Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98.

mBio - 13 Apr 2021

Addetia Amin, Lieberman Nicole A P, Phung Quynh, Hsiang Tien-Ying, Xie Hong, Roychoudhury Pavitra, Shrestha Lasata, Loprieno Michelle A, Huang Meei-Li, Gale Michael, Jerome Keith R, Greninger Alexander L

Abstract excerpt

RNA viruses that replicate in the cytoplasm often disrupt nucleocytoplasmic transport to preferentially translate their own transcripts and prevent host antiviral responses. The Sarbecovirus accessory protein ORF6 has previously been shown to be a major inhibitor of interferon production in both severe acute respiratory syndrome coronavirus (SARS-CoV) and severe acute respiratory syndrome coronavirus 2...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Active Transport, Cell Nucleus
Share to Cell Nucleus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COVID-19

Share to Nuclear Matrix-Associated Proteins

Share to Nuclear Pore Complex Proteins

Share to Nucleocytoplasmic Transport Proteins

Share to SARS-CoV-2

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 33849972
DOI: 10.1128/mBio.00065-21
PMCID: PMC8092196

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98.PMID 33849972Read ↗

SARS-CoV-2 ORF6 disrupts nucleocytoplasmic transport through interactions with Rae1 and Nup98Semantic proximity Read ↗

Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1–Nup98 Complex to Compete With mRNA Nuclear ExportSemantic proximity Read ↗

Impact of SARS-CoV-2 ORF6 and its variant polymorphisms on host responses and viral pathogenesisSemantic proximity Read ↗

Impact of SARS-CoV-2 ORF6 and its variant polymorphisms on host responses and viral pathogenesisSemantic proximity Read ↗

Decoupling SARS-CoV-2 ORF6 localization and interferon antagonismSemantic proximity Read ↗

SARS-CoV-2 ORF6 disturbs nucleocytoplasmic trafficking to advance the viral replicationSemantic proximity Read ↗

Release of Severe Acute Respiratory Syndrome Coronavirus Nuclear Import Block Enhances Host Transcription in Human Lung CellsSemantic proximity Read ↗

Decoupling SARS-CoV-2 ORF6 localization and interferon antagonismSemantic proximity Read ↗

Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane.Semantic proximity Read ↗

<i>Sarbecovirus</i> ORF6 Proteins Hamper the Induction of Interferon Signaling by Blocking mRNA Nuclear ExportSemantic proximity Read ↗

SARS-CoV-2 infection triggers widespread host mRNA decay leading to an mRNA export blockSemantic proximity Read ↗

Molecular mechanism underlying selective inhibition of mRNA nuclear export by herpesvirus protein ORF10Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.