HPV16 E2 protein possesses intrinsic helicase activity and sterically hinders E1 function through direct interaction.

Ping Xu, Shuning Cai, Lihong Zhang, Yueqi Wu, Ke Xu, Yigang Tong, Shan Xu

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Ping XuBAICSM, State Key Laboratory of Green Biomanufacturing, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, China.

Shuning CaiBAICSM, State Key Laboratory of Green Biomanufacturing, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, China.

Lihong ZhangBAICSM, State Key Laboratory of Green Biomanufacturing, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, China.

Yueqi WuBAICSM, State Key Laboratory of Green Biomanufacturing, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, China.

Ke XuDepartment of Pharmacy, The Second Qilu Hospital of Shandong University, Jinan, China. Electronic address: 937303075@qq.com.

Yigang TongBAICSM, State Key Laboratory of Green Biomanufacturing, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, China. Electronic address: tongyigang@mail.buct.edu.cn.

Shan XuBAICSM, State Key Laboratory of Green Biomanufacturing, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, China. Electronic address: shanxu@buct.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HPV16 E2 protein is a key regulatory protein essential for viral replication, yet no enzymatic activity has been attributed to it until now. In this study, we report for the first time that E2 possesses intrinsic ATP-dependent DNA unwinding activity. Mutational analysis identified residues K299, Y303, and K306 as critical for this helicase function. We further demonstrate that podophyllotoxin directly binds to E2 and inhibits its unwinding activity with an IC

Indexed as

DNA-Binding ProteinsDNA HelicasesHuman papillomavirus 16Oncogene Proteins, ViralHumansProtein BindingDNA-Binding ProteinsDNA HelicasesE1 protein, Human papillomavirus 16E2 protein, Human papillomavirus type 16Oncogene Proteins, ViralATPE1E2helicaseHPV16

Identifiers

PMID42155768

DOI10.1016/j.jbc.2026.113143

PMCPMC13284460

What Socratic holds

Textmetadata

LicenceCC BY

Read underepoch 390

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 Socratic graph.