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- Donhauser, Zachary J.; Saunders, Jared T.; D’Urso, Dennis S.; Garrett, Teresa A.
- Biochemistry 2017 v.56 no.44 pp. 5900-5909
- atomic force microscopy; axons; chemical interactions; depolymerization; dimerization; electrolytes; electrostatic interactions; humans; ionic strength; mica; microtubules; models; mutants; polymerization; proteins; silicon nitride
- ... Tau is a microtubule-associated protein found in neuronal axons that has several well-known functions, such as promoting microtubule polymerization, stabilizing microtubules against depolymerization, and spatially organizing microtubules in axons. Two contrasting models have been previously described to explain tau’s ability to organize the spacing between microtubules: complementary dimerization ...
- Qin, Lingyun; Liu, Huili; Chen, Rong; Zhou, Jingjing; Cheng, Xiyao; Chen, Yao; Huang, Yongqi; Su, Zhengding
- Biochemistry 2017 v.56 no.44 pp. 5943-5954
- amino acid sequences; binding capacity; chemical interactions; drugs; engineering; ligands; mice; models; molecular dynamics; mutants; oncogene proteins; pharmacology; prediction; protein conformation; protein engineering; screening
- ... The oncoprotein MdmX (mouse double minute X) is highly homologous to Mdm2 (mouse double minute 2) in terms of their amino acid sequences and three-dimensional conformations, but Mdm2 inhibitors exhibit very weak affinity for MdmX, providing an excellent model for exploring how protein conformation distinguishes and alters inhibitor binding. The intrinsic conformation flexibility of proteins plays ...