Evidence map›Paper›PMID 32107404›Full record

ArticleScientific reports2020

Oligomerization and characteristics of phosphoenolpyruvate carboxylase in Synechococcus PCC 7002.

Claudia Durall, Sandesh Kanchugal P, Maria Selmer, Peter Lindblad

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2020. 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
0.2field-weighted citation impact, top 51% 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, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

4 authors at 1 institution in 1 country.

Claudia DurallMicrobial Chemistry, Department of Chemistry - Ångström, Uppsala University, P.O. Box 523, SE-751 20, Uppsala, Sweden.
Sandesh Kanchugal PDepartment of Cell and Molecular Biology, BMC, Uppsala University, P.O. Box 596, SE-751 24, Uppsala, Sweden.
Maria SelmerDepartment of Cell and Molecular Biology, BMC, Uppsala University, P.O. Box 596, SE-751 24, Uppsala, Sweden.
Peter LindbladMicrobial Chemistry, Department of Chemistry - Ångström, Uppsala University, P.O. Box 523, SE-751 20, Uppsala, Sweden. peter.lindblad@kemi.uu.se.
Uppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoenolpyruvate carboxylase (PEPc) is an essential enzyme in plants. A photosynthetic form is present both as dimer and tetramer in C4 and CAM metabolism. Additionally, non-photosynthetic PEPcs are also present. The single, non-photosynthetic PEPc of the unicellular cyanobacterium Synechococcus PCC 7002 (Synechococcus), involved in the TCA cycle, was examined. Using size exclusion chromatography (SEC) and small angle X-ray scattering (SAXS), we observed that PEPc in Synechococcus exists as both a dimer and a tetramer. This is the first demonstration of two different oligomerization states of a non-photosynthetic PEPc. High concentration of Mg

Indexed as

Allosteric RegulationBacterial ProteinsChromatography, GelCrystallizationCrystallography, X-RayDimerizationEscherichia coliGlutamineMagnesiumPhosphoenolpyruvate CarboxylaseProtein ConformationScattering, Small AngleSynechococcusBacterial ProteinsGlutamineMagnesiumPhosphoenolpyruvate Carboxylase

Identifiers

PMID32107404
PMCPMC7046716
OpenAlexW3009072866

What OpenQuestion holds

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LicenceCC BY
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.