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The FDA-approved drug ivermectin inhibits the replication of SARS-CoV-2 in vitro
Nuclear targeting signal recognition: a key control point in nuclear transport?
This work has shown that the targeting sequence‐importin interaction can be influenced directly by phosphorylation increasing the affinity of the interaction with importins or by targeting sequence masking throughosphorylation or specific protein binding.
Ivermectin is a specific inhibitor of importin α/β-mediated nuclear import able to inhibit replication of HIV-1 and dengue virus
- K. Wagstaff, Haran Sivakumaran, Steven M Heaton, D. Harrich, D. Jans
- Biology, ChemistryThe Biochemical journal
- 14 March 2012
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.
An efficient system for high‐level expression and easy purification of authentic recombinant proteins
- Ann-Maree Catanzariti, T. Soboleva, D. Jans, P. Board, R. Baker
- BiologyProtein science : a publication of the Protein…
- 1 May 2004
The development of an efficient expression system, utilizing the ubiquitin fusion technique, which allows convenient high yield and easy purification of authentic protein and should be amenable to high‐throughput applications.
Regulation of Nuclear Transport: Central Role in Development and Transformation?
Altering of the level of the expression of components of the nuclear transport machinery also appears to be a key determinant of transport efficiency, having central importance in development, differentiation and transformation.
The Type III Effectors NleE and NleB from Enteropathogenic E. coli and OspZ from Shigella Block Nuclear Translocation of NF-κB p65
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.
Nuclear Import of Insulin-like Growth Factor-binding Protein-3 and -5 Is Mediated by the Importin β Subunit*
- L. Schedlich, Sophie Le Page, S. Firth, L. Briggs, D. Jans, R. Baxter
- BiologyThe Journal of Biological Chemistry
- 4 August 2000
The results suggest that the NLSs within the C-terminal domain of IGF BP-3 and IGFBP-5 are required for importin-β-dependent nuclear uptake and probably also accumulation through mediating binding to nuclear components.
The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T‐antigen.
We have previously demonstrated [Rihs, H.‐P. and Peters, R. (1989) EMBO J., 8, 1479–1484] that the nuclear transport of recombinant proteins in which short fragments of the SV40 T‐antigen are fused…
Regulation of protein transport to the nucleus: central role of phosphorylation.
Results indicate that NLS-dependent nuclear protein import is precisely regulated, and the CcN motif appears to be a special form of phosphorylation-regulated NLS (prNLS), where phosphorylated at site(s) close to the NLS specifically regulates NLS function.
Towards safe, non-viral therapeutic gene expression in humans
Recent advances indicate that efficient, long-term gene expression can be achieved by non-viral means and integration of DNA can be targeted to specific genomic sites without deleterious consequences.