Evidence map›Paper›PMID 24611007›Full record

ReviewInternational journal of nanomedicine2014

Nanoparticles in relation to peptide and protein aggregation.

Masihuz Zaman, Ejaz Ahmad, Atiyatul Qadeer, Gulam Rabbani, Rizwan Hasan Khan

Abstract readReview
In one paragraph

Review in International journal of nanomedicine, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
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  10. Review
  11. Nanoformulation of SeaweedMarine drugs · 2022
    Article
  12. Article
  13. Nanoparticles Influence Lytic Phage T4-like Performance In Vitro.International journal of molecular sciences · 2022
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
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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

5 authors.

Masihuz ZamanInterdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.
Ejaz AhmadInterdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.
Atiyatul QadeerInterdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.
Gulam RabbaniInterdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.
Rizwan Hasan KhanInterdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over the past two decades, there has been considerable research interest in the use of nanoparticles in the study of protein and peptide aggregation, and of amyloid-related diseases. The influence of nanoparticles on amyloid formation yields great interest due to its small size and high surface area-to-volume ratio. Targeting nucleation kinetics by nanoparticles is one of the most searched for ways to control or induce this phenomenon. The observed effect of nanoparticles on the nucleation phase is determined by particle composition, as well as the amount and nature of the particle's surface. Various thermodynamic parameters influence the interaction of proteins and nanoparticles in the solution, and regulate the protein assembly into fibrils, as well as the disaggregation of preformed fibrils. Metals, organic particles, inorganic particles, amino acids, peptides, proteins, and so on are more suitable candidates for nanoparticle formulation. In the present review, we attempt to explore the effects of nanoparticles on protein and peptide fibrillation processes from both perspectives (ie, as inducers and inhibitors on nucleation kinetics and in the disaggregation of preformed fibrils). Their formulation and characterization by different techniques have been also addressed, along with their toxicological effects, both in vivo and in vitro.

Indexed as

Protein AggregatesAlbuminsAmyloidAnimalsHumansMetal NanoparticlesNanomedicineNanoparticlesNanotechnologyPeptidesAlbuminsAmyloidPeptidesProtein Aggregatesamyloid formationinducerinhibitornanoparticlenucleationtoxicity

Identifiers

PMID24611007
PMCPMC3928455

What OpenQuestion holds

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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.