Evidence map›Paper›PMID 29110596›Full record

ReviewCurrent medicinal chemistry2019

γ-AApeptides as a New Strategy for Therapeutic Development.

Alekhya Nimmagadda, Yan Shi, Jianfeng Cai

Abstract readReview
In one paragraph

Review in Current medicinal chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Development of Low-Toxicity Antimicrobial Polycarbonates Bearing Lysine Residues.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Current and Future Treatments in Alzheimer Disease: An Update.Journal of central nervous system disease · 2020
    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

3 authors.

Alekhya NimmagaddaDepartment of Chemistry, University of South Florida, 4202 E. Fowler Ave, Tampa, FL 33620, United States.
Yan ShiDepartment of Chemistry, University of South Florida, 4202 E. Fowler Ave, Tampa, FL 33620, United States.
Jianfeng CaiDepartment of Chemistry, University of South Florida, 4202 E. Fowler Ave, Tampa, FL 33620, United States.

Funding

Requesting HPLC for the project of "Alpha-AApeptides as a Novel Class of Antimicrobial Biomaterials"R01GM112652 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI CAI, JIANFENG · 2015 to 2019
$1.5M
NIGMS NIH HHS R01 GM112652
6 · The paper itself

Abstract

A new class of peptidomimetics termed as "γ-AApeptides" was recently developed by our group. Similar to other peptidomimetics, γ-AApeptides are resistant to proteolytic degradation, and possess limitless potential to introduce chemically diverse functional groups. γ-AApeptides have shown great promise in biomedical applications. In this article, we will review a few examples of γ-AApeptides with biological potential. Certain γ-AApeptides can permeate cell membranes and therefore they can be used as potential drug carrier. γ-AApeptides can also bind to HIV RNA with high specificity and affinity, suggesting their potential application as anti-HIV agents. Moreover, they can mimic host-defense peptides and display potent and broad-spectrum activity towards a range of drug-resistant bacterial pathogens. They are also potential anti-cancer agents. For instance, they have shown great promise in targeted imaging of tumor in mouse model, and they are also capable of disrupting p53/DNA interactions, and thus antagonize STAT3 signaling pathway. Recently, from combinatorial screening, γ-AApeptides are identified to inhibit Aβ peptide aggregation, and thus they can be developed into potential anti- Alzheimer's disease agent.

Indexed as

Amyloid beta-PeptidesAnimalsAnti-Bacterial AgentsAnti-HIV AgentsAntineoplastic AgentsCell Line, TumorHumansPeptide FragmentsPeptides, CyclicPeptidomimeticsProtein Conformation, alpha-HelicalProtein MultimerizationAmyloid beta-Peptidesamyloid beta-protein (1-40)Anti-Bacterial AgentsAnti-HIV AgentsAntineoplastic AgentsPeptide FragmentsPeptides, CyclicPeptidomimeticsanti-Aβ aggregationanticancer activityanti-HIV activityantimicrobial activitypeptidomimeticsstructuresγ-AApeptides.

Identifiers

PMID29110596
PMCPMC5936681

What OpenQuestion holds

Textmetadata
LicenceTDM
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.