Evidence map›Paper›PMID 34577034›Full record

ArticleMolecules (Basel, Switzerland)2021

Enabling Efficient Folding and High-Resolution Crystallographic Analysis of Bracelet Cyclotides.

Yen-Hua Huang, Qingdan Du, Zhihao Jiang, Gordon J King, Brett M Collins, Conan K Wang, David J Craik

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Protein Structure Determination by Racemic and Quasi-Racemic X-Ray Crystallography.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. D-Peptide and D-Protein Technology: Recent Advances, Challenges, and Opportunities.Chembiochem : a European journal of chemical biology · 2023
    Review
  6. Article
  7. Review
  8. 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

7 authors.

Yen-Hua HuangInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.ORCID 0000-0001-6937-2660
Qingdan DuInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.
Zhihao JiangInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.
Gordon J KingThe Centre for Microscopy and Microanalysis, The University of Queensland, Brisbane, QLD 4072, Australia.ORCID 0000-0001-5592-5789
Brett M CollinsInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.
Conan K WangInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.ORCID 0000-0002-7973-7632
David J CraikInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia.ORCID 0000-0003-0007-6796

Funding

Australian Research Council CE200100012Australian Research Council FL150100146National Health and Medical Research Council APP1136021
6 · The paper itself

Abstract

Cyclotides have attracted great interest as drug design scaffolds because of their unique cyclic cystine knotted topology. They are classified into three subfamilies, among which the bracelet subfamily represents the majority and comprises the most bioactive cyclotides, but are the most poorly utilized in drug design applications. A long-standing challenge has been the very low in vitro folding yields of bracelets, hampering efforts to characterize their structures and activities. Herein, we report substantial increases in bracelet folding yields enabled by a single point mutation of residue Ile-11 to Leu or Gly. We applied this discovery to synthesize mirror image enantiomers and used quasi-racemic crystallography to elucidate the first crystal structures of bracelet cyclotides. This study provides a facile strategy to produce bracelet cyclotides, leading to a general method to easily access their atomic resolution structures and providing a basis for development of biotechnological applications.

Indexed as

CyclotidesProtein FoldingAmino Acid SequenceCrystallography, X-RayModels, MolecularProtein ConformationCyclotidescrystal structurescyclic peptidescyclotidespeptidesquasi-racemic crystallography

Identifiers

PMID34577034
PMCPMC8467136

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.