Evidence map›Paper›PMID 17089214›Full record

ArticlePhotosynthesis research2006

Transferring redox regulation properties from sorghum NADP-malate dehydrogenase to Thermus NAD-malate dehydrogenase.

Emmanuelle Issakidis-Bourguet, Danièle Lavergne, Xavier Trivelli, Paulette Decottignies, Myroslawa Miginiac-Maslow

Abstract read
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In one paragraph

Article in Photosynthesis research, 2006. 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
0.3field-weighted citation impact, top 43% 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, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Thioredoxins in chloroplasts.Current genetics · 2007
    Review
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 1 country.

Emmanuelle Issakidis-BourguetInstitut de Biotechnologie des Plantes, UMR CNRS 8618, Bât. 630, Université Paris-Sud, 91405, Orsay Cedex, France. issakidi@ibp.u-psud.fr
Danièle Lavergne
Xavier Trivelli
Paulette Decottignies
Myroslawa Miginiac-Maslow
Centre National de la Recherche Scientifique · FRUnité de Glycobiologie Structurale et Fonctionnelle · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NADP-dependent chloroplastic malate dehydrogenase (E.C.1.1.1.82) is regulated by thiol disulfide-interchange with thioredoxin. It displays two regulatory disulfides per subunit, located in specific sequence extensions respectively at the N- and C-terminal ends of each subunit. In the present study, attempts were made to transfer the regulatory properties of sorghum NADP-malate dehydrogenase to a constitutively active NAD-dependent malate dehydogenase (E.C.1.1.1.37) from the thermophilic bacteria Thermus flavus, by grafting the regulatory extensions of the former to the latter. The results demonstrate that a successful transfer of redox regulation properties requires the grafting of both full-length extensions, but also the introduction of specific hydrophobic residues in the core part of the protein. These residues are very likely involved in the interaction between monomers, and structural changes at the active site.

Indexed as

Protein EngineeringAmino Acid SequenceMalate DehydrogenaseMalate Dehydrogenase (NADP+)Models, MolecularMutant Chimeric ProteinsOxidation-ReductionProtein ConformationSorghumThermusMalate DehydrogenaseMalate Dehydrogenase (NADP+)Mutant Chimeric Proteins

Identifiers

PMID17089214
OpenAlexW2033437323

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.