Evidence map›Paper›PMID 22639603›Full record

ArticleFrontiers in plant science2011

Aldehyde Dehydrogenases in Arabidopsis thaliana: Biochemical Requirements, Metabolic Pathways, and Functional Analysis.

Naim Stiti, Tagnon D Missihoun, Simeon O Kotchoni, Hans-Hubert Kirch, Dorothea Bartels

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification of Aldehyde Dehydrogenase Gene Family inInternational journal of molecular sciences · 2025
    Article
  4. Functional characterization ofBiochemistry and biophysics reports · 2024
    Article
  5. Article
  6. Article
  7. Roles of Reactive Carbonyl Species (RCS) in Plant Response to Abiotic Stress.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Redox Regulation of Salt Tolerance inInternational journal of molecular sciences · 2023
    Article
  9. Review
  10. Frontiers in plant science · 2023
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Functional study ofFrontiers in plant science · 2022
    Article
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 2 countries.

Naim StitiInstitute of Molecular Physiology and Biotechnology of Plants, University of Bonn Bonn, Germany.
Tagnon D Missihoun
Simeon O Kotchoni
Hans-Hubert Kirch
Dorothea Bartels
University of Bonn · DERutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldehyde dehydrogenases (ALDHs) are a family of enzymes which catalyze the oxidation of reactive aldehydes to their corresponding carboxylic acids. Here we summarize molecular genetic and biochemical analyses of selected ArabidopsisALDH genes. Aldehyde molecules are very reactive and are involved in many metabolic processes but when they accumulate in excess they become toxic. Thus activity of aldehyde dehydrogenases is important in regulating the homeostasis of aldehydes. Overexpression of some ALDH genes demonstrated an improved abiotic stress tolerance. Despite the fact that several reports are available describing a role for specific ALDHs, their precise physiological roles are often still unclear. Therefore a number of genetic and biochemical tools have been generated to address the function with an emphasis on stress-related ALDHs. ALDHs exert their functions in different cellular compartments and often in a developmental and tissue specific manner. To investigate substrate specificity, catalytic efficiencies have been determined using a range of substrates varying in carbon chain length and degree of carbon oxidation. Mutational approaches identified amino acid residues critical for coenzyme usage and enzyme activities.

Indexed as

aldehyde dehydrogenasesaminoaldehyde dehydrogenasesbetaine aldehyde dehydrogenasescoenzyme bindingenzyme activitiesstress tolerance

Identifiers

PMID22639603
PMCPMC3355590
OpenAlexW2087925221

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.