Evidence map›Paper›PMID 35424305›Full record

ArticleRSC advances2021

Impact of porous nanomaterials on inhibiting protein aggregation behaviour.

Munmun Bardhan, Sandip Dolui, Siddhi Chaudhuri, Uttam Paul, Gaurav Bhattacharjee, Manorama Ghosal, Nakul C Maiti, Debashis Mukhopadhyay, Dulal Senapati

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2021. 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
0.6field-weighted citation impact, top 34% 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, 13 citations in OpenAlex.

  1. Insulin and Human Serum Albumin Interactions with Core-Shell FeThe journal of physical chemistry. B · 2025
    Article
  2. Review
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

9 authors at 2 institutions in 3 countries.

Munmun BardhanChemical Sciences Division, Saha Institute of Nuclear Physics HBNI, 1/AF Bidhannagar Kolkata 700064 India dulal.senapati@saha.ac.in +91-9433139141.
Sandip DoluiIndian Institute of Chemical Biology Jadavpur Kolkata-700032 India.
Siddhi ChaudhuriBiophysics and Structural Genomics Division, Saha Institute of Nuclear Physics HBNI, 1/AF Bidhannagar Kolkata 700064 India.
Uttam PaulChemical Sciences Division, Saha Institute of Nuclear Physics HBNI, 1/AF Bidhannagar Kolkata 700064 India dulal.senapati@saha.ac.in +91-9433139141.ORCID https://orcid.org/0000-0003-2110-4610
Gaurav BhattacharjeeSurface Physics Division, Saha Institute of Nuclear Physics HBNI, 1/AF Bidhannagar Kolkata 700064 India.ORCID https://orcid.org/0000-0003-0796-7436
Manorama GhosalChemical Sciences Division, Saha Institute of Nuclear Physics HBNI, 1/AF Bidhannagar Kolkata 700064 India dulal.senapati@saha.ac.in +91-9433139141.
Nakul C MaitiBiophysics and Structural Genomics Division, Saha Institute of Nuclear Physics HBNI, 1/AF Bidhannagar Kolkata 700064 India.
Debashis MukhopadhyayBiophysics and Structural Genomics Division, Saha Institute of Nuclear Physics HBNI, 1/AF Bidhannagar Kolkata 700064 India.
Dulal SenapatiChemical Sciences Division, Saha Institute of Nuclear Physics HBNI, 1/AF Bidhannagar Kolkata 700064 India dulal.senapati@saha.ac.in +91-9433139141.ORCID https://orcid.org/0000-0001-5002-4631
Saha Institute of Nuclear Physics · INIndian Institute of Chemical Biology · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aggregation of intrinsically disordered as well as the ordered proteins under certain premises or physiological conditions leads to pathological disorder. Here we have presented a detailed investigation on the effect of a porous metallic (Au) and a non-metallic (Si) nanomaterial on the formation of ordered (fiber-like/amyloid) and disordered (amorphous) aggregates of proteins. Porous nanogold (PNG) was found to reduce the amyloid aggregation of insulin but does not have much impact on the lag phase in the aggregation kinetics, whereas porous nano-silica (PNS) was found both to decrease the amount of aggregation as well as prolong the lag phase of amyloid fiber formation from insulin. On the other hand, both the porous nanoparticles are found to decrease the extent of amorphous aggregation (with slight improvement for PNS) of pathogenic huntingtin (Htt) protein in Huntington's disease cell model. This is a noted direct observation in controlling and understanding protein aggregation diseases which may help us to formulate nanotherapeutic drugs for future clinical applications.

Identifiers

PMID35424305
PMCPMC8693984
OpenAlexW3126010167

What OpenQuestion holds

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LicenceCC BY-NC
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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.