Evidence map›Paper›PMID 27551040›Full record

ArticleThe Journal of biological chemistry2016

Hepatitis C Virus Nonstructural 5A Protein Interacts with Abelson Interactor 1 and Modulates Epidermal Growth Factor-mediated MEK/ERK Signaling Pathway.

Van T T Huynh, Yun-Sook Lim, Si C Tran, Tu M Pham, Lam N Nguyen, Soon B Hwang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Adaptor protein Abelson interactor 1 in homeostasis and disease.Cell communication and signaling : CCS · 2024
    Review
  2. Article
  3. Article
  4. Article
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  9. [Effect of hepatitis C virus nonstructural protein 5A and its domains II on hepatocyte gluconeogenesis in mice].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2017
    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

6 authors at 1 institution in 1 country.

Van T T HuynhFrom the National Research Laboratory of Hepatitis C Virus and Ilsong Institute of Life Science, Hallym University, Anyang 14066, Korea.
Yun-Sook LimFrom the National Research Laboratory of Hepatitis C Virus and Ilsong Institute of Life Science, Hallym University, Anyang 14066, Korea.
Si C TranFrom the National Research Laboratory of Hepatitis C Virus and Ilsong Institute of Life Science, Hallym University, Anyang 14066, Korea.
Tu M PhamFrom the National Research Laboratory of Hepatitis C Virus and Ilsong Institute of Life Science, Hallym University, Anyang 14066, Korea.
Lam N NguyenFrom the National Research Laboratory of Hepatitis C Virus and Ilsong Institute of Life Science, Hallym University, Anyang 14066, Korea.
Soon B HwangFrom the National Research Laboratory of Hepatitis C Virus and Ilsong Institute of Life Science, Hallym University, Anyang 14066, Korea sbhwang@hallym.ac.kr.
Hallym University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The propagation of hepatitis C virus (HCV) is highly dependent on host cellular factors. To identify the cellular factors involved in HCV propagation, we have previously performed protein microarray assays using the HCV nonstructural 5A (NS5A) protein as a probe. Of ∼9,000 host proteins immobilized in a microarray, ∼90 cellular proteins were identified as HCV NS5A interacting partners. Of these candidates, we selected Abelson interactor 1 (Abi1) for further characterization. Binding of HCV NS5A to Abi1 was verified by both in vitro pulldown and coimmunoprecipitation assays. HCV NS5A interacted with Abi1 through regions I + II of Abi1 and domain I of NS5A. We further demonstrated that Abi1 colocalized with the HCV NS5A protein in the cytoplasm. We showed that NS5A inhibited epidermal growth factor-mediated ERK and Egr1 activations and this inhibitory activity of NS5A was nullified in Abi1-knockdown cells. Moreover, silencing of Abi1 expression impaired HCV replication, whereas overexpression of Abi1 promoted HCV propagation. Collectively, these data indicate that HCV exploits host Abi1 protein via NS5A to modulate MEK/ERK signaling pathway for its own propagation.

Indexed as

MAP Kinase Signaling SystemAdaptor Proteins, Signal TransducingCell LineCytoskeletal ProteinsEarly Growth Response Protein 1Epidermal Growth FactorGene SilencingHepacivirusHumansProtein BindingRNA-Dependent RNA PolymeraseViral Nonstructural ProteinsVirus ReplicationABI1 protein, humanAdaptor Proteins, Signal TransducingCytoskeletal ProteinsEarly Growth Response Protein 1EGR1 protein, humanEpidermal Growth FactorNS-5 protein, hepatitis C virusRNA-Dependent RNA PolymeraseViral Nonstructural Proteinsearly growth response protein 1 (EGR1)epidermal growth factor (EGF)extracellular-signal-regulated kinase (ERK)growth factor receptor-bound protein 2 (GRB2)hepatitis C virus (HCV)signal transduction

Identifiers

PMID27551040
PMCPMC5077197
OpenAlexW2516081867

What OpenQuestion holds

Textmetadata
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.