1.

Proteomic identification of cysteine cathepsin substrates shed from the surface of cancer cell

In this report we have shown cysteine cathepsins can act like sheddases and cleave protein ectodomains from the cell surface. Proteomic analysis of various cell types has shown that cysteine cathepsins can shed structurally closely related group of cell adhesion molecules and membrane receptors. Observed substrate cleavages were confirmed also in vivo in murine cancer model.

COBISS.SI-ID: 28696103

2.

Fast profiling of protease specificity reveals similar substrate specificities for cathepsins K, L and S

In this report we presented a fast and straightforward approach for profiling of protease specificity. The method was applied for the profiling of cysteine cathepsins K, L and S.

COBISS.SI-ID: 28342823

3.

Current trends and challenges in proteomic identification of protease substrates

In this review article we presented the latest methodologies for identification of protease substrates and profiling of protease specificity.

COBISS.SI-ID: 29060647

4.

Cysteine cathepsins and extracellular matrix degradation

Cysteine cathepsins are among the major proteases involved in ECM remodeling and their role is not limited to degradation only. In this review we focused in their extracellular functions linked to ECM degradation and discussed their importance in pathologies and treatment of ECM related diseases.

COBISS.SI-ID: 27616039

5.

Selective targeting of tumor and stromal cells by a nanocarrier system displaying lipidated cathepsin B inhibitor

In this study we have performed proteomic analysis of cancer cell secretome of murine model of mammarian gland cancer. We have identified cathepsin B as the most abundant protease in the secretome.

COBISS.SI-ID: 27932455