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The FDA-approved drug ivermectin inhibits the replication of SARS-CoV-2 in vitro
TLDR
Ivermectin, an FDA-approved anti-parasitic previously shown to have broad-spectrum anti-viral activity in vitro, is an inhibitor of the causative virus (SARS-CoV-2), with a single addition to Vero-hSLAM cells 2 h post infection able to effect ~5000-fold reduction in viral RNA at 48 h. Expand
The Type III Effectors NleE and NleB from Enteropathogenic E. coli and OspZ from Shigella Block Nuclear Translocation of NF-κB p65
TLDR
Overall the data show that EPEC and Shigella have evolved similar T3SS-dependent means to manipulate host inflammatory pathways by interfering with the activation of selected host transcriptional regulators. Expand
Ivermectin is a specific inhibitor of importin α/β-mediated nuclear import able to inhibit replication of HIV-1 and dengue virus
TLDR
It is established for the first time that ivermectin has potent antiviral activity towards both HIV-1 and dengue virus, both of which are strongly reliant on importin α/β nuclear import, with respect to the HIV- 1 integrase and NS5 (non-structural protein 5) polymerase proteins respectively. Expand
Targeted delivery to the nucleus.
TLDR
The mechanisms which regulate nuclear import of endogenous molecules are described and how viruses exploit these mechanisms during their life cycle are indicated. Expand
Importins and Beyond: Non‐Conventional Nuclear Transport Mechanisms
TLDR
This review examines several of these novel pathways, including facilitation of Imp‐dependent transport by microtubule motors, and Imp‐independent pathways involving either other transport molecules such as the calcium‐binding protein calmodulin or through direct binding to the components of the NPC. Expand
An AlphaScreen®-Based Assay for High-Throughput Screening for Specific Inhibitors of Nuclear Import
TLDR
A novel high-throughput screening assay for identifying inhibitors of nuclear import, particularly IN, based on amplified luminescent proximity homogeneous assay (AlphaScreen®) technology is described, which is high throughput, requires low amounts of material, and is efficient and cost-effective. Expand
Nuclear import and export inhibitors alter capsid protein distribution in mammalian cells and reduce Venezuelan Equine Encephalitis Virus replication.
TLDR
It is confirmed that VEEV uses host importins and exportins during part of its life cycle and suggests that temporarily targeting host proteins that are hijacked for use by viruses is a viable antiviral therapy. Expand
The N-terminal basic domain of the HIV-1 matrix protein does not contain a conventional nuclear localization sequence but is required for DNA binding and protein self-association.
TLDR
It is determined that, despite the ability of MA to interact with importins, the full-length protein fails to enter the nucleus of cells and the N-terminal basic domain of MA appears to be a crucial structural and functional motif whose integrity is required for a number of other roles performed by MA during viral infection. Expand
Nucleocytoplasmic transport of DNA: enhancing non-viral gene transfer.
TLDR
This review focuses on the nucleocytoplasmic delivery of DNA and mechanisms to enhance to non-viral-mediated gene transfer. Expand
Intramolecular masking of nuclear localization signals: analysis of importin binding using a novel AlphaScreen-based method.
TLDR
A modified AlphaScreen-based assay able to estimate the solution binding affinities of such interactions using biotinylated IMPs and His6-tagged NLS-containing proteins is developed and used to examine IMP binding to the cancer cell-specific proapoptotic factor viral protein 3 (VP3) from the chicken anemia virus. Expand
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