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Structure of E6AP in complex with HPV16-E6 and p53 reveals a novel ordered domain important for E3 ligase activation

Structure(2025)10.1016/j.str.2024.12.013Source: DataRank Database

Structure of E6AP in complex with HPV16-E6 and p53 reveals a novel ordered domain important for E3 ligase activation is a research paper published in Structure (2025). On theSindex it has a DataRank of 0. It has been cited 6 times.

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Open Access6 citations

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Enrichment:Funding (11 grants)Impact (FWCI 2.45)OA: greenTopics (39)IDs (PubMed, PMC, OpenAlex)Annotations (4)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (10)

Shalini Iyer,C. Gabel ORCID,Natalia M. Tegenfeldt,Andrew G. DeMarco ORCID,Mark C. Hall ORCID

Live enrichment

PubMed:39818213 PMC:PMC12207913 OpenAlex:https://openalex.org/W4406385231

National Institute of General Medical Sciences

Grant: T32 GM132024

National Institute of General Medical Sciences

Grant: R01GM126296

National Institutes of Health

Grant: U24GM129541

National Institute of Allergy and Infectious Diseases Division of Intramural Research

Grant: R01AI158426

Purdue University Center for Cancer Research

Grant: P30CA023168

American Heart Association Inc

Grant: 905924/SK/2021

NIMH NIH HHS

Grant: R01 MH071533

NIMH NIH HHS

Grant: T32 MH016804

SLAC National Accelerator Laboratory

Stanford University

National Institute of Allergy and Infectious Diseases

FWCI

2.45

Citation Percentile

0.9%

Citation Trend

2025

2026

greenLicense: http://www.elsevier.com/open-access/userlicense/1.0/

repositoryhttps://pmc.ncbi.nlm.nih.gov/articles/PMC12207913/pdf/nihms-2043800.pdf

publisherhttps://api.elsevier.com/content/article/PII:S0969212624005483?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S0969212624005483?httpAccept=text/plain

repositoryhttps://pmc.ncbi.nlm.nih.gov/articles/PMC12207913/

Fields of Study

Ubiquitin and proteasome pathwaysProtein Degradation and InhibitorsCancer-related Molecular PathwaysMedicineBiology

MeSH Terms

Protein DomainsBinding SitesHumansModels, MolecularOncogene Proteins, ViralProtein BindingRepressor ProteinsTumor Suppressor Protein p53Cryoelectron MicroscopyUbiquitin-Protein LigasesHuman papillomavirus 16Ubiquitination

Keywords

Ubiquitin ligaseDNA ligaseUbiquitin-Protein LigasesUbiquitinDomain (mathematical analysis)Cell biologyChemistryComputational biologyBiologyBiochemistryGeneticsDNAGeneMathematicsHPVE6apE3 LigaseCryo-emViral FactorTargeted DegradationYeast HybridLigase Activation

Structure of E6AP in complex with HPV16-E6 and p53 reveals a novel ordered domain important for E3 ligase activation

FAIR Checklist

Authors (10)

Funding (11 grants)

Impact

Open Access

Topics

Annotations (Europe PMC)