Evidence map›Paper›PMID 10889258›Full record

ArticlePlant physiology2000

Characterization of sulfate assimilation in marine algae focusing on the enzyme 5'-adenylylsulfate reductase.

Y Gao, O M Schofield, T Leustek

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

18 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Sulfur metabolites in the pelagic ocean.Nature reviews. Microbiology · 2019
    Review
  5. Article
  6. Article
  7. Article
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  9. Article
  10. Review
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  13. Review
  14. Review
  15. Article
  16. Article
  17. Sulfate metabolism.The arabidopsis book · 2002
    Article
  18. 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.

Y GaoBiotechnology Center for Agriculture and the Environment and Institute of Marine and Coastal Sciences, Rutgers University, New Brunswick, New Jersey 08901-8520, USA. gao@aesop.rutgers.edu
O M Schofield
T Leustek
Rutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

5'-Adenylylsulfate (APS) reductase was characterized in diverse marine algae. A cDNA encoding APS reductase from Enteromorpha intestinalis (EAPR) was cloned by functional complementation of an Escherichia coli cysH mutant. The deduced amino acid sequence shows high homology with APS reductase (APR) from flowering plants. Based on the probable transit peptide cleavage site the mature protein is 45.7 kD. EAPR expressed as a His-tagged recombinant protein catalyzes reduced glutathione-dependent reduction of APS to sulfite, exhibiting a specific activity of approximately 40 micromol min(-1) mg protein(-1) and Michealis-Menten kinetic constants of approximately 1.4 mM for reduced glutathione and approximately 6.5 microM for APS. APR activity and expression were studied in relation to the production of 3-dimethylsulfoniopropionate (DMSP), a sulfonium compound produced by many marine algae. A diverse group of DMSP-producing species showed extremely high enzyme activity (up to 400 times that found in flowering plants). Antibodies raised against a conserved peptide of APR strongly cross-reacted with a protein of 45 kD in several chlorophytes but insignificantly with chromophytes. In the chlorophyte Tetraselmis sp., APR activity varies significantly during the culture cycle and does not follow the changes in cellular DMSP content. However, a positive correlation was found between cell-based APR activity and specific growth rate.

Indexed as

Oxidoreductases Acting on Sulfur Group DonorsAmino Acid SequenceCells, CulturedChlorophytaEscherichia coliGenetic Complementation TestMolecular Sequence DataOxidoreductasesPhytoplanktonRecombinant ProteinsSequence Homology, Amino AcidSulfonium CompoundsTime Factorsadenylylsulfate reductasedimethylpropiothetinOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsRecombinant ProteinsSulfonium Compounds

Identifiers

PMID10889258
PMCPMC59072
OpenAlexW2149020559

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.