A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon
about
An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication.Rhythmic serotonin N-acetyltransferase mRNA degradation is essential for the maintenance of its circadian oscillation.The yin and yang of hepatitis C: synthesis and decay of hepatitis C virus RNAThe polypyrimidine tract binding protein is required for efficient picornavirus gene expression and propagation.Hepatitis C virus internal ribosome entry site-dependent translation in Saccharomyces cerevisiae is independent of polypyrimidine tract-binding protein, poly(rC)-binding protein 2, and La proteinQuantitative Analysis of the Hepatitis C Virus Replication ComplexThe Hepatitis C Virus RNA 3'-Untranslated Region Strongly Enhances Translation Directed by the Internal Ribosome Entry SiteThe internal initiation of translation in bovine viral diarrhea virus RNA depends on the presence of an RNA pseudoknot upstream of the initiation codonRole of the Hepatitis C Virus Core+1 Open Reading Frame and Core cis-Acting RNA Elements in Viral RNA Translation and ReplicationRNA-Binding Protein hnRNP D Modulates Internal Ribosome Entry Site-Dependent Translation of Hepatitis C Virus RNAAnalysis of natural variants of the hepatitis C virus internal ribosome entry site reveals that primary sequence plays a key role in cap-independent translationIGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTRProanthocyanidin from Blueberry Leaves Suppresses Expression of Subgenomic Hepatitis C Virus RNAA cell-permeable peptide inhibits hepatitis C virus replication by sequestering IRES transacting factorsInsights into the Biology of IRES Elements through Riboproteomic ApproachesNuclear proteins hijacked by mammalian cytoplasmic plus strand RNA virusesRhythmic control of AANAT translation by hnRNP Q in circadian melatonin productionWHEP domains direct noncanonical function of glutamyl-Prolyl tRNA synthetase in translational control of gene expressionInhibition of hepatitis C virus replication by single-stranded RNA structural mimics.The duck hepatitis virus 5'-UTR possesses HCV-like IRES activity that is independent of eIF4F complex and modulated by downstream coding sequences.eIF2A mediates translation of hepatitis C viral mRNA under stress conditions.Hepatitis C virus translation preferentially depends on active RNA replication.Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.Anti-inflammatory lipid mediator 15d-PGJ2 inhibits translation through inactivation of eIF4A.Control of translation and miRNA-dependent repression by a novel poly(A) binding protein, hnRNP-Q.Drosophila Hephaestus/polypyrimidine tract binding protein is required for dorso-ventral patterning and regulation of signalling between the germline and soma.SYNCRIP (synaptotagmin-binding, cytoplasmic RNA-interacting protein) is a host factor involved in hepatitis C virus RNA replicationPoly(A) RNA-binding proteins and polyadenosine RNA: new members and novel functions.Poly(C)-binding protein 2 interacts with sequences required for viral replication in the hepatitis C virus (HCV) 5' untranslated region and directs HCV RNA replication through circularizing the viral genome.Translation-competent 48S complex formation on HCV IRES requires the RNA-binding protein NSAP1.A feedback loop between Wolbachia and the Drosophila gurken mRNP complex influences Wolbachia titer.Subcellular relocalization of a trans-acting factor regulates XIAP IRES-dependent translation.Spinal muscular atrophy and a model for survival of motor neuron protein function in axonal ribonucleoprotein complexesInhibition of hepatitis C virus in chimeric mice by short synthetic hairpin RNAs: sequence analysis of surviving virus shows added selective pressure of combination therapy.Hepatitis C viral protein translation: mechanisms and implications in developing antivirals.Establishment of chronic hepatitis C virus infection: translational evasion of oxidative defenceAn mRNA-specific tRNAi carrier eIF2A plays a pivotal role in cell proliferation under stress conditions: stress-resistant translation of c-Src mRNA is mediated by eIF2A.HuR Displaces Polypyrimidine Tract Binding Protein To Facilitate La Binding to the 3' Untranslated Region and Enhances Hepatitis C Virus Replication.Identification of the IFITM3 gene as an inhibitor of hepatitis C viral translation in a stable STAT1 cell line.hnRNP A1 regulates UV-induced NF-kappaB signalling through destabilization of cIAP1 mRNA.
