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and develop analytical methods for peptides and proteins, membrane spanning proteins, and receptor binding proteins. Candidate must possess a complete understanding of HPLC methods including normal and reverse-phase chromatography, Gel… Read more here: and develop analytical methods for peptides and proteins, membrane spanning proteins, and receptor binding proteins. Candidate must possess a complete understanding of HPLC methods including normal and reverse-phase chromatography, Gel… Read more here: column chromatography, and membrane concentration of proteins . The individual will document experimental methods and results in well-maintained laboratory notebook, participate in interaction with R&D, QC and Manufacturing and presentation… The rest is here:
Invest Ophthalmol Vis Sci. 2012 Apr 24; Purpose:Mutations in either retinoid isomerase (RPE65) or lecithin-retinol acyltransferase (LRAT) lead to Leber congenital amaurosis (LCA). By using the Lrat(-/-) mouse model, we have shown previously that the rapid cone degeneration in LCA was caused by endoplasmic reticulum (ER) stress induced by S-opsin aggregation. The purpose of this study is to examine the efficacy of an ER chemical chaperone, tauroursodeoxycholic acid (TUDCA), in preserving cones in the Lrat(-/-) model. Methods:Lrat(-/-) mice were systemically administered with TUDCA and vehicle (0.15 M NaHCO(3)) every 3 days from P9 to P28. Cone cell survival was determined by counting cone cells on flat-mounted retinas. The expression and subcellular localization of cone specific proteins were analyzed by western blotting and immunohistochemistry, respectively. Results:TUDCA treatment reduced ER stress and apoptosis in Lrat(-/-) retina. It significantly slowed down cone degeneration in Lrat(-/-) mice, resulting in a ~ 3-fold increase in cone density in the ventral and central retina as compared to the vehicle treated mice at P28. Furthermore, TUDCA promoted the degradation of cone membrane associated proteins by enhancing the ER-associated protein degradation pathway (ERAD). Conclusions:Systemic injection of TUDCA is effective in reducing ER stress, preventing apoptosis, and preserving cones in Lrat(-/-) mice. TUDCA has the potential to lead to the development of a new class of therapeutic drugs for treating LCA. Read the original post: Specialist will study the structure and function of membrane proteins and will use a variety of cutting-edge biophysical and high-throughput methods to interrogate enzymatic mechanisms. Responsibilities include, but are not limited to,… Read more here: Specialist will study the structure and function of membrane proteins and will use a variety of cutting-edge biophysical and high-throughput methods to interrogate enzymatic mechanisms. Responsibilities include, but are not limited to,… Read more here:
PLoS One. 2012; 7(4): e34845 Dyrk1A phosphorylated multiple proteins in the clathrin-coated vesicle (CCV) preparations obtained from rat brains. Mass spectrometric analysis identified MAP1A, MAP2, AP180, and α- and β-adaptins as the phosphorylated proteins in the CCVs. Each protein was subsequently confirmed by [(32)P]-labeling and immunological methods. The Dyrk1A-mediated phosphorylation released the majority of MAP1A and MAP2 and enhanced the release of AP180 and adaptin subunits from the CCVs. Furthermore, Dyrk1A displaced adaptor proteins physically from CCVs in a kinase-concentration dependent manner. The clathrin heavy chain release rate, in contrast, was not affected by Dyrk1A. Surprisingly, the Dyrk1A-mediated phosphorylation of α- and β-adaptins led to dissociation of the AP2 complex, and released only β-adaptin from the CCVs. AP180 was phosphorylated by Dyrk1A also in the membrane-free fractions, but α- and β-adaptins were not. Dyrk1A was detected in the isolated CCVs and was co-localized with clathrin in neurons from mouse brain sections and from primary cultured rat hippocampus. Previously, we proposed that Dyrk1A inhibits the onset of clathrin-mediated endocytosis in neurons by phosphorylating dynamin 1, amphiphysin 1, and synaptojanin 1. Current results suggest that besides the inhibition, Dyrk1A promotes the uncoating process of endocytosed CCVs. Go here to read the rest:
Biopolymers. 2012 Jul; 97(7): 558-67 Membrane transporters catalyze the transport of small solute molecules across biological barriers such as lipid bilayer membranes. As the experimental annotation of which proteins transport which substrates is incomplete it is highly desirable to develop computational methods that can assist in the classification and substrate annotation of putative membrane transport proteins. Here, we determined the similarity of membrane transporter sequences annotated in the Transport Classification Database (Saier et al., Nucleic Acids Res 2006, 34, D181-D186) and Arabidopsis thaliana membrane transporters annotated in the database Aramemnon (Schwacke et al., Plant Physiol 2003, 131, 16-26). The similarity measure was based on the amino acid composition either considering the full sequences or separately in the transmembrane (TM) and external parts of the sequences. We considered four different substrate sets and three different subfamilies and tried to classify the given proteins into these classes. Family or substrate prediction based on the simple amino acid frequency had an average accuracy of 76%. The differentiation between TM and non-TM regions led to an improved accuracy of 80% on average. © 2012 Wiley Periodicals, Inc. Biopolymers 97:558-567, 2012. Read the rest here: |
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