Current Proteomics - Volume 11, Issue 1, 2014

Heat shock protein 90 (Hsp90) is highly conserved chaperone protein which plays vital roles in stabilization, regulation and folding of client proteins in cancer cells. Client proteins are key macromolecules for carcinogenesis and their maintenance (stabilization and protection from aggregation and misfolding) is provided by Hsp90 chaperone activity. Hsp90 allows proliferation of cancer cells by keeping misfolded client proteins i Read More

Numerous genome sequence projects of various organisms have resulted in generation of large amount of data on genes and proteins sequence information. Functional annotation of these proteins is important to bridge gap between sequence information and functional characterization. As experimental approaches for characterizing the functional class of an enzyme are expensive and time consuming, computational predic Read More

Purified chitin binding protein the CBP50 from Bacillus thuringiensis and three bacterial chitinases (Chi74, Chi39 and ChiA) from two different genome sources i.e. Bacillus thuringiensis (Bt) and Serratia proteamaculans, were used to study the crystalline chitin degradation using different combinations of chitinases with and without chitin binding protein CBP50. Overall 2-4 folds increase in enzymatic activity of all three chiti Read More

Cadmium (Cd) is a well known environmental and industrial heavy metal with multi-organ toxic effects. In this study, we examined the effects of Cd as cadmium chloride (CdCl2) on the proteomic profiles of exposed HEK 293, HepG2 and 1321N1 cells in an attempt to develop suitable biomarkers for Cd toxicity. 2D-gel electrophoresis (2DE) was performed on the cell extracts after 24 hr exposure to 5, 10 and 50 µM Cd and protein Read More

The molecular mechanisms that cause myopia are largely unknown. However, signaling pathways originating in the retina are implicated in regulating refractive development. The study of retinal protein expression profiles ("proteomics") in animal eyes is a powerful approach to unraveling these molecular mechanisms. Previously, we used this proteomics approach in the chick model to identify a number of protei Read More

Background and Aims: Our previous yeast two-hybrid screening data showed the Fibrinogen alpha chain (FGA) as one of the candidate binding proteins of S regional of the HBsAg (HBs). In this study, we aimed to define that FGA is a binding protein of HBs and to determine its function in Hepatocellular carcinoma (HCC) tumorigenesis. Methods: The binding and co-localization between HBs and FGA were confirmed using c Read More

We demonstrate the Binary Identified Contact Domain (BICD) method for predicting binding sites for proteins that starts with amino-acid sequences of several species, finds regions that are evolutionarily conserved, and weights regions by their local hydrophilicity. The measure of conservation takes transversions as significant but transitions as insignificant, in keeping with a theory of original singlet codes. The BICD method corr Read More

To understand the cold stress response of soybean, 480 soybean germplasms were used to find the tolerant and sensitivity of germplasm to cold. Then a comparative proteomic analysis between soybean seed treated at chilling and non-chilling temperature was carried out using the tolerant cold soybean germplasm. During the germination of seed, it was possible to discriminate between proteins involved in symptoms and pr Read More

The aleurone layer (AL) is an inner tissue of the wheat grain. It contains micronutrients, vitamins, antioxidants and fibre, and can greatly increase the nutritional quality of flour if it is not removed from the kernel with the bran. The AL of mature kernels of three varieties of the two major cultivated wheat species T. aestivum (genome A, B and D) and T. monococcum (genome A) were manually dissected and analyzed using Read More