We demonstrated, for the first time, the translocation of an sPLA2 from the extracellular space into the cytosol of a cell. Such an event may thus be important in explaining the action of a range of homologous endogenous sPLA2s enzymes in mammals whose roles in various cellular processes are not yet completely understood.
COBISS.SI-ID: 21453095
APOBEC3s are proteins of mammalian innate immunity and have an important role in antiviral defence. Mice lacking APOBEC3 were more susceptible to MMTV infection than wild type mice. This is the first study demonstrating the important role of APOBEC3 proteins in inhibiting viral replication in vivo.
COBISS.SI-ID: 20903975
L1 retrotransposons constitute the largest single component of mammalian genomes. We demonstrated that the genomes of Deuterostomia possess three highly divergent groups of L1 retrotransposons. This study establishes that the loss of L1 diversity and explosion in copy numbers occurred in the synapsid ancestors of mammals (Cynodontia). Importance of these findings is in the explanation of the 600 My of evolution of L1 retrotransposons in Deuterostomia, in the explanation of the origin of unique structure of mammalian genomes and in the involvement of paleogenomic investigations.
COBISS.SI-ID: 20498215
Actinoporins lyse cells by forming pores in cell membranes. Sphingomyelin plays an important role in their lytic activity, with membranes lacking this lipid being largely refractory to these toxins. As a means of characterising membrane binding by the actinoporin equinatoxin II (EqTII), we have used 19F NMR to probe the environment of tryptophan residues in the presence of micelles and bicelles. This study is the first attempt to describe the molecular mechanism of sphingomylein recognition by the protein molecule at the molecular level.
COBISS.SI-ID: 18918873
Actinoporins are pore-forming proteins that create pores in natural and model lipid membranes by the self-association of four monomers. It was shown recently that the N-terminal region (residues 10-28) of equinatoxin, an actinoporin from Actinia equina, participates in building of the final pore wall. Since the pore is formed solely by a polypeptide chain, other parts of the toxin should constitute the conductive channel. Results show that the flexible N-terminal region and stable beta-sandwich are pre-requisite for proper pore formation by the actinoporin protein family.
COBISS.SI-ID: 18475481
We demonstrated, for the first time, the translocation of an sPLA2 from the extracellular space into the cytosol of a cell. Such an event may thus be important in explaining the action of a range of homologous endogenous sPLA2s enzymes in mammals whose roles in various cellular processes are not yet completely understood.
COBISS.SI-ID: 21453095