Evidence map›Paper›PMID 30635453›Full record

ReviewThe Biochemical journal2019

Using backbone-cyclized Cys-rich polypeptides as molecular scaffolds to target protein-protein interactions.

Dipankar Chaudhuri, Teshome Aboye, Julio A Camarero

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

14 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Lipidation of a bioactive cyclotide-based CXCR4 antagonist greatly improves its pharmacokinetic profile in vivo.Journal of controlled release : official journal of the Controlled Release Society · 2023
    Article
  7. Article
  8. Review
  9. Engineered Cyclotides with Potent Broad in Vitro and in Vivo Antimicrobial Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  10. Plant derived cyclic peptides.Biochemical Society transactions · 2021
    Review
  11. Review
  12. Review
  13. Recombinant Expression of Cyclotides Using Expressed Protein Ligation.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  14. 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 at 1 institution in 1 country.

Dipankar ChaudhuriDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, CA 90089-9121, U.S.A.
Teshome AboyeDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, CA 90089-9121, U.S.A.
Julio A CamareroDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California, Los Angeles, CA 90089-9121, U.S.A. jcamarer@usc.edu.ORCID 0000-0001-9150-0665
University of Southern California · US

Funding

Using the Ultrastable Cyclotide Scaffold to Modulate Protein-protein InteractionsR35GM132072 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CAMARERO, JULIO A · 2019 to 2023
$2.3M
Screening and selection of specific protein-protein antagonists using ultrastable microprotein scaffoldsR01GM113636 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CAMARERO, JULIO A · 2015 to 2018
$1.3M
NIGMS NIH HHS R01 GM113636NIGMS NIH HHS R35 GM132072
6 · The paper itself

Abstract

The use of disulfide-rich backbone-cyclized polypeptides, as molecular scaffolds to design a new generation of bioimaging tools and drugs that are potent and specific, and thus might have fewer side effects than traditional small-molecule drugs, is gaining increasing interest among the scientific and in the pharmaceutical industries. Highly constrained macrocyclic polypeptides are exceptionally more stable to chemical, thermal and biological degradation and show better biological activity when compared with their linear counterparts. Many of these relatively new scaffolds have been also found to be highly tolerant to sequence variability, aside from the conserved residues forming the disulfide bonds, able to cross cellular membranes and modulate intracellular protein-protein interactions both

Indexed as

CyclotidesDefensinsModels, MolecularMolecular ImagingPeptides, CyclicAnimalsCyclizationDisulfidesHumansCyclotidesDefensinsDisulfidesPeptides, CyclicSFTI-1 peptide, sunflowertheta-defensinCCKcyclic peptidescyclotidescystine knotdrug designprotein–protein interactions

Identifiers

PMID30635453
PMCPMC7080216
OpenAlexW2908739336

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.