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Regulation of nucleolar signalling to p53 through NEDDylation of L11
TLDR
By controlling the correct localization and stability of L11, NEDD8 acts as a crucial, new regulator of nucleolar signalling to p53, which is required for p53 stabilization during nucleolar stress. Expand
Basic Residues Are Critical to the Activity of Peptide Inhibitors of Human T Cell Leukemia Virus Type 1 Entry*
TLDR
The core inhibitor provides a valuable lead in the search for smaller more bio-available peptides and peptido-mimetics that possess anti-viral activity and may be attractive candidates for therapeutic intervention in human T cell leukemia virus type 1 infections. Expand
Nonhelical Leash and α-Helical Structures Determine the Potency of a Peptide Antagonist of Human T-Cell Leukemia Virus Entry
TLDR
It is suggested that the deep pockets on the coiled coil are ideal targets for small-molecule inhibitors of HTLV-1 entry into cells and that leash-like mimetic peptides may be of value as entry inhibitors for other clinically important viral infections. Expand
Antibodies to the Envelope Glycoprotein of Human T Cell Leukemia Virus Type 1 Robustly Activate Cell-Mediated Cytotoxic Responses and Directly Neutralize Viral Infectivity at Multiple Steps of the
TLDR
This work uses a soluble recombinant surface glycoprotein fused to the Fc region of human IgG as an immunogen to vaccinate mice and demonstrates that recombinant forms of SU possess immunological features that are of significant utility to subunit vaccine design. Expand
An antibody that blocks human T-cell leukemia virus type 1 six-helix-bundle formation in vitro identified by a novel assay for inhibitors of envelope function.
TLDR
A stable, trimeric TM derivative that mimics the coiled-coil structure of fusion-active TM has been used to develop a plate-based assay to identify reagents that interfere with the formation of the six-helix bundle and it is suggested that the pre-hairpin motif is a valid target for antiviral therapy. Expand
Resistance to Neutralization by Antibodies Targeting the Coiled Coil of Fusion-active Envelope Is a Common Feature of Retroviruses*
TLDR
The data imply that the coiled coil of viral envelope is poorly exposed to antibody during membrane fusion, and suggests resistance to neutralization by antibodies directed to fusion-associated structures is a common property of retroviral TM and perhaps of other viral class I fusion proteins. Expand
Conformation-Specific Antibodies Targeting the Trimer-of-Hairpins Motif of the Human T-Cell Leukemia Virus Type 1 Transmembrane Glycoprotein Recognize the Viral Envelope but Fail To Neutralize Viral
TLDR
It is demonstrated that a recombinant trimer-of-hairpins form of the TM ectodomain is strongly immunogenic, suggesting that envelope-derived immunogens capable of eliciting a combination of neutralizing and complement-fixing antibodies would be of value as subunit vaccines for intervention in HTLV infections. Expand
Probing Cell-to-cell Transfer of Human T-cell Leukaemia Virus Type-1 Using Novel Inhibitors of Viral Entry
TLDR
It is demonstrated that upon contact with HTLV-1 infected T-cells, the HT LV-1 receptor glucose transporter, Glut-1, is redistributed within the membrane of target cells, and it is found that redistribution of GlUT-1 reflects the pattern of envelope accumulation on the HTLV -1 infected cell. Expand
Probing the Fusion-Active Structures of Envelope of Human T-cell Leukaemia Virus Type-1 with Conformation-Specific Monoclonal Antibodies
Infection of cells by human T cell leukaemia virus (HTLV1) is mediated by the viral envelope glycoproteins. The gp46 surface glycoprotein binds to the cell surface receptor Glut-1, allowing theExpand