Evidence map›Paper›PMID 28587164›Full record

ReviewMolecules (Basel, Switzerland)2017

Chemical Methods to Knock Down the Amyloid Proteins.

Na Gao, Yong-Xiang Chen, Yu-Fen Zhao, Yan-Mei Li

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Targeted protein degradation: from mechanisms to clinic.Nature reviews. Molecular cell biology · 2024
    Review
  2. Self-Blinking Thioflavin T for Super-resolution Imaging.The journal of physical chemistry letters · 2024
    Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. PROTACs: great opportunities for academia and industry.Signal transduction and targeted therapy
    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

4 authors at 1 institution in 1 country.

Na GaoKey Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China. gaona_chocolate@126.com.
Yong-Xiang ChenKey Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China. chen-yx@mail.tsinghua.edu.cn.
Yu-Fen ZhaoKey Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China. yfzhao@xmu.edu.cn.
Yan-Mei LiKey Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China. liym@mail.tsinghua.edu.cn.
Tsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid proteins are closely related with amyloid diseases and do tremendous harm to human health. However, there is still a lack of effective strategies to treat these amyloid diseases, so it is important to develop novel methods. Accelerating the clearance of amyloid proteins is a favorable method for amyloid disease treatment. Recently, chemical methods for protein reduction have been developed and have attracted much attention. In this review, we focus on the latest progress of chemical methods that knock down amyloid proteins, including the proteolysis-targeting chimera (PROTAC) strategy, the "recognition-cleavage" strategy, the chaperone-mediated autophagy (CMA) strategy, the selectively light-activatable organic and inorganic molecules strategy and other chemical strategies.

Indexed as

Amyloidogenic ProteinsAutophagyMolecular ChaperonesProteasome Endopeptidase ComplexProtein BindingProteolysisStructure-Activity RelationshipUbiquitinsAmyloidogenic ProteinsMolecular ChaperonesProteasome Endopeptidase ComplexUbiquitinsamyloid proteinschemical methodsdegradation

Identifiers

PMID28587164
PMCPMC6152772
OpenAlexW2620636819

What OpenQuestion 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 OpenQuestion graph.