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Substantia nigra (SN) colocalized with TH in neurons, GFAP in astrocytes and OX-6 and OX-42 in activated microglia [166?68]. Using different carboxy terminal directed AT1 and AT2 antibodies for Western blotting, it was shown that estrogen treatment of ovariectomized rats, which was protective against 6-hydroxydopamine induced neurotoxicity in the SN, decreased AT1 and increased AT2 expression in t
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Substantia nigra (SN) colocalized with TH in neurons, GFAP in astrocytes and OX-6 and OX-42 in activated microglia [166?68]. Using different carboxy terminal directed AT1 and AT2 antibodies for Western blotting, it was shown that estrogen treatment of ovariectomized rats, which was protective against 6-hydroxydopamine induced neurotoxicity in the SN, decreased AT1 and increased AT2 expression in t
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Ns [102, 106]. In contrast, IDPs are charged proteins, thus they can control their interfacial absorption onto solid surfaces [106]. Experiments, in silico, suggest that intrinsically disordered peptides absorbed to a surface with a complementary pattern form a well-defined structure (-helix) indicating that a specific surface can stabilize the structure of an IDP peptide. The effect of a compleme
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Tructures on binding. 2.4 Self-Assembly of IDPs IDPs frequently undergo self-assembly. The extended conformation of IDPs facilitates the intermolecular interactions between them and promotes formation of supramolecular architecture [109]. This is illustrated in some of the mineralized tissues discussed above. Silaffins, for example, are protein constituents of biosilica, playing an active role in
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Tructures on binding. 2.4 Self-Assembly of IDPs IDPs frequently undergo self-assembly. The extended conformation of IDPs facilitates the intermolecular interactions between them and promotes formation of supramolecular architecture [109]. This is illustrated in some of the mineralized tissues discussed above. Silaffins, for example, are protein constituents of biosilica, playing an active role in
1
Tructures on binding. 2.4 Self-Assembly of IDPs IDPs frequently undergo self-assembly. The extended conformation of IDPs facilitates the intermolecular interactions between them and promotes formation of supramolecular architecture [109]. This is illustrated in some of the mineralized tissues discussed above. Silaffins, for example, are protein constituents of biosilica, playing an active role in
1
Ns [102, 106]. In contrast, IDPs are charged proteins, thus they can control their interfacial absorption onto solid surfaces [106]. Experiments, in silico, suggest that intrinsically disordered peptides absorbed to a surface with a complementary pattern form a well-defined structure (-helix) indicating that a specific surface can stabilize the structure of an IDP peptide. The effect of a compleme
1
Ns [102, 106]. In contrast, IDPs are charged proteins, thus they can control their interfacial absorption onto solid surfaces [106]. Experiments, in silico, suggest that intrinsically disordered peptides absorbed to a surface with a complementary pattern form a well-defined structure (-helix) indicating that a specific surface can stabilize the structure of an IDP peptide. The effect of a compleme