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The cyclophilins are a conserved class of proteins that bind the immunosuppressive drug cyclosporin A (CsA) with high affinity. CsA blocks helper T-cell activation at a step between T-cell receptor stimulation and the transcriptional activation of cytokine genes. Cyclophilins from many species possess peptidyl-prolyl cis-trans isomerase (PPIase) activity that is blocked by CsA and therefore may be relevant in CsA-mediated immunosuppression.

Modulation of the chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. The N-terminal tail of core histones undergoes different posttranslational modifications including acetylation, phosphorylation and methylation. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression. In most spec

oading Control$nGlyceraldehyde 3 phosphate dehydrogenase (GAPDH) is well known as one of the key enzymes involved in glycolysis. As well as functioning as a glycolytic enzyme in cytoplasm, recent evidence suggests that mammalian GAPDH is also involved in a great number of intracellular proceses such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. During the last decade a lot of data appeared concerning the role of GAPD