Publications by authors named "Nenad Tomic"

Kidney damage can be induced by ischemia, autoimmune diseases, hypertension, allograft rejection, metabolic or genetic disorders, infections or toxins. The influence of these factors could result in acute kidney injury (AKI) defined as an unexpected decrease in urine output or renal function, or encourage the development of chronic kidney disease (CKD). Biomarkers of renal function, measured in urine and serum, are in increasing use in order to estimate the severity and nature of kidney injury, and consequently apply appropriate therapy and improve patient management.

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Peroxisomal biogenesis and function critically depends on the import of cytosolic proteins carrying a PTS1 sequence into this organelle upon interaction with the peroxin Pex5p. Recent structural studies have provided important insights into the molecular recognition of cargo proteins by Pex5p. Peroxisomal import is a key feature in the pathogenesis of primary hyperoxaluria type 1 (PH1), where alanine:glyoxylate aminotransferase (AGT) undergoes mitochondrial mistargeting in about a third of patients.

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Traits expected to be lost in the evolutionary history of a species occasionally reappear apparently out of the blue. Such traits as extra nipples or tails in humans, hind limbs in whales, teeth in birds, or wings in wingless stick insects remind us that certain genetic information is not completely lost, but can be reactivated. Atavisms seem to violate one of the central evolutionary principles, known as Dollo's law, that "an organism is unable to return, even partially, to a previous stage already realized in the ranks of its ancestors.

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The reaction between [PtCl2(DMSO)2] and L-cysteine (L-Cys) has been investigated in the presence of micelles of sodium dodecyl sulfate (SDS)--as a model for biological membranes. Additionally, the inhibitory effect of [PtCl2(DMSO)2] on the Na+,K+-ATPase activity and its partial prevention with 10 mM L-Cys were demonstrated. The interaction of L-Cys with [PtCl2(DMSO)2] resulted in the formation of a [Pt(DMSO)2(L-Cys)2]2+ (DMSO)2] complex, which most probably occurs through stepwise replacement of Cl(-) with L-Cys.

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The in vitro influence of potassium ion modulations, in the concentration range 2 mM-500 mM, on digoxin-induced inhibition of porcine cerebral cortex Na+ / K+-ATPase activity was studied. The response of enzymatic activity in the presence of various K+ concentrations to digoxin was biphasic, thereby, indicating the existence of two Na+ / K+-ATPase isoforms, differing in the affinity towards the tested drug. Both isoforms showed higher sensitivity to digoxin in the presence of K+ ions below 20 mM in the medium assay.

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