Purification, characterization and functional site prediction of the vaccinia-related kinase 2A small transmembrane domain.

Rashmi Puja, Ayon Chakraborty, Shubhankar Dutta, Kakoli Bose

Open access · goldAbstract read

In one paragraph

Article in MethodsX, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.1field-weighted citation impact, top 71% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 1 country.

Rashmi PujaIntegrated Biophysics and Structural Biology Lab, ACTREC, Tata Memorial Centre, Tata Memorial Centre, Sector 22, Kharghar, Navi Mumbai 410210, India.

Ayon ChakrabortyIntegrated Biophysics and Structural Biology Lab, ACTREC, Tata Memorial Centre, Tata Memorial Centre, Sector 22, Kharghar, Navi Mumbai 410210, India.

Shubhankar DuttaIntegrated Biophysics and Structural Biology Lab, ACTREC, Tata Memorial Centre, Tata Memorial Centre, Sector 22, Kharghar, Navi Mumbai 410210, India.

Kakoli BoseIntegrated Biophysics and Structural Biology Lab, ACTREC, Tata Memorial Centre, Tata Memorial Centre, Sector 22, Kharghar, Navi Mumbai 410210, India.

Advanced Centre for Treatment, Research and Education in Cancer · INTata Memorial Hospital · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vaccinia-related kinases (VRK) are serine-threonine kinases that regulate several signaling pathways. The isoform-VRK2A of one such kinase VRK2 controls cell stress response by interacting with TAK1, a mitogen-activated protein 3 kinase (MAP3K), via its partly cytosolic C-terminal transmembrane domain (VTMD). To establish the driving force and identify the key residues of the VRK2A-TAK1 interaction, we expressed and purified the standalone 3.6 kDa VTMD in the bacterial system using a unique and atypical two-step approach, when the effort to obtain full-length VRK2A remained unsuccessful. Characterization of biophysical properties demonstrated that VTMD domain maintains its structural integrity. Furthermore, dissecting the VRK2A-TAK1 binding interface using

Indexed as

Molecular dockingProtein-protein interactionSmall protein purificationTAK1Transmembrane domainVRK2A

Identifiers

PMID35518920

DOI10.1016/j.mex.2022.101704

PMCPMC9062753

OpenAlexW4223994498

What OpenQuestion holds

Textmetadata

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.