Evidence map›Paper›PMID 40763985›Full record

ArticleLife science alliance2025

Tuning ubiquitin transfer by RING E3 ubiquitin ligases through the linchpin residue.

Mark A Nakasone, Lori Buetow, Mads Gabrielsen, Syed F Ahmed, Karolina A Majorek, Gary J Sibbet, Brian O Smith, Danny T Huang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Life science alliance, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

8 authors.

Mark A NakasoneCancer Research UK Scotland Institute, Glasgow, UK mark.nakasone@glasgow.ac.uk.ORCID 0000-0002-1362-191X
Lori BuetowCancer Research UK Scotland Institute, Glasgow, UK.ORCID 0000-0003-4951-8057
Mads GabrielsenCancer Research UK Scotland Institute, Glasgow, UK.
Syed F AhmedCancer Research UK Scotland Institute, Glasgow, UK.ORCID 0000-0003-1033-2538
Karolina A MajorekCancer Research UK Scotland Institute, Glasgow, UK.
Gary J SibbetCancer Research UK Scotland Institute, Glasgow, UK.
Brian O SmithSchool of Molecular Biosciences, University of Glasgow, Glasgow, UK.ORCID 0000-0003-3363-4168
Danny T HuangCancer Research UK Scotland Institute, Glasgow, UK d.huang@crukscotlandinstitute.ac.uk.ORCID 0000-0002-6192-259X

Funding

Cancer Research UK - CRUK Scotland Institute A17196Cancer Research UK - CRUK Scotland Institute A31287
6 · The paper itself

Abstract

RING family ubiquitin ligases (E3s) employ the RING domain to recruit the E2 thioester ubiquitin (E2∼Ub) intermediate to catalyze the transfer of ubiquitin (Ub) to substrates. A cationic Arg linchpin (LP) residue in the RING domain plays a key role in stabilizing the interface with E2∼Ub, but the identity of the LP residue varies across E3s. Here, we investigate how the LP residue contributes to ubiquitination. Using the model RNF38 system, we demonstrate that substitution of LP

Indexed as

UbiquitinUbiquitin-Protein LigasesCrystallography, X-RayHumansModels, MolecularProtein BindingProtein ConformationUbiquitinationUbiquitin-Conjugating EnzymesX-Linked Inhibitor of Apoptosis ProteinUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesXIAP protein, humanX-Linked Inhibitor of Apoptosis Protein

Identifiers

PMID40763985
PMCPMC12326332

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.