence for its role is lacking. Here, AidB was shown to form tight complexes with both flavodoxin and acyl carrier protein. In addition, electron transfer between 1-electron and 2-electron reduced flavodoxin to oxidized AidB was observed, although with very small rate constants. AidB was found to bind to RNA, raising the prospect that the protein may have a role in protection of RNA from chemical alkylation. Finally, the reagent N-methyl-N'-nitro-N-nitrosoguanidine was eliminated as a direct substrate of the enzyme.

Indexed as

Acyl Carrier ProteinAlkylationBase SequenceDNA, BacterialDNA RepairDNA Repair EnzymesElectron TransportEscherichia coliEscherichia coli ProteinsFlavodoxinMethylnitronitrosoguanidineMultiprotein ComplexesOxidation-ReductionProtein BindingRecombinant ProteinsRNA, BacterialAcyl Carrier ProteinAidB protein, E coliDNA, BacterialDNA Repair EnzymesEscherichia coli ProteinsFlavodoxinMethylnitronitrosoguanidineMultiprotein ComplexesRecombinant ProteinsRNA, Bacterial

Identifiers

PMID21782785
PMCPMC3166795
OpenAlexW2127958226

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.