Atx forms a high-affinity complex with calmodulin CaM which leads to increase of its stability and enzymatic. We generated energetically the most favourable model of the complex. It explains, in structural terms, all of the effects observed. Based on the proposed structure we suggested that the four structurally similar mammalian sPLA2 isoforms from groups V and X, but not from IB and IIA, form stable complexes with CaM, which should also result in the augmentation of their enzymatic activity. By confirming the latter, the model is validated.
COBISS.SI-ID: 23512103
AtxA and its natural isoform AtxC from the venom of Vipera a. ammodytes exhibit strong neurotoxic and anticoagulant effects. We determined the crystal structures of the two isoforms and suggested the structural explanation of the significant differences in neurotoxicity and anticoagulant properties that they display.
COBISS.SI-ID: 23047975
We used natural toxin equinatoxin II to prepare a fusion protein with green fluorescent protein. We showed that fusion protein selectively recognizes membranes that contain sphingomylein, an important cellular lipid. The fusion protein stained plasma membrane of cells when added to the apical side of epithelial cells (MDCK cells), but not to the basolateral side. The fusion protein stained Golgi apparatus, when transiently expressed in cells. The study opens a lot of questions about synthesis and distribution of sphingomyelin in cells.
COBISS.SI-ID: 2119855
In this work, Fourier-transformed infrared spectroscopy (FTIR) and electron paramagnetic resonance (EPR) were used to analyze the ordering and dynamics of membrane lipids and the membrane domain structure of a series of unilamellar liposomes. We show that chemical properties of membrane constituents, their specific distribution, and physical characteristics of membrane nanodomains, resulted from the presence of sterol and sphingomyelin (or a highly ordered phospholipid, dipalmitoylphosphatidylcholine), are essential prerequisites for ostreolysin membrane binding and pore-formation.
COBISS.SI-ID: 2185551
We have identified that TDP-43 is imported into the nucleus via the Karyopheirn beta 1 pathway and that knockdown of members of the pathway can lead to cytoplasmic accumulation of TDP-43. We have also observed that one of the members of the pathway, CAS (cell apoptosis susceptibility protein) is greatly reduced in the post-mortem brain tissue of patients who had FTLD, which may be one of the reasons for cytoplasmic TDP-43 accumulation in this disease.
COBISS.SI-ID: 23645223