P2860
Q24293290-BF54C0F8-7EDF-441F-A29A-EAE61C400D92Q24520629-F03EA15E-0B55-48AE-B741-CEDF9723B2DBQ26800446-D0664D4D-106F-4228-99DF-E313F827D990Q27469504-A8D54EF1-F5BC-406C-AD26-5D814D970A80Q27470417-940BFE70-8D01-41D2-8FB3-4E236500A114Q27472670-955EB7AD-A08F-4E45-B312-E5EBF3DAEE52Q27477654-48E35382-457E-42AA-8454-F28A9BB33DA7Q27485201-28FA558C-3062-4C22-9AED-58D5CA6C5459Q27487337-21BFA421-4454-40B7-9732-C26CCC225CF6Q27487410-2E7D4875-1C4E-4743-8F93-A935101D2CC7Q27487957-3A735EC6-69AE-4DEB-8A45-F871FAA364FBQ27488967-6AC5F49C-9052-433F-8A36-46492C913A40Q27489836-278A9B72-7A66-4C95-9C43-E5F5965D05C2Q27490232-043E7B87-25D3-47F0-B8D8-A03389006C28Q27490895-F849D963-F50C-432B-9A2B-7B33DBF6CE0EQ28083735-9D9FE29F-09E7-4C1D-97D6-EBD18E2C697CQ28572763-67E18550-9591-4A2B-BA52-8467DD432C83Q33642469-8CCEBB77-7FAA-44CB-A41C-99BDC048B530Q33830704-0EBE692B-F627-47FD-BEE6-EE6597DC2FCAQ34174362-B7999DA5-D49F-4275-8C5B-6F380B367208Q34183856-DA900446-9E81-4633-88E3-DECDD21B0D69Q34399244-5646D821-1CB9-4451-9562-BBCB0AE291B2Q34416559-8CE0BC6F-CA45-458D-A446-E7925FC329D0Q34717638-413AC856-501C-4FB3-B316-19EA9ED1BD8BQ34734843-DD880903-DA28-40E7-B7C3-8CEAF14D47DBQ34874964-6308404F-0057-470B-B92A-B4CBB7DF658BQ34996437-01A5B661-E0B7-49B1-A3E7-1A05FABC11E7Q35095113-493F0626-C898-4D4F-B41D-AB806CA37DBDQ35140492-3862B1E6-6617-49CF-8B26-E9EFFC2F9F38Q35224421-2C2AFFD4-08B9-4DF2-87EE-DE6C45400199Q35672139-1041DEE6-6B3D-42C4-8C17-23A556D0923BQ35723781-9ACDC90E-4481-4312-885C-1224BA653F1DQ37033848-C548A45E-2552-4D63-9A53-9095A0BF86F9Q37714008-25AF9CAE-511E-4140-A97B-35826E93AC72Q37899939-D9F87A03-1426-4E70-AB16-FA6E0313C2C6Q38198617-3A23DCCA-824F-4B6F-B147-E347983FBF8CQ38728366-B8439735-8BA5-423C-9091-503E2E50598FQ38838070-A8A51BEC-EDED-4EBB-BAAA-3F3F39D5EDC0Q39474516-A698D7C0-85BD-45C7-A5EB-FE1220391FC6Q39930616-BA240B93-35BC-4BD5-851E-636D60E17D26
P2860
A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon
description
2004 nî lūn-bûn
@nan
2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
name
A cellular RNA-binding protein ...... s polyprotein initiation codon
@ast
A cellular RNA-binding protein ...... s polyprotein initiation codon
@en
A cellular RNA-binding protein ...... s polyprotein initiation codon
@nl
type
label
A cellular RNA-binding protein ...... s polyprotein initiation codon
@ast
A cellular RNA-binding protein ...... s polyprotein initiation codon
@en
A cellular RNA-binding protein ...... s polyprotein initiation codon
@nl
prefLabel
A cellular RNA-binding protein ...... s polyprotein initiation codon
@ast
A cellular RNA-binding protein ...... s polyprotein initiation codon
@en
A cellular RNA-binding protein ...... s polyprotein initiation codon
@nl
P2093
P2860
P1476
A cellular RNA-binding protein ...... s polyprotein initiation codon
@en
P2093
Chon Saeng Kim
Jong Heon Kim
Ki Young Paek
Kobong Choi
Sang Hoon Ha
Sung Key Jang
Sungchan Cho
P2860
P304
P356
10.1128/MCB.24.18.7878-7890.2004
P407
P50
P577
2004-09-01T00:00:00Z