Mapping N- and C-terminals of Leishmania donovani tyrosine aminotransferase by gene truncation strategy: a functional study using in vitro and in silico approaches.

Santanu Sasidharan, Prakash Saudagar

Open access · goldAbstract read

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 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

2.3field-weighted citation impact, top 11% 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, 15 citations in OpenAlex.

Highly flexible metabolism of the marine euglenozoan protist Diplonema papillatum.BMC biology · 2021
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

2 authors at 1 institution in 1 country.

Santanu SasidharanDepartment of Biotechnology, National Institute of Technology, Warangal, Telangana, 506004, India.

Prakash SaudagarDepartment of Biotechnology, National Institute of Technology, Warangal, Telangana, 506004, India. ps@nitw.ac.in.

National Institute of Technology Warangal · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tyrosine aminotransferase (TAT) catalyzes the transamination of amino acids in Leishmania sp.. TAT from Leishmania donovani has been found to be extremely stable at extreme temperatures and pH conditions. This study was conceived to map the functions of the non-conserved N-terminal and conserved C-terminal domain of TAT. N-terminal (NTAT) and C-terminal (CTAT) domain of TAT was truncated and cloned into the pET28a(+) vector. The truncated proteins were expressed, purified, and biochemically characterized. The K

Indexed as

Amino Acid SequenceCatalytic DomainComputer SimulationHumansKineticsLeishmania donovaniLeishmaniasis, VisceralProtein DomainsProtozoan ProteinsSequence AlignmentTyrosine TransaminaseProtozoan ProteinsTyrosine Transaminase

Identifiers

PMID32719483

DOI10.1186/1756-0500-5-367

PMCPMC7385629

OpenAlexW3044544192

What OpenQuestion holds

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LicenceCC BY

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Registered trials

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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.