Evidence map›Paper›PMID 41813103›Full record

ReviewThe FEBS journal2026

A guide to mapping ubiquitin and ubiquitin-like E3 ligases to their substrates.

Laura Merino-Cacho, Claudia Guinea-Pérez, Mónica Pozo-Rodríguez, Sandra Cano-López, Juanma Ramirez, Orhi Barroso-Gomila, Ugo Mayor, James D Sutherland, Rosa Barrio

Abstract readReview
In one paragraph

Review in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

9 authors.

Laura Merino-CachoCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.ORCID https://orcid.org/0000-0003-1551-4074
Claudia Guinea-PérezCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.
Mónica Pozo-RodríguezCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.
Sandra Cano-LópezCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.
Juanma RamirezUniversity of the Basque Country, Biochemistry and Molecular Biology Department, Leioa, Spain.
Orhi Barroso-GomilaCell Signaling and Clinical Proteomics Group, Biobizkaia Health Research Institute, Barakaldo, Spain.
Ugo MayorUniversity of the Basque Country, Biochemistry and Molecular Biology Department, Leioa, Spain.ORCID https://orcid.org/0000-0003-2812-8287
James D SutherlandCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.ORCID https://orcid.org/0000-0003-3229-793X
Rosa BarrioCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.ORCID https://orcid.org/0000-0002-9663-0669

Funding

COST: European Cooperation for Science & Technology CA20113Diputación Foral de Bizkaia 6/12/TT/2023/00001Ministerio de Ciencia, Innovación y Universidades CEX2021-001136-SMinisterio de Ciencia, Innovación y Universidades CEX2021-001202-MMinisterio de Ciencia, Innovación y Universidades FPU20/05282Ministerio de Ciencia, Innovación y Universidades JDC2022-048335-IMinisterio de Ciencia, Innovación y Universidades PID2020-114178GB-I00Ministerio de Ciencia, Innovación y Universidades PID2020-117333GB-I00Ministerio de Ciencia, Innovación y Universidades PID2023-147399NB-I00Ministerio de Ciencia, Innovación y Universidades PRE2021-099359Ministerio de Ciencia, Innovación y Universidades PRE2022-104553Ministerio de Ciencia, Innovación y Universidades PREP2023-001398
6 · The paper itself

Abstract

Ubiquitination is a post-translational modification that plays a key role in the maintenance of protein homeostasis. Ubiquitin is covalently attached to the target proteins through a three-step enzymatic cascade in which substrate specificity is conferred by the E3 ligases. However, to match more than 600 E3s with their specific substrates is one of the major challenges in the field. The dynamic and reversible nature of ubiquitination requires the development of techniques to systematically address this question. Here we provide a comprehensive overview of the current methodologies used to reveal targets of E3 ligases, discussing their strengths and limitations. This is particularly relevant in light of emerging pharmacological strategies for targeted protein degradation.

Indexed as

UbiquitinUbiquitin-Protein LigasesAnimalsHumansProtein Processing, Post-TranslationalSubstrate SpecificityUbiquitinationUbiquitinUbiquitin-Protein LigasesE3 ligasespost‐translational modificationssubstrate identificationubiquitinubiquitin‐like proteins

Identifiers

PMID41813103
PMCPMC13580308

What Socratic 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 Socratic graph.