Prediction of the heat transfer characteristics on natural convection in a long rectangular enclosure with a twisted cylinder using direct simulation and artificial neural networks

Journal of Mechanical Science and Technology - A three-dimensional direct simulation was carried out to examine the natural convective fluid flow and heat transfer characteristics in a long...     

Stress states investigation of adhesive bonded joint between spar cap and shear webs of a large wind turbine rotor blade

Journal of Mechanical Science and Technology - The debonding failure at the adhesive bonded joints between spar caps and shear webs is one of failure modes of the wind turbine rotor blades. To...     

Co-overexpression of the malate dehydrogenase (Mdh) and the malic enzyme A (MaeA) in several Escherichia coli mutant backgrounds increases malate redirection towards hydrogen production

The combustion of fossil fuels is leading to global warming due to the emissions of greenhouse gases. Hydrogen (H₂) is a clean and sustainable energy source and a promising alternative to fossil fuels. The bacteria Escherichia coli naturally produces H₂, and it has been widely modified by metabolic engineering to enhance this production. Malate plays an important role in H₂ synthesis when glycerol is used as a C source. In this work, C-flux was more efficiently redirected from malate to H₂ by the P_BAD promoter-controlled co-overexpression of the malate dehydrogenase and the malic enzyme MaeA in the dcuD and frdCdcuD mutants. These mutants previously have been reported as improved producing strains, but by using this strategy, H₂ production increased 36 and 24%, respectively. The overexpression of both enzymes is essential, although MaeA expression was higher than Mdh, using the pBAD promoter, which was more appropriate than the pTrc99a one.     

E3 Ubiquitin Ligase APC/CCdh1 Negatively Regulates FAH Protein Stability by Promoting Its Polyubiquitination

Fumarylacetoacetate hydrolase (FAH) is the last enzyme in the degradation pathway of the amino acids tyrosine and phenylalanine in mammals that catalyzes the hydrolysis of 4-fumarylacetoacetate into acetoacetate and fumarate. Mutations of the FAH gene are associated with hereditary tyrosinemia type I (HT1), resulting in reduced protein stability, misfolding, accelerated degradation and deficiency in functional proteins. Identifying E3 ligases, which are necessary for FAH protein stability and degradation, is essential. In this study, we demonstrated that the FAH protein level is elevated in liver cancer tissues compared to that in normal tissues. Further, we showed that the FAH protein undergoes 26S proteasomal degradation and its protein turnover is regulated by the anaphase-promoting complex/cyclosome-Cdh1 (APC/C)^Cdh1 E3 ubiquitin ligase complex. APC/C^Cdh1 acts as a negative stabilizer of FAH protein by promoting FAH polyubiquitination and decreases the half-life of FAH protein. Thus, we envision that Cdh1 might be a key factor in the maintenance of FAH protein level to regulate FAH-mediated physiological functions.     

Unsteady characteristics of laminar free convection in an enclosure in the presence of power law fluid at Ra = 107

Journal of Mechanical Science and Technology - The present study deals with an unsteady laminar free convection inside the annuli confined between an outer square enclosure and an inner circular...     

Revisiting “Steady-State” Monotonic and Cyclic Deformation: Emphasizing the Quasi-Stationary State of Deformation

Metallurgical and Materials Transactions A - High-temperature creep, cyclic deformation in saturation, and a number of technologically important processes are typical examples of the so-called...