Tafazzin regulates human conjunctiva epithelial cell proliferation via inhibiting TGFβ signaling pathway

Molecular Vision181402-1410MVEP

Effect of dispase denudation on amniotic membrane

Molecular Vision151962-197

Effect of intracameral injection of fibrin tissue sealant on the rabbit anterior segment

Molecular Vision161087-1097MVEP

Preservation of mesophilic mixed culture for anaerobic palm oil mill effluent treatment by convective drying methods

[EN] While anaerobic digestion is a reliable method that treats the waste and produces renewable biomethane fuel, the necessary sludge in liquid form is difficult to handle due to the constant biogas generation. Therefore, this study investigates the possibility of convective air drying, namely heat pump and hot air circulation oven as preservation methods for anaerobic microbial sludge. Drying was conducted at various temperatures, ranging from 22℃ to 70℃. The study found that heat pump drying at 22℃ resulted in highest COD removal of 55.3% as well as the least log reduction in methanogens and anaerobes at 1.4 and 2.4, respectively.Chin, SK.; Tan, DT.; Tan, HM.; Poh, PE. (2018). Preservation of mesophilic mixed culture for anaerobic palm oil mill effluent treatment by convective drying methods. En IDS 2018. 21st International Drying Symposium Proceedings. Editorial Universitat Politècnica de València. 1971-1978. https://doi.org/10.4995/IDS2018.2018.7295OCS1971197

Analysis of conjunctival fibroblasts from a proband with Schnyder corneal dystrophy

Molecular Vision141277-128

Cornea lenticule viability and structural integrity after refractive lenticule extraction (ReLEx) and cryopreservation

Molecular Vision173437-3449MVEP

Insights into biofilm dispersal regulation from the crystal structure of the PAS-GGDEF-EAL region of RbdA from Pseudomonas aeruginosa

© 2018 American Society for Microbiology. RbdA is a positive regulator of biofilm dispersal of Pseudomonas aeruginosa. Its cytoplasmic region (cRbdA) comprises an N-terminal Per-ARNT-Sim (PAS) domain followed by a diguanylate cyclase (GGDEF) domain and an EAL domain, whose phosphodiesterase activity is allosterically stimulated by GTP binding to the GGDEF domain. We report crystal structures of cRbdA and of two binary complexes: one with GTP/Mg 2+ bound to the GGDEF active site and one with the EAL domain bound to the c-di-GMP substrate. These structures unveil a 2-fold symmetric dimer stabilized by a closely packed N-terminal PAS domain and a noncanonical EAL dimer. The autoinhibitory switch is formed by an α-helix (S-helix) immediately N-terminal to the GGDEF domain that interacts with the EAL dimerization helix (α6-E) of the other EAL monomer and maintains the protein in a locked conformation. We propose that local conformational changes in cRbdA upon GTP binding lead to a structure with the PAS domain and S-helix shifted away from the GGDEF-EAL domains, as suggested by small-angle X-ray scattering (SAXS) experiments. Domain reorientation should be facilitated by the presence of an α-helical lever (H-helix) that tethers the GGDEF and EAL regions, allowing the EAL domain to rearrange into an active dimeric conformation