Evidence map›Paper›PMID 32198136›Full record

ArticleThe Journal of biological chemistry2020

Structural and mutational analyses of the bifunctional arginine dihydrolase and ornithine cyclodeaminase AgrE from the cyanobacterium

Haehee Lee, Sangkee Rhee

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

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
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  4. Isolation ofMolecules (Basel, Switzerland) · 2023
    Article
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  6. Review
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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

2 authors at 1 institution in 1 country.

Haehee LeeDepartment of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Korea.
Sangkee RheeDepartment of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Korea; Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 151-921, Korea. Electronic address: srheesnu@snu.ac.kr.
Seoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In cyanobacteria, metabolic pathways that use the nitrogen-rich amino acid arginine play a pivotal role in nitrogen storage and mobilization. The N-terminal domains of two recently identified bacterial enzymes: ArgZ from

Indexed as

Ammonia-LyasesAnabaenaBacterial ProteinsCatalytic DomainCrystallography, X-RayHydrolasesModels, MolecularMutationProtein ConformationProtein MultimerizationSubstrate SpecificityAmmonia-Lyasesarginine deiminaseBacterial ProteinsHydrolasesornithine cyclodeaminaseammonia productionarginine catabolismcatalytic triadcrystal structurecyanobacteriaenzyme catalysisenzyme structurenitrogen remobilizationsubstrate channelingX-ray crystallography

Identifiers

PMID32198136
PMCPMC7186175
OpenAlexW3011845373

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.