Evidence map›Paper›PMID 38107173›Full record

ReviewRSC medicinal chemistry2023

Stabilized cyclic peptides as modulators of protein-protein interactions: promising strategies and biological evaluation.

Jiongjia Cheng, Junlong Zhou, Lingyan Kong, Haiying Wang, Yuchi Zhang, Xiaofeng Wang, Guangxiang Liu, Qian Chu

Open access · greenAbstract readReview
In one paragraph

Review in RSC medicinal chemistry, 2023. 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
4.3field-weighted citation impact, top 5% 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, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. β-Hairpin Peptidomimetics for Protein-Protein Interaction Inhibition.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. Review
  6. Review
  7. Article
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

8 authors at 3 institutions in 1 country.

Jiongjia ChengKey Laboratory of Advanced Functional Materials of Nanjing, School of Environmental Science, Nanjing Xiaozhuang University 3601 Hongjing Avenue Nanjing 211171 China liugx@njxzc.edu.cn.
Junlong ZhouDepartment of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University 639 Longmian Avenue Nanjing 211198 China qianchu@cpu.edu.cn.
Lingyan KongCollege of Food Science and Engineering, Nanjing University of Finance and Economics Nanjing 210023 China.
Haiying WangKey Laboratory of Advanced Functional Materials of Nanjing, School of Environmental Science, Nanjing Xiaozhuang University 3601 Hongjing Avenue Nanjing 211171 China liugx@njxzc.edu.cn.ORCID https://orcid.org/0000-0002-0057-7745
Yuchi ZhangKey Laboratory of Advanced Functional Materials of Nanjing, School of Environmental Science, Nanjing Xiaozhuang University 3601 Hongjing Avenue Nanjing 211171 China liugx@njxzc.edu.cn.ORCID https://orcid.org/0000-0002-7413-7232
Xiaofeng WangKey Laboratory of Advanced Functional Materials of Nanjing, School of Environmental Science, Nanjing Xiaozhuang University 3601 Hongjing Avenue Nanjing 211171 China liugx@njxzc.edu.cn.
Guangxiang LiuKey Laboratory of Advanced Functional Materials of Nanjing, School of Environmental Science, Nanjing Xiaozhuang University 3601 Hongjing Avenue Nanjing 211171 China liugx@njxzc.edu.cn.
Qian ChuDepartment of Medicinal Chemistry, School of Pharmacy, China Pharmaceutical University 639 Longmian Avenue Nanjing 211198 China qianchu@cpu.edu.cn.ORCID https://orcid.org/0000-0001-6550-6975
Nanjing Xiaozhuang University · CNChina Pharmaceutical University · CNNanjing University of Finance and Economics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interactions (PPIs) control many essential biological pathways which are often misregulated in disease. As such, selective PPI modulators are desirable to unravel complex functions of PPIs and thus expand the repertoire of therapeutic targets. However, the large size and relative flatness of PPI interfaces make them challenging molecular targets for conventional drug modalities, rendering most PPIs "undruggable". Therefore, there is a growing need to discover innovative molecules that are able to modulate crucial PPIs. Peptides are ideal candidates to deliver such therapeutics attributed to their ability to closely mimic structural features of protein interfaces. However, their inherently poor proteolysis resistance and cell permeability inevitably hamper their biomedical applications. The introduction of a constraint (

Identifiers

PMID38107173
PMCPMC10718590
OpenAlexW4387816840

What OpenQuestion holds

Textmetadata
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.