Evidence map›Paper›PMID 34611966›Full record

ReviewAngewandte Chemie (International ed. in English)2022

Chemical Synthesis and Semisynthesis of Lipidated Proteins.

Cameron C Hanna, Julia Kriegesmann, Luke J Dowman, Christian F W Becker, Richard J Payne

Abstract readReview
In one paragraph

Review in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review on the o-Aminoaniline Moiety in Peptide and Protein Chemistry.Chembiochem : a European journal of chemical biology · 2025
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Enzymatic Fluoromethylation as a Tool for ATP-Independent Ligation.Angewandte Chemie (International ed. in English) · 2024
    Article
  17. Enzymatic Fluoromethylation as a Tool for ATP-Independent Ligation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  18. Review
  19. Article
  20. 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

5 authors.

Cameron C HannaSchool of Chemistry, The University of Sydney, Sydney, NSW, 2006, Australia.ORCID 0000-0002-8809-6232
Julia KriegesmannInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Vienna, Austria.ORCID 0000-0003-3852-5147
Luke J DowmanSchool of Chemistry, The University of Sydney, Sydney, NSW, 2006, Australia.ORCID 0000-0002-9728-5166
Christian F W BeckerInstitute of Biological Chemistry, Faculty of Chemistry, University of Vienna, Vienna, Austria.ORCID 0000-0002-8890-7082
Richard J PayneSchool of Chemistry, The University of Sydney, Sydney, NSW, 2006, Australia.ORCID 0000-0002-3618-9226

Funding

Austrian Science Fund FWF P 29458
6 · The paper itself

Abstract

Lipidation is a ubiquitous modification of peptides and proteins that can occur either co- or post-translationally. An array of different lipid classes can adorn proteins and has been shown to influence a number of crucial biological activities, including the regulation of signaling, cell-cell adhesion events, and the anchoring of proteins to lipid rafts and phospholipid membranes. Whereas nature employs a range of enzymes to install lipid modifications onto proteins, the use of these for the chemoenzymatic generation of lipidated proteins is often inefficient or impractical. An alternative is to harness the power of modern synthetic and semisynthetic technologies to access lipid-modified proteins in a pure and homogeneously modified form. This Review aims to highlight significant advances in the development of lipidation and ligation chemistry and their implementation in the synthesis and semisynthesis of homogeneous lipidated proteins that have enabled the influence of these modifications on protein structure and function to be uncovered.

Indexed as

PeptidesProteinsLipid MetabolismLipidsLipidsPeptidesProteinschemical protein synthesislipidated proteinlipopeptidespost-translational modificationsemisynthesis

Identifiers

PMID34611966
PMCPMC9303669

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.