Evidence map›Paper›PMID 34202166›Full record

ArticleInternational journal of molecular sciences2021

A Novel Cu(II)-Binding Peptide Identified by Phage Display Inhibits Cu

Xiaoyu Zhang, Xiancheng Zhang, Manli Zhong, Pu Zhao, Chuang Guo, You Li, He Xu, Tao Wang, Huiling Gao

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. 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
2.3field-weighted citation impact, top 11% 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, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Mechanism of Metal Complexes in Alzheimer's Disease.International journal of molecular sciences · 2024
    Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Peptide-Based Materials That Exploit Metal Coordination.International journal of molecular sciences · 2022
    Review
  9. 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 3 institutions in 1 country.

Xiaoyu ZhangCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, China.
Xiancheng ZhangCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, China.
Manli ZhongCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, China.
Pu ZhaoCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, China.
Chuang GuoCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, China.
You LiCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, China.
He XuDepartment of Histology and Embryology, School of Medicine, Shenzhen University, Shenzhen 518060, China.ORCID 0000-0002-9087-9041
Tao WangCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, China.
Huiling GaoCollege of Life and Health Sciences, Northeastern University, Shenyang 110819, China.
Northeastern University · CNDalian Institute of Chemical Physics · CNShenzhen University · CN

Funding

Fundamental Research Funds for the Central Universities of China N2020004National Natural Science Foundation of China 31970967National Natural Science Foundation of China 81301102National Natural Science Foundation of China 81600941National Natural Science Foundation of China 81771174National Natural Science Foundation of China 81971015the 111 Project B16009the Basic Scientific Research Fund of Northeastern University N2020002
6 · The paper itself

Abstract

Copper (Cu) has been implicated in the progression of Alzheimer's disease (AD), and aggregation of Cu and amyloid β peptide (Aβ) are considered key pathological features of AD. Metal chelators are considered to be potential therapeutic agents for AD because of their capacity to reduce metal ion-induced Aβ aggregation through the regulation of metal ion distribution. Here, we used phage display technology to screen, synthesize, and evaluate a novel Cu(II)-binding peptide that specifically blocked Cu-triggered Aβ aggregation. The Cu(II)-binding peptide (S-A-Q-I-A-P-H, PCu) identified from the phage display heptapeptide library was used to explore the mechanism of PCu inhibition of Cu

Indexed as

Protein AggregatesProtein Interaction MappingAmino Acid SequenceAmyloid beta-PeptidesAnimalsCarrier ProteinsCell Surface Display TechniquesCopperHumansMiceOxidation-ReductionOxidative StressPeptidesProtein Aggregation, PathologicalAmyloid beta-PeptidesCarrier ProteinsCoppercopper-binding proteinPeptidesProtein AggregatesAlzheimer’s diseaseAβCu(II)metal-binding peptidephage display

Identifiers

PMID34202166
PMCPMC8269028
OpenAlexW3175380629

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.