Evidence map›Paper›PMID 38424304›Full record

ReviewNature reviews. Cancer2024

Protein lipidation in cancer: mechanisms, dysregulation and emerging drug targets.

Edward W Tate, Lior Soday, Ana Losada de la Lastra, Mei Wang, Hening Lin

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Cancer, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
13.4field-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

28 citing papers in PubMed, 41 citations in OpenAlex.

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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

5 authors at 4 institutions in 3 countries.

Edward W TateDepartment of Chemistry, Imperial College London, London, UK. e.tate@imperial.ac.uk.ORCID http://orcid.org/0000-0003-2213-5814
Lior SodayDepartment of Chemistry, Imperial College London, London, UK.ORCID http://orcid.org/0000-0001-6927-2985
Ana Losada de la LastraDepartment of Chemistry, Imperial College London, London, UK.
Mei WangProgram in Cancer and Stem Cell Biology, Duke-NUS Medical School, Singapore, Singapore.ORCID http://orcid.org/0000-0001-6887-6840
Hening LinHoward Hughes Medical Institute, Cornell University, Ithaca, NY, USA.ORCID http://orcid.org/0000-0002-0255-2701
Imperial College London · GBHoward Hughes Medical Institute · USNational University of Singapore · SGThe Francis Crick Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein lipidation describes a diverse class of post-translational modifications (PTMs) that is regulated by over 40 enzymes, targeting more than 1,000 substrates at over 3,000 sites. Lipidated proteins include more than 150 oncoproteins, including mediators of cancer initiation, progression and immunity, receptor kinases, transcription factors, G protein-coupled receptors and extracellular signalling proteins. Lipidation regulates the physical interactions of its protein substrates with cell membranes, regulating protein signalling and trafficking, and has a key role in metabolism and immunity. Targeting protein lipidation, therefore, offers a unique approach to modulate otherwise undruggable oncoproteins; however, the full spectrum of opportunities to target the dysregulation of these PTMs in cancer remains to be explored. This is attributable in part to the technological challenges of identifying the targets and the roles of protein lipidation. The early stage of drug discovery for many enzymes in the pathway contrasts with efforts for drugging similarly common PTMs such as phosphorylation and acetylation, which are routinely studied and targeted in relevant cancer contexts. Here, we review recent advances in identifying targetable protein lipidation pathways in cancer, the current state-of-the-art in drug discovery, and the status of ongoing clinical trials, which have the potential to deliver novel oncology therapeutics targeting protein lipidation.

Indexed as

NeoplasmsProtein Processing, Post-TranslationalHumansOncogene ProteinsPhosphorylationTranscription FactorsOncogene ProteinsTranscription Factors

Identifiers

PMID38424304
OpenAlexW4392298160

What OpenQuestion holds

Textmetadata
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.