Is HIV-1 RNA dimerization a prerequisite for packaging? Yes, no, probably? [PDF]
During virus assembly, all retroviruses specifically encapsidate two copies of full-length viral genomic RNA in the form of a non-covalently linked RNA dimer.
Liang, Chen+2 more
core +3 more sources
Viral suppressors: Combatting RNA silencing [PDF]
[EN] Plants defend themselves from invading viruses using RNA silencing. However, plant viruses try to spoil this defensive mechanism by expressing one or more proteins that act as RNA silencing suppressors. One such protein spoils plant defence by transporting the silencing signal into the peroxisomes to avoid its systemic spread.
openaire +4 more sources
Stochastic variation in the FOXM1 transcription program mediates replication stress tolerance
Cellular heterogeneity is a major cause of drug resistance in cancer. Segeren et al. used single‐cell transcriptomics to investigate gene expression events that correlate with sensitivity to the DNA‐damaging drugs gemcitabine and prexasertib. They show that dampened expression of transcription factor FOXM1 and its target genes protected cells against ...
Hendrika A. Segeren+4 more
wiley +1 more source
Class of {varphi}X174 Mutants Relatively Deficient in Synthesis of Viral RNA [PDF]
Nonpermissive cells infected with {varphi}X174 gene D amber mutants synthesized some sixfold less viral RNA than permissive cells. The decrease was unaffected by increasing the multiplicity of infection and was a consequence of an overall decrease in all
Clements, J. Barklie+1 more
core
Levels of feline infectious peritonitis virus in blood, effusions, and various tissues and the role of lymphopenia in disease outcome following experimental infection. [PDF]
Twenty specific pathogen free cats were experimentally infected with a virulent cat-passaged type I field strain of FIPV. Eighteen cats succumbed within 2-4 weeks to effusive abdominal FIP, one survived for 6 weeks, and one seroconverted without outward ...
Eckstrand, Chrissy+4 more
core +2 more sources
It’s the Little Things (in Viral RNA)
Chemical modifications of viral RNA are an integral part of the viral life cycle and are present in most classes of viruses. To date, more than 170 RNA modifications have been discovered in all types of cellular RNA. Only a few, however, have been found in viral RNA, and the function of most of these has yet to be elucidated.
Jiří František Potužník+1 more
openaire +4 more sources
Packaging of viral RNAs in virions of adenoviruses [PDF]
Earlier, we detected viral RNAs packaged in the porcine adenovirus (PAdV) -3 virions. Using Southern blot analysis, we further demonstrated that the viral RNAs were predominantly packaged in CsCl purified mature capsids (containing viral genome) than empty/intermediate capsids. Some of the packaged viral RNAs appear to be polyadenylated.
Li Xing, Suresh K. Tikoo
openaire +4 more sources
CircCCNB1 expression is down‐regulated in nasopharyngeal carcinoma (NPC); thus, less NF90 protein is bound to circCCNB1 and more binds to pri‐miRNAs, blocking their (pri‐miRNAs) binding to DGCR8 and inhibiting the processing and generation of miR‐15b‐5p/miR‐7‐1‐3p. Furthermore, decreased miR‐15b‐5p/miR‐7‐1‐3p promotes the expression of the target genes
Chunmei Fan+6 more
wiley +1 more source
Non-Natural Linker Configuration in 2,6-Dipeptidyl-Anthraquinones Enhances the Inhibition of TAR RNA Binding/Annealing Activities by HIV-1 NC and Tat Proteins [PDF]
The HIV-1 nucleocapsid (NC) protein represents an excellent molecular target for the development of antiretrovirals by virtue of its well-characterized chaperone activities, which play pivotal roles in essential steps of the viral life cycle. Our ongoing
Caliendo, Giuseppe+16 more
core +2 more sources
Translation of a nonpolyadenylated viral RNA is enhanced by binding of viral coat protein or polyadenylation of the RNA [PDF]
On entering a host cell, positive-strand RNA virus genomes have to serve as messenger for the translation of viral proteins. Efficient translation of cellular messengers requires interactions between initiation factors bound to the 5′-cap structure and the poly(A) binding protein bound to the 3′-poly(A) tail.
Neeleman, L.+3 more
openaire +4 more sources