Evidence map›Paper›PMID 33294634›Full record

ArticleBiochemistry and biophysics reports2020

A versatile tool in controlling aggregation and Ag nanoparticles assisted in vitro folding of thermally denatured zDHFR.

Preeti Gupta, Ritu Verma, Anita Kamra Verma, Pratima Chaudhuri Chattopadhyay

Abstract read
In one paragraph

Article in Biochemistry and biophysics 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
–field-weighted citation impact
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.

  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

4 authors.

Preeti GuptaMolecular Biophysics Lab, Amity Institute of Biotechnology, Amity University, Sector 125, Noida, Uttar Pradesh, 201313, India.
Ritu VermaMolecular Biophysics Lab, Amity Institute of Biotechnology, Amity University, Sector 125, Noida, Uttar Pradesh, 201313, India.
Anita Kamra VermaDepartment of Zoology, Kirori Mal College, University of Delhi, New Delhi, 110007, India.
Pratima Chaudhuri ChattopadhyayMolecular Biophysics Lab, Amity Institute of Biotechnology, Amity University, Sector 125, Noida, Uttar Pradesh, 201313, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProteins have tendency to form inactive aggregates at higher temperatures due to thermal instability. Maintenance of thermal stability is essential to gain the protein in sufficient quantity and biologically active form during their commercial production.

methodsBL21-DE3 Rosetta

resultsThe protein completely lost its activity at 55 °C. Kinetics of inactivated zDHFR follows first order model in presence and absence of AgNPs. Decrease in rate constant (

conclusionsAgNPs helps in maintaining thermostability and reducing the aggregation propensity of zDHFR protein. GENERAL SIGNIFICANCE: Result explains that AgNPs are recommended as a valuable system in enhancing the industrial production of biologically active zDHFR protein which is an important component in folate cycle and essential for survival of cells and prevents the protein from being aggregated.

Indexed as

AgNPs, Silver nanoparticlesDHF, Dihydrofolic acidGdnHCl, Guanidine hydrochlorideGSH, Reduced glutathioneGSSG, oxidized glutathioneInactivation rate constantIPTG, Isopropyl d-1thiogalactopyranosideNADPH, Nicotinamide adenine dinucleotide phosphateRefolding studiesSilver nanoparticlesStabilityThermodynamic parametersTHF, tetrahydrofolateZebrafish dihydrofolate

Identifiers

PMID33294634
PMCPMC7695922

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.