Evidence map›Paper›PMID 34716632›Full record

ArticleProtein science : a publication of the Protein Society2022

Role of unique loops in oligomerization and ATPase function of Plasmodium falciparum gyrase B.

Monica Purushothaman, Suman Kumar Dhar, Ramanathan Natesh

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

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. 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 2 institutions in 1 country.

Monica PurushothamanSchool of Biology, Indian Institute of Science Education and Research Thiruvananthapuram, Thiruvananthapuram, Kerala, India.
Suman Kumar DharSpecial Centre of Molecular Medicine, Jawaharlal Nehru University, New Delhi, India.
Ramanathan NateshSchool of Biology, Indian Institute of Science Education and Research Thiruvananthapuram, Thiruvananthapuram, Kerala, India.ORCID 0000-0002-1145-5962
Indian Institute of Science Education and Research Thiruvananthapuram · INJawaharlal Nehru University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA gyrase is an ATP dependent Type IIA topoisomerase that is unique to prokaryotes. Interestingly DNA gyrase has also been found in the apicoplasts of apicomplexan parasites like Plasmodium falciparum (Pf) the causative agent of Malaria. Gyrase B (GyrB), a subunit of gyrase A

Indexed as

Adenosine TriphosphatasesDNA GyrasePlasmodium falciparumProtozoan ProteinsAdenosine TriphosphateDimerizationAdenosine TriphosphatasesAdenosine TriphosphateDNA GyraseProtozoan ProteinsATP hydrolysisbinding affinitycircular dichroismcoumermycingyrase Binhibitionisothermal titration calorimetryPlasmodium falciparum

Identifiers

PMID34716632
PMCPMC8820116
OpenAlexW3210724494

What Socratic 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 Socratic graph.