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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

Alpha-L-fucosidase,AFU is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.

The connexin family of proteins form hexameric complexes called connexons that facilitate movement of low molecular weight proteins between cells via gap junctions. Connexin proteins share a common topology of four transmembrane alpha-helical domains, two extracellular loops, a cytoplasmic loop and cytoplasmic N- and C-termini. Many of the key functional differences between connexins arise from specific amino-acid substitutions in the most highly conserved domains: the transmembrane and extr

Neurofibromin is a product of the tumor suppressor gene, Neurofibromatosis type I. Neurofibromin is known to have GTPase activity that modulates the ras pathway. The absence of or alteration of the neurofibromin protein may lead to Neurofibromatosis disease. This protein has not been purified, therefore, most of the information regarding this protein has been deduced from homology analysis of its gene sequence.

Binds to the Fc region of immunoglobulins alpha. Mediates several functions including cytokine production.$n $nTissue specificity; $n Isoform A.1, isoform A.2 and isoform A.3 are differentially expressed between blood and mucosal myeloid cells. Isoform A.1, isoform A.2 and isoform A.3 are expressed in monocytes. Isoform A.1 and isoform A.2 are expressed in alveolar macrophages; however only one isoform is expressed at alveolar macrophages surfaces.

Syntrophins are cytoplasmic peripheral membrane scaffold proteins that are components of the dystrophin-associated protein complex. This gene is a member of the syntrophin gene family and encodes the most common syntrophin isoform found in cardiac tissues. The N-terminal PDZ domain of this syntrophin protein interacts with the C-terminus of the pore-forming alpha subunit (SCN5A) of the cardiac sodium channel Nav1.5. This protein also associates cardiac sodium channels with the nitric oxide syn