Stimulation of the Internal Ribosome Entry Site (IRES)-Dependent Translation of Enterovirus 71 by DDX3X RNA Helicase and Viral 2A and 3C Proteases

The Initiation Factors eIF2, eIF2A, eIF2D, eIF4A, and eIF4G Are Not Involved in Translation Driven by Hepatitis C Virus IRES in Human Cells

(2018) Esther González-Almela et al.   Frontiers in Microbiology

Idarubicin is a broad-spectrum enterovirus replication inhibitor that selectively targets the virus internal ribosomal entry site

(2016) Hsin-Yu Hou et al.   JOURNAL OF GENERAL VIROLOGY

Additive Promotion of Viral Internal Ribosome Entry Site-Mediated Translation by Far Upstream Element-Binding Protein 1 and an Enterovirus 71-Induced Cleavage Product

(2016) Chuan-Tien Hung et al.   PLoS Pathogens

Nuclear Protein Sam68 Interacts with the Enterovirus 71 Internal Ribosome Entry Site and Positively Regulates Viral Protein Translation

(2015) Hua Zhang et al.   JOURNAL OF VIROLOGY

Nuclear proteins hijacked by mammalian cytoplasmic plus strand RNA viruses

(2015) Richard E. Lloyd   VIROLOGY

HuR and Ago2 Bind the Internal Ribosome Entry Site of Enterovirus 71 and Promote Virus Translation and Replication

(2015) Jing-Yi Lin et al.   PLoS One

The mechanism of translation initiation on Type 1 picornavirus IRESs

(2013) Trevor R Sweeney et al.   EMBO JOURNAL

DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs

(2012) Ricardo Soto-Rifo et al.   EMBO JOURNAL

Identification of RNA-Protein Interaction Networks Involved in the Norovirus Life Cycle

(2012) S. Vashist et al.   JOURNAL OF VIROLOGY

Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiation

(2012) Dmitri E. Andreev et al.   NUCLEIC ACIDS RESEARCH

The DEAD-box helicase DDX3 supports the assembly of functional 80S ribosomes

(2012) Rene Geissler et al.   NUCLEIC ACIDS RESEARCH

Poliovirus Switches to an eIF2-Independent Mode of Translation during Infection

(2011) J. P. White et al.   JOURNAL OF VIROLOGY

Differential Processing of Nuclear Pore Complex Proteins by Rhinovirus 2A Proteases from Different Species and Serotypes

(2011) K. Watters et al.   JOURNAL OF VIROLOGY

Viral subversion of the host protein synthesis machinery

(2011) Derek Walsh et al.   NATURE REVIEWS MICROBIOLOGY

mRNA helicases: the tacticians of translational control

(2011) Armen Parsyan et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Far upstream element binding protein 1 binds the internal ribosomal entry site of enterovirus 71 and enhances viral translation and viral growth

(2011) P.-N. Huang et al.   NUCLEIC ACIDS RESEARCH

Specific Cleavage of the Nuclear Pore Complex Protein Nup62 by a Viral Protease

(2010) Nogi Park et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

DDX3 Regulates Cell Growth through Translational Control of Cyclin E1

(2010) M.-C. Lai et al.   MOLECULAR AND CELLULAR BIOLOGY

Human DEAD-box protein 3 has multiple functions in gene regulation and cell cycle control and is a prime target for viral manipulation

(2009) Martina Schröder   BIOCHEMICAL PHARMACOLOGY

Uncoupling Stress Granule Assembly and Translation Initiation Inhibition

(2009) Sophie Mokas et al.   MOLECULAR BIOLOGY OF THE CELL

Human P-selectin glycoprotein ligand-1 is a functional receptor for enterovirus 71

(2009) Yorihiro Nishimura et al.   NATURE MEDICINE

Direct functional interaction of initiation factor eIF4G with type 1 internal ribosomal entry sites

(2009) S. de Breyne et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Cleavage of Poly(A)-Binding Protein by Poliovirus 3C Proteinase Inhibits Viral Internal Ribosome Entry Site-Mediated Translation

(2008) J. M. Bonderoff et al.   JOURNAL OF VIROLOGY

The DEAD-Box RNA Helicase DDX3 Associates with Export Messenger Ribonucleoproteins as well asTip-associated Protein and Participates in Translational Control

(2008) Ming-Chih Lai et al.   MOLECULAR BIOLOGY OF THE CELL

Human DDX3 functions in translation and interacts with the translation initiation factor eIF3

(2008) C.-S. Lee et al.   NUCLEIC ACIDS RESEARCH