SAM breaks its stereotype.
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The 1-(4-mercaptobutyl)-4-(2-ferrocenylvinyl)pyridinium bromide (1-HS(CH2)(4)-4-[(E)-FcCH=CH]C5H4N)+Br- and its hydrogenated product [1-HS(CH2)(4)-4-(-FcCH2CH2)C5H4N]+Br- were synthesized and assembled on an Au electrode to form self-assembled monolayers which showed a structure-dependent electrochemical-response in phosphate buffer aqueous solutions (pH = 7).
A variety of groups like a Fischer carbene complex, an N-hydroxysuccinimide or a ferrocene derivative have been grafted by ruthenium-catalyzed cross-metathesis reaction with terminal alkene groups on monolayer-protected gold clusters as a mild and convenient strategy to anchor functional molecules.
We report the fabrication of flavin-functionalised self-assembled monolayers upon gold electrodes and their subsequent redox modulation via hydrogen bonding to 2,6-diethylamidopyridine.
Tankyrases 1 and 2 are two highly related poly(ADP-ribose) polymerases that interact with a variety of cytoplasmic and nuclear proteins. Both proteins have been implicated in telomere length regulation, insulin signalling and centrosome function. To learn more about their mode of action, we have isolated the chicken tankyrase homologues and examined their interaction partners and subcellular location. Cross-species sequence comparison indicated that tankyrase domain structure is highly conserved and supports division of the ankyrin domain into five subdomains, which are each separated by a highly conserved LLEAAR/K motif. Glutathione S-transferase pull-down experiments demonstrated that the ankyrin domains of both proteins interact with chicken telomere repeat factor 1 (TRF1). Analysis of total cellular and nuclear proteins revealed that cells contain approximately twice as much tankyrase 1 as tankyrase 2. Although > or = 90% of each protein is present in the cytoplasm, both tankyrase 1 and 2 were detected in the nucleus. The nuclear location together with its ability to interact with TRF1, point to tankyrase 2 having a telomeric function. Yeast two-hybrid and cross-linking experiments show that both tankyrases can multimerize through their sterile-alpha motif domains. These results indicate that tankyrases may be master scaffolding proteins, capable of regulating assembly of large protein complexes.
We present a sporadic case of a Japanese female infant with ectodermal dysplasia, complete cleft lip and palate, severe skin erosions at birth and recurrent scalp infection. She had typical clinical features of ankyloblepharon, ectodermal defects and cleft lip and palate (AEC) syndrome without ankyloblepharon. Histological and immunohistochemical analyses showed reduced granular cell layers and aberrant expression of the p63 protein in the suprabasal keratinocytes. Mutation analysis of the exon 13 of p63 gene revealed a heterozygous in-frame 3-bp insert (c. 538-539 ins TTC) encoding additional amino acid residues (F). This is the first report of sterile alpha motif domain mutation except for single nucleotide transitions.
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Explore the source record for details and available documents.
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Explore the source record for details and available documents.
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