Evidence map›Paper›PMID 31489375›Full record

ArticleScience advances2019

Viperin catalyzes methionine oxidation to promote protein expression and function of helicases.

Lei Bai, Jiazhen Dong, Zhenqiu Liu, Youliang Rao, Pinghui Feng, Ke Lan

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
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

19 citing papers in PubMed, 54 citations in OpenAlex.

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  17. Viperin Reveals Its True Function.Annual review of virology · 2020
    Review
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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

6 authors at 4 institutions in 2 countries.

Lei BaiState Key Laboratory of Virology, College of Life Sciences, Medical Research Institute, Wuhan University, Wuhan 430072, P.R. China.ORCID 0000-0001-8968-3386
Jiazhen DongInstitut Pasteur of Shanghai, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai 200031, P.R. China.ORCID 0000-0001-6040-4363
Zhenqiu LiuState Key Laboratory of Genetic Engineering and Collaborative Innovation Center for Genetics and Development, School of Life Sciences, Fudan University, Shanghai 200438, P.R. China.ORCID 0000-0002-5244-6894
Youliang RaoSection of Infection and Immunity, Herman Ostrow School of Dentistry and Norris Comprehensive Cancer Center, University of Southern California, 925 W 34th Street, Los Angeles, CA 90089, USA.ORCID 0000-0002-8416-8104
Pinghui FengSection of Infection and Immunity, Herman Ostrow School of Dentistry and Norris Comprehensive Cancer Center, University of Southern California, 925 W 34th Street, Los Angeles, CA 90089, USA.ORCID 0000-0002-8494-0205
Ke LanState Key Laboratory of Virology, College of Life Sciences, Medical Research Institute, Wuhan University, Wuhan 430072, P.R. China.ORCID 0000-0002-0384-8598
University of Southern California · USWuhan University · CNFudan University · CNInstitut Pasteur of Shanghai · CN

Funding

Exploring roles of protein deamidation in oral inflammationR35DE027556 · NIDCR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, CASEY · 2017 to 2020
$4.1M
NFAT activation in kGPCR tumorigenesisR01CA221521 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FENG, PINGHUI · 2017 to 2021
$1.9M
Versatile functions of LANA in KSHV pathogenesisR01AI116442 · NIAID · WUHAN UNIVERSITY · PI LAN, KE · 2015 to 2019
$517k
NCI NIH HHS R01 CA221521NIAID NIH HHS R01 AI116442NIDCR NIH HHS R35 DE027556
6 · The paper itself

Abstract

Helicases play pivotal roles in fundamental biological processes, and posttranslational modifications regulate the localization, function, and stability of helicases. Here, we report that methionine oxidation of representative helicases, including DNA and RNA helicases of viral (ORF44 of KSHV) and cellular (MCM7 and RIG-I) origin, promotes their expression and functions. Cellular viperin, a major antiviral interferon-stimulated gene whose functions beyond host defense remain largely unknown, catalyzes the methionine oxidation of these helicases. Moreover, biochemical studies entailing loss-of-function mutations of helicases and a pharmacological inhibitor interfering with lipid metabolism and, hence, decreasing viperin activity indicate that methionine oxidation potently increases the stability and enzyme activity of these helicases that are critical for DNA replication and immune activation. Our work uncovers a pivotal role of viperin in catalyzing the methionine oxidation of helicases that are implicated in diverse fundamental biological processes.

Indexed as

Antiviral AgentsDNA ReplicationHEK293 CellsHumansInterferonsLipid MetabolismMethionineOxidation-ReductionOxidoreductases Acting on CH-CH Group DonorsProtein Processing, Post-TranslationalProteinsRNA HelicasesViperin ProteinVirus ReplicationAntiviral AgentsInterferonsMethionineOxidoreductases Acting on CH-CH Group DonorsProteinsRNA HelicasesRSAD2 protein, humanViperin Protein

Identifiers

PMID31489375
PMCPMC6713503
OpenAlexW2970163801

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.