Evidence map›Paper›PMID 32117877›Full record

ArticleFrontiers in chemistry2020

Pristine and Hydroxylated Fullerenes Prevent the Aggregation of Human Islet Amyloid Polypeptide and Display Different Inhibitory Mechanisms.

Cuiqin Bai, Zenghui Lao, Yujie Chen, Yiming Tang, Guanghong Wei

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

Article in Frontiers in chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 37 citations in OpenAlex.

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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 at 1 institution in 1 country.

Cuiqin BaiState Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.
Zenghui LaoState Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.
Yujie ChenState Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.
Yiming TangState Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.
Guanghong WeiState Key Laboratory of Surface Physics, and Key Laboratory for Computational Physical Science (Ministry of Education), Department of Physics, Multiscale Research Institute of Complex Systems, Fudan University, Shanghai, China.
Fudan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregation, involving the formation of dimers, oligomers, and fibrils, is associated with many human diseases. Type 2 diabetes is one of the common amyloidosis and linked with the aggregation of human islet amyloid polypeptide (hIAPP). A series of nanoparticles are reported to be able to interact with proteins and enhance/inhibit protein aggregation. However, the effects of C

Indexed as

C60hIAPP aggregationinhibitory mechanismreplica exchange molecular dynamics simulationstype 2 diabetes

Identifiers

PMID32117877
PMCPMC7013002
OpenAlexW3004970917

What Socratic 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 Socratic graph.