Evidence map›Paper›PMID 38191663›Full record

ArticleNature biotechnology2024

A palmitoyl transferase chemical-genetic system to map ZDHHC-specific S-acylation.

Cory A Ocasio, Marc P Baggelaar, James Sipthorp, Ana Losada de la Lastra, Manuel Tavares, Jana Volarić, Christelle Soudy, Elisabeth M Storck, Jack W Houghton, Susana A Palma-Duran and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Nature biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
11.0field-weighted citation impact, top 1% 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

37 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Biochemistry · 2026
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  7. Article
  8. Article
  9. Article
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  11. The Roles of ProteinCancer communications (London, England) · 2026
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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

16 authors at 4 institutions in 2 countries.

Cory A Ocasio *The Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-4957-4131
Marc P Baggelaar *The Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-9784-6250
James Sipthorp *The Francis Crick Institute, London, UK.
Ana Losada de la LastraThe Francis Crick Institute, London, UK.
Manuel TavaresThe Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-3048-5331
Jana VolarićImperial College London, Department of Chemistry, Molecular Sciences Research Hub, London, UK.
Christelle SoudyThe Francis Crick Institute, London, UK.
Elisabeth M StorckKing's College London, Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences and Department of Chemistry, London, UK.
Jack W HoughtonThe Francis Crick Institute, London, UK.
Susana A Palma-DuranThe Francis Crick Institute, London, UK.
James I MacRaeThe Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-1464-8583
Goran TomićThe Francis Crick Institute, London, UK.
Lotte CarrThe Francis Crick Institute, London, UK.
Julian DownwardThe Francis Crick Institute, London, UK.ORCID http://orcid.org/0000-0002-2331-4729
Ulrike S EggertKing's College London, Randall Centre for Cell and Molecular Biophysics, School of Basic and Medical Biosciences and Department of Chemistry, London, UK.ORCID http://orcid.org/0000-0003-0932-5525
Edward W TateThe Francis Crick Institute, London, UK. e.tate@imperial.ac.uk.ORCID http://orcid.org/0000-0003-2213-5814
The Francis Crick Institute · GBKing's College London · GBImperial College London · GBUniversity of Applied Sciences Utrecht · NL

Funding

Cancer Research UK 27506Cancer Research UK (CRUK) C24523/A27435Cancer Research UK (CRUK) C29637/A20183Cancer Research UK (CRUK) C29637/A27506Cancer Research UK (CRUK) DRCNPG-Nov21\100001Cancer Research UK (CRUK) NS/A000078/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) NS/A000078/1Wellcome Trust FC001070Wellcome Trust (Wellcome) 103799/Z/14/ZWellcome Trust (Wellcome) 110060/Z/15/Z
6 · The paper itself

Abstract

The 23 human zinc finger Asp-His-His-Cys motif-containing (ZDHHC) S-acyltransferases catalyze long-chain S-acylation at cysteine residues across an extensive network of hundreds of proteins important for normal physiology or dysregulated in disease. Here we present a technology to directly map the protein substrates of a specific ZDHHC at the whole-proteome level, in intact cells. Structure-guided engineering of paired ZDHHC 'hole' mutants and 'bumped' chemically tagged fatty acid probes enabled probe transfer to specific protein substrates with excellent selectivity over wild-type ZDHHCs. Chemical-genetic systems were exemplified for five human ZDHHCs (3, 7, 11, 15 and 20) and applied to generate de novo ZDHHC substrate profiles, identifying >300 substrates and S-acylation sites for new functionally diverse proteins across multiple cell lines. We expect that this platform will elucidate S-acylation biology for a wide range of models and organisms.

Indexed as

AcyltransferasesAcylationHumansSubstrate SpecificityAcyltransferases

Identifiers

PMID38191663
PMCPMC11471619
OpenAlexW4390669556

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.