Evidence map›Paper›PMID 32669283›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2020

RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.

Jessica L Irons, Kelsey Hodge-Hanson, Diana M Downs

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. The role of colony morphotype in shaping gene essentiality inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. RidA proteins contribute to fitness ofMicrobial cell (Graz, Austria) · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Metabolic versatility ofFrontiers in microbiology · 2023
    Article
  17. Review
  18. DadY (PA5303) is required for fitness ofMicrobial cell (Graz, Austria) · 2022
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Jessica L IronsDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.
Kelsey Hodge-HansonDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.
Diana M DownsDepartment of Microbiology, University of Georgia, Athens, Georgia, USA dmdowns@uga.edu.ORCID 0000-0002-1564-6205
University of Georgia · US

Funding

Rid family members neutralize endogenous metabolic stressorsR01GM095837 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DOWNS, DIANA M. · 2011 to 2023
$3.7M
NIGMS NIH HHS R01 GM095837
6 · The paper itself

Abstract

The Rid (YjgF/YER057c/UK114) protein superfamily was first defined by sequence homology with available protein sequences from bacteria, archaea, and eukaryotes (L. Parsons, N. Bonander, E. Eisenstein, M. Gilson, et al., Biochemistry 42:80-89, 2003, https://doi.org/10.1021/bi020541w). The archetypal subfamily, RidA (reactive intermediate deaminase A), is found in all domains of life, with the vast majority of free-living organisms carrying at least one RidA homolog. In over 2 decades, close to 100 reports have implicated Rid family members in cellular processes in prokaryotes, yeast, plants, and mammals. Functional roles have been proposed for Rid enzymes in amino acid biosynthesis, plant root development and nutrient acquisition, cellular respiration, and carcinogenesis. Despite the wealth of literature and over a dozen high-resolution structures of different RidA enzymes, their biochemical function remained elusive for decades. The function of the RidA protein was elucidated in a bacterial model system despite (i) a minimal phenotype of

Indexed as

Stress, PhysiologicalAlanineAmino AcidsAminohydrolasesBacteriaBacterial ProteinsEukaryotaGene Expression Regulation, BacterialHydrocarbons, AromaticIminesMetabolic Networks and PathwaysSalmonella entericaSubstrate SpecificityUracilAlanineAmino AcidsAminohydrolasesBacterial ProteinsdehydroalanineHydrocarbons, AromaticIminesUracilYjgF protein, Bacteria2-aminoacrylate stressenamine/imine metabolismRidAYjgF/YER057c/UK114

Identifiers

PMID32669283
PMCPMC7373157
OpenAlexW3042603042

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.