Evidence map›Paper›PMID 40408472›Full record

ArticleScience advances2025

Mechanism of D-type cyclin recognition by the AMBRA1 E3 ligase receptor.

Yang Wang, Ming Liu, Shan Wang, Xinyi Mai, Xi Wang, Fei Teng, Tianrui Lyu, Ming-Yuan Su, Goran Stjepanovic

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2025. 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.

Yang WangKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Guangdong 518172, China.ORCID 0000-0002-3839-0003
Ming LiuKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Guangdong 518172, China.ORCID 0000-0002-6102-698X
Shan WangDepartment of Biochemistry, School of Medicine, Southern University of Science and Technology, Shenzhen, Guangdong 518055, China.ORCID 0009-0001-5301-4540
Xinyi MaiKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Guangdong 518172, China.ORCID 0009-0004-7828-061X
Xi WangKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Guangdong 518172, China.ORCID 0000-0002-2526-2782
Fei TengKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Guangdong 518172, China.ORCID 0000-0001-6782-7676
Tianrui LyuKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Guangdong 518172, China.
Ming-Yuan SuDepartment of Biochemistry, School of Medicine, Southern University of Science and Technology, Shenzhen, Guangdong 518055, China.ORCID 0000-0003-1581-0914
Goran StjepanovicKobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Guangdong 518172, China.ORCID 0000-0002-4841-9949

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMBRA1 is a tumor suppressor protein that functions as a substrate receptor in the ubiquitin conjugation system and regulates the stability of D-type cyclins and cell proliferation. Here, we present the cryo-EM structure of cyclin D1-bound AMBRA1-DDB1 complex at 3.55-Å resolution. The structure reveals a substrate interaction surface on the AMBRA1 WD40 domain that specifically binds to the C-terminal region of D-type cyclins. This interaction is dependent on the phosphorylation of Thr

Indexed as

Adaptor Proteins, Signal TransducingCyclin D1DNA-Binding ProteinsUbiquitin-Protein LigasesBinding SitesCryoelectron MicroscopyDNA DamageHumansModels, MolecularPhosphorylationProtein BindingProtein ConformationAdaptor Proteins, Signal TransducingAMBRA1 protein, humanCyclin D1DDB1 protein, humanDNA-Binding ProteinsUbiquitin-Protein Ligases

Identifiers

PMID40408472
PMCPMC12101500

What OpenQuestion holds

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Registered trials

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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.