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Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
Cardif is described, a new CARD-containing adaptor protein that interacts with RIG-I and recruits IKKα, IKKβ and IKKɛ kinases by means of its C-terminal region, leading to the activation of NF-κB and IRF3.
TRADD protein is an essential component of the RIG-like helicase antiviral pathway.
An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication
This domain is required to form a stable complex with unassembled NP (P-NP0) and to prevent NP from assembling illegitimately, i.e., independently of the concurrent assembly of a nascent viral genome.
Paramyxovirus RNA Synthesis and the Requirement for Hexamer Genome Length: the Rule of Six Revisited
- D. Kolakofsky, T. Pelet, D. Garcin, S. Hausmann, J. Curran, L. Roux
- Biology, ChemistryJournal of Virology
- 1 February 1998
The template for paramyxovirus RNA synthesis is not naked RNA but the helical nucleocapsid core of the virus, in which each nucleocapsid protein (N protein) is predicted to be associated with…
A highly recombinogenic system for the recovery of infectious Sendai paramyxovirus from cDNA: generation of a novel copy‐back nondefective interfering virus.
- D. Garcin, T. Pelet, P. Calain, L. Roux, J. Curran, D. Kolakofsky
- BiologyThe EMBO journal
- 1 December 1995
A novel copy‐back nondefective virus was generated which interferes with wild‐type virus replication when a fifth plasmid containing a new genomic 3′ end without the presumably deleterious BglII site was included as another target for recombination.
Tetrameric coiled coil domain of Sendai virus phosphoprotein
- N. Tarbouriech, J. Curran, R. Ruigrok, W. Burmeister
- Chemistry, PhysicsNature Structural Biology
- 1 September 2000
The high resolution X-ray structure of the Sendai virus oligomerization domain reveals a homotetrameric coiled coil structure with many details that are different from classic coiled coils with…
The hypervariable C-terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidation
- J. Curran, H. Homann, C. Buchholz, S. Rochat, W. Neubert, D. Kolakofsky
- BiologyJournal of virology
- 1 July 1993
The results are interpreted as indicating that the tail is not required for RNA assembly but is required for the template to function in RNA synthesis, and the protein nonfunctional in either system.
Paramyxovirus phosphoproteins form homotrimers as determined by an epitope dilution assay, via predicted coiled coils.
The predicted coiled-coil region of the measles virus P protein, when grafted onto the C-terminus of the normally monomeric La protein, led to the efficient oligomerization of this reporter protein.
An acidic activation-like domain of the Sendai virus P protein is required for RNA synthesis and encapsidation.
Deletion analysis of the P gene found that residues 1-77 in the N-terminal half were in fact essential for RNA encapsidation, and either residues 1 -77 or 78-144 also provided a function that was essential forRNA synthesis per se.
Complexes of Sendai virus NP-P and P-L proteins are required for defective interfering particle genome replication in vitro
The replication data suggest that two protein complexes, NP-P and P-L, are required for nucleocapsid RNA replication and that these complexes must form during or soon after synthesis of the proteins.