P4-0127 — Annual report 2015
1.
Non-immunoglobulin scaffolds: a focus on their targets

Non-immunoglobulin (non-Ig) scaffolds are, in contrast to antibodies, require no post-translational modification and can be used in bacteria. 102 proteins have been specifically targeted by 139 different non-Ig scaffold binders. Selected antiinflammatory scaffolds will be expressed in lactobacteria and used for treatment of inflammatory bowel disease.

COBISS.SI-ID: 3851377
2.
Lysosomal cysteine peptidases - molecules signaling tumor cell death and survival

Lysosomal cysteine peptidases - cysteine cathepsins - are general intracellular protein-degrading enzymes that control also a variety of specific physiological processes. They can trigger irreversible events leading to signal transduction and activation of signaling pathways, resulting in cell survival and proliferation or cell death. In cancer cells, lysosomal cysteine peptidases are involved in multiple processes during malignant progression.

COBISS.SI-ID: 3908977
3.
Anti-sense DNA d(GGCCCC)[sup]n expansions in C9ORF72 form i-motifs and protonated hairpins

Anti-sense DNA d(GGCCCC)[sup] expansions are repeats in genes encoding proteins, involved in neurodegenerative disorders. Authors demonstrated molecular mechanism involving the repeats in neurodegeneration.

COBISS.SI-ID: 29086759
4.
Nitroxoline impairs tumor progression in vitro and in vivo by regulating cathepsin B activity

Cathepsin B been shown to be involved in cancer progression. We reported an established antibiotic nitroxoline as a potent and selective inhibitor of cathepsin and elucidated its anti-tumor properties in in vitro and in vivo tumor models. Nitroxoline significantly abrogated tumor growth, angiogenesis and metastasis in vivo in LPB fibrosarcoma and MMTV-PyMT breast cancer mouse models. Overall, our results designate nitroxoline as a promising drug candidate for anti-cancer treatment.

COBISS.SI-ID: 3834225
5.
Phosphorylation of C-terminal tyrosine residue 526 in FUS impairs its nuclear import

Protein FUS is important in pathogenesis in neurodegenerative disease ALS. Authors demonstrated that its transport to nucleus depends on the phosphorylation of C-terminal tyrosine, resulting in formation of deposits in the cytoplasm of neuronal cells.

COBISS.SI-ID: 29044263