VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway.

By Paula A. Faria, Papia Chakraborty, A. Levay, G. Barber, H. Ezelle, J. Enninga, C. Arana, J. V. van Deursen, B. Fontoura. 2005

254 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. G. Barber
2. A. García‐Sastre
3. F. Weber
4. M. Gale
5. Simon B. Rasmussen
6. S. Paludan
7. R. Hartmann
8. V. Wagner

In Molecular Biology

1. G. Barber
2. Ren Sun
3. F. Weber
4. T. Rana
5. M. Gale
6. Nevan J. Krogan
7. S. Paludan
8. Günter Blobel

Citations in the corpus

• SARS-CoV-2 ORF6 Disrupts Bidirectional Nucleocytoplasmic Transport through Interactions with Rae1 and Nup98 (2021, background): “VSV M and KSHV ORF10, which both interact with Rae1 and Nup98, produce an accumulation of mRNA in the nuclei of transfected cells (7, 9).”
• Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1 (2010, background): “Interferon γ treatment of VSV infected cells was found to reverse the RNA export inhibition by up-regulation of Nup98 and Rae1 expression (15, 16), thereby underlining the importance of the interaction between Rae1 and Nup98 for RNA export.”
• SARS-CoV-2 ORF6 disrupts nucleocytoplasmic transport through interactions with Rae1 and Nup98 (2020, background): “interactions with the nuclear mRNA export factor Rae1 and nuclear pore complex 156 component Nup98 (6, 8).”
• Complexes of Vesicular Stomatitis Virus Matrix Protein with Host Rae1 and Nup98 Involved in Inhibition of Host Transcription (2012, methodology): “Mutant M protein, M(D), which has three amino acid substitutions (D52A, T53A, and Y54A), has been shown to be defective in interacting with Rae1 and Nup98 [14].”
• Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1•Nup98) (2014, methodology): “X-ray intensities were processed using the HKL2000 denzo/scalepack package (2), and subsequent calculations were carried out using the CCP4 program package (3).”
• A herpesvirus protein selectively inhibits cellular mRNA nuclear export (2016, background): “Through binding to Rae1, VSV M protein blocks mRNA export during interphase (Faria et al., 2005; von Kobbe et al., 2000), and interferes with mitotic progression during mitosis (Chakraborty et al.”
• SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling (2020, background): “Furthermore, VSV M inhibits cellular mRNA export by forming a complex with Rae1 and Nup98 (41, 57).”
• STING an Endoplasmic Reticulum Adaptor that Facilitates Innate Immune Signaling (2008, methodology): “VSV-ΔM was constructed as described in Faria et al[17].”
• Double-Stranded RNA Is Produced by Positive-Strand RNA Viruses and DNA Viruses but Not in Detectable Amounts by Negative-Strand RNA Viruses (2006, background): “This view is not contradicted by previous reports about biologically active dsRNA derived from FLUAV-infected cells (41), since those studies involved the extraction of RNA from infected tissue and the removal of all proteins, thus allowing hybridization of RNAs which may have been well separated fr”
• Molecular mechanism underlying selective inhibition of mRNA nuclear export by herpesvirus protein ORF10 (2020, background): “Moreover, ORF10 selectively inhibits the export of a subset of cellular mRNAs (25), while the M protein nonspecifically prevents export of bulk mRNAs (15, 24).”