Evidence map›Paper›PMID 34458436›Full record

ArticleBio-protocol2017

Aggregation Prevention Assay for Chaperone Activity of Proteins Using Spectroflurometry.

Manish Bhuwan, Madhuri Suragani, Nasreen Z Ehtesham, Seyed E Hasnain

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

Article in Bio-protocol, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. 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 at 3 institutions in 1 country.

Manish BhuwanMolecular Infection and Functional Biology Laboratory, Kusuma School of Biological Sciences, Indian Institute of Technology, New Delhi, India.
Madhuri SuraganiDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Professor C.R. Rao Road, Hyderabad, India.
Nasreen Z EhteshamInflammation Biology and Cell Signaling Laboratory, National Institute of Pathology, New Delhi, India.
Seyed E HasnainMolecular Infection and Functional Biology Laboratory, Kusuma School of Biological Sciences, Indian Institute of Technology, New Delhi, India.
Indian Institute of Technology Delhi · INJamia Hamdard · INNational Institute of Pathology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability to stabilize other proteins against thermal aggregation is one of the major characteristics of chaperone proteins. Molecular chaperones bind to nonnative conformations of proteins. Folding of the substrate is triggered by a dynamic association and dissociation cycles which keep the substrate protein on track of the folding pathway (Figure 1). Usually molecular chaperones exhibit differential affinities with different conformations of the substrate. With the exception of the sHsp family of molecular chaperones, the shift from a high-affinity binding state to the low-affinity release state is triggered by ATP binding and hydrolysis (Haselback and Buchner, 2015). Aggregation prevention assay is a simple, yet definitive assay to determine the chaperone activity of heat labile proteins such as Maltodextrin glucosidase (MalZ), Citrate Synthase (CS) and

Indexed as

ATPase activity assayGroELMolecular chaperoneMoxR1Refolding of Enzymes & ProteinsResistin proteinsThermal aggregation prevention

Identifiers

PMID34458436
PMCPMC8376500
OpenAlexW2586927290

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.