anki [dot] mossberg [at] med [dot] lu [dot] se
Publikationer (hämtat ur Lunds universitets publikationsdatabas)
- Eight Nucleotide Substitutions Inhibit Splicing to HPV-16 3'-Splice Site SA3358 and Reduce the Efficiency by which HPV-16 Increases the Life Span of Primary Human Keratinocytes.
- Suppression of HPV-16 late L1 5'-splice site SD3632 by binding of hnRNP D proteins and hnRNP A2/B1 to upstream AUAGUA RNA motifs.
- HAMLET Treatment Delays Bladder Cancer Development.
- HAMLET interacts with lipid membranes and perturbs their structure and integrity.
- Human milk as a source of tumor killing molecules. From MAL to HAMLET.
- Structure and function of human α-lactalbumin made lethal to tumor cells (HAMLET)-type complexes.
- Can misfolded proteins be beneficial? The HAMLET case.
- HAMLET (human alpha-lactalbumin made lethal to tumor cells) triggers autophagic tumor cell death.
- alpha-Lactalbumin, Engineered to be Non-native and Inactive, Kills Tumor Cells when in Complex with Oleic Acid: A new biological function resulting from partial unfolding.
- Human alpha-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival.
- Treatment of skin papillomas with topical alpha-lactalbumin-oleic acid
- Treatment of skin papillomas with topical alpha-lactalbumin-oleic acid.
- HAMLET kills tumor cells by an apoptosis-like mechanism--cellular, molecular, and therapeutic aspects.
- Lipids as cofactors in protein folding: Stereo-specific lipid-protein interactions are required to form HAMLET (human alpha-lactalbumin made lethal to tumor cells).
- alpha-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human alpha-lactalbumin made lethal to tumor cells).