Evidence map›Paper›PMID 34723257›Full record

ReviewJACS Au2021

Aminovinyl Cysteine Containing Peptides: A Unique Motif That Imparts Key Biological Activity.

Emily S Grant-Mackie, Elyse T Williams, Paul W R Harris, Margaret A Brimble

Abstract readReview
In one paragraph

Review in JACS Au, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. 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

4 authors.

Emily S Grant-MackieSchool of Chemical Sciences, The University of Auckland, 23 Symonds Street, Auckland 1132, New Zealand.
Elyse T WilliamsSchool of Chemical Sciences, The University of Auckland, 23 Symonds Street, Auckland 1132, New Zealand.
Paul W R HarrisSchool of Chemical Sciences, The University of Auckland, 23 Symonds Street, Auckland 1132, New Zealand.ORCID https://orcid.org/0000-0002-2579-4543
Margaret A BrimbleSchool of Chemical Sciences, The University of Auckland, 23 Symonds Street, Auckland 1132, New Zealand.ORCID https://orcid.org/0000-0002-7086-4096

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural products that contain distinctive chemical functionality can serve as useful starting points to develop Nature's compounds into viable therapeutics. Peptide natural products, an under-represented class of medicines, such as ribosomally synthesized and post-translationally modified peptides (RiPPs), often contain noncanonical amino acids and structural motifs that give rise to potent biological activity. However, these motifs can be difficult to obtain synthetically, thereby limiting the transition of RiPPs to the clinic. Aminovinyl cysteine containing peptides, which display potent antimicrobial or anticancer activity, possess an intricate C-terminal ring that is critical for bioactivity. To date, successful methods for the total chemical synthesis of such peptides are yet to be realized, although several advancements have been achieved. In this perspective, we review this burgeoning class of aminovinyl cysteine peptides and critically evaluate the chemical strategies to install the distinct aminovinyl cysteine motif.

Identifiers

PMID34723257
PMCPMC8549060

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.