Voegtli WC, Madrona AY, Wilson DK (2003) The structure of Aip1p, a WD repeat protein that regulates Cofilin-mediated actin depolymerization. Neer EJ, Schmidt CJ, Nambudripad R, Smith TF (1994) The ancient regulatory-protein family of WD-repeat proteins. Janda L, Tichý P, Spízek J, Petrícek M (1996) A deduced Thermomonospora curvata protein containing serine/threonine protein kinase and WD-repeat domains. Letunic I, Doerks T, Bork P (2009) SMART 6: recent updates and new developments. Ouyang Y, Huang X, Lu Z, Yao J (2012) Genomic survey, expression profile and co-expression network analysis of OsWD40 family in rice. Van Nocker S, Ludwig P (2003) The WD-repeat protein superfamily in Arabidopsis: conservation and divergence in structure and function. Īndrade MA, Perez-Iratxeta C, Ponting CP (2001) Protein repeats: structures, functions, and evolution. Xu C, Min J (2011) Structure and function of WD40 domain proteins. Stirnimann CU, Petsalaki E, Russell RB, Müller CW (2010) WD40 proteins propel cellular networks. Smith TF, Gaitatzes C, Saxena K, Neer EJ (1999) The WD repeat: a common architecture for diverse functions. Li D, Roberts R (2001) WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases. The review summarizes the vast array of functions performed by different WD40 domain containing proteins, their domain organization and functional conservation during the course of evolution. Several WD40 domain-containing proteins have been recently characterized in prokaryotes as well. So far, no WD40 domain has been identified with intrinsic enzymatic activity. To play the regulatory role in various processes, they act as a scaffold for protein–protein or protein–DNA interaction. WD40 repeats containing proteins, in lower eukaryotes, are mainly involved in growth, cell cycle, development and virulence, while in higher organisms, they play an important role in diverse cellular functions like signal transduction, cell cycle control, intracellular transport, chromatin remodelling, cytoskeletal organization, apoptosis, development, transcriptional regulation, immune responses. In proteins the WD domain folds into a β-propeller structure, providing a platform for the interaction and assembly of several proteins into a signalosome.
This study showed better adhesion and growth of endothelial cells in the vessel's inner wall.The WD40 domain is one of the most abundant and interacting domains in the eukaryotic genome.
The absence of cytotoxicity in this system was investigated, and these nanofibers with the drug showed 91% cell survival after seven days. Also, the MTT dialysis bag was used to release the Heparin and toxicity of the produced nanofibers. Also, the obtained fibers were miscible and had no fuzzy separation. The prepared nanofibers were examined for morphology (FT-IR, SEM, and XRD). gossypinus coating (3%)/gelatin by electrospinning method with two-phase voltage 16.5 kW-distance needle up to 18 cm collector feed rate 0.2 was prepared. Therefore, nanofibers of chitosan complex (2%)/polyurethane (14.5%)/cow protein (1%)/gelatin (20%) with A. This study was to load the anticoagulant drug heparin on nanofibers. This study aimed to synthesize electrospun of polyurethane/chitosan/ Vicia ervilia protein/gelatin/heparin-coated with Astragalus gossypinus scaffold for cardiovascular tissue engineering. With the increasing number of patients with heart disease and the relative inefficiency of existing treatments, finding a new way to treat heart disease is one of the main topics studied by researchers in recent decades.
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