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SIRT3 - Safic-Alcan Italia
SIRT3 - Safic-Alcan Italia

... is the third member of the mammalian sirtuin family. The SIRT3 gene encodes the protein SIRT3, which exhibits NAD+-dependent deacetylase activity. ƒ SIRT3 is a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin c ...
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... The present syllabus reinforces the ideas introduced till the secondary classes. It provides the students with new concepts along with an extended exposure to contemporary areas of the subject. The syllabus also aims at emphasizing on the underlying principles that are common to both animals and pla ...
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... The separated protein bands are then blotted onto a nitrocellulose blue gel images on the left. Next show the ‘nitrocellulose membrane. These membranes are then probed either by means of sheet’ which must be superimposed on the gel. When specific anti-phospho-amino acid antibodies or more recently, ...
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... resulted in IL-6 independence, decreased apoptosis, and an enhanced proliferative response to IL-6. In the presence of ligand, wild-type FGFR3-expressing cells also exhibited enhanced proliferation and survival in comparison to controls. B9 clones expressing either wild-type FGFR3 at high levels or ...
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... Subunit composition and topology GABAA receptors are composed of pentameric arrangements of subunits around a central ion channel pore. Eighteen possible subunits including a1–6, b1–3, g 1–3, d, e, p, r1–3 subtypes have been identified in the mammalian genome. If there were no limitations to recepto ...
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... pockets of EF-Tu and the ribosomal A-site could easily show specificity for the different amino acid side chains. The hidden specificities of EF-Tu As would be expected for a protein that must bind multiple substrates, EF-Tu binds to all cognate aa-tRNAs within a narrow range of affinities [17,18]. ...
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video slide - Independent School District 196
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... A different structural model exists for the highest molecular weight gliadins. Omega-gliadins contain short, distinct C and N terminal sequences, separated by a region of repeatable sequences similar to γ gliadins. The sequence differs from that of γ gliadins, however, in having additional glutamine ...
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Cell-penetrating peptide



Cell-penetrating peptides (CPPs) are short peptides that facilitate cellular uptake of various molecular cargo (from nanosize particles to small chemical molecules and large fragments of DNA). The ""cargo"" is associated with the peptides either through chemical linkage via covalent bonds or through non-covalent interactions. The function of the CPPs are to deliver the cargo into cells, a process that commonly occurs through endocytosis with the cargo delivered to the endosomes of living mammalian cells.CPPs hold great potential as in vitro and in vivo delivery vectors for use in research and medicine. Current use is limited by a lack of cell specificity in CPP-mediated cargo delivery and insufficient understanding of the modes of their uptake.CPPs typically have an amino acid composition that either contains a high relative abundance of positively charged amino acids such as lysine or arginine or has sequences that contain an alternating pattern of polar/charged amino acids and non-polar, hydrophobic amino acids. These two types of structures are referred to as polycationic or amphipathic, respectively. A third class of CPPs are the hydrophobic peptides, containing only apolar residues, with low net chargeor have hydrophobic amino acid groups that are crucial for cellular uptake.The first CPP was discovered independently by two laboratories in 1988, when it was found that the trans-activating transcriptional activator (TAT) from human immunodeficiency virus 1 (HIV-1) could be efficiently taken up from the surrounding media by numerous cell types in culture. Since then, the number of known CPPs has expanded considerably and small molecule synthetic analogues with more effective protein transduction properties have been generated.
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