The aim of this study was to analyze the microhardness of two resin-modified glass ionomer cements (Vitremer; Fuji II LC); two polyacid-modified composite resins (Freedom; F2000) and a hybrid composite resin (Prodigy), at different depths from the upper surface. Six hemi-cylinders (3 mm height; 3 mm radius) per tested material were obtained. Vickers Hardness was determined using a micro-indenta...

The effect of flaxseed gum (FG) on the rheological and nonlinear stress response behaviors of mixed soy protein isolate (SPI)-flaxseed gum (FG) dispersions were studied. Results showed that the viscosity of the SPI-FG mixed dispersions increased significantly with increase in the FG concentration. Both the shear stress and the apparent viscosity values as a function of shear rate were fitted we...

Nucleocytoplasmic transport has been the subject of a large body of research in the past few decades. Recently, the focus of investigations in this field has shifted from studies of the overall function of the nuclear pore complex (NPC) to the examination of the role of different domains of phenylalanine-glycine nucleoporin (FG Nup) sequences on the NPC function. In our recent bioinformatics st...

Entropy guards pore T he rapid fl uctuations of fl exible FG repeat–containing nucleoporins (FG Nups) form an entropic barrier to would-be entrants into the nuclear pore complex (NPC), according to Roderick Lim (University of Basel, Switzerland) and colleagues. FG Nups, which consist of large natively unfolded domains, are the pore’s gatekeepers—they keep out proteins that are not bound to tran...

The origin of platelet alpha-granule fibrinogen (Fg), whether from endogeneous synthesis or exogeneous derivation, remains unknown. Although Fg biosynthesis by megakaryocytes (MK) has been suggested, recent studies have demonstrated that certain alpha-granular proteins originate primarily from plasma. To study the origin of alpha-granule Fg, platelet-associated Fg was measured by ELISA and West...

Nucleoporins with phenylalanine-glycine repeats (FG Nups) function at the nuclear pore complex (NPC) to facilitate nucleocytoplasmic transport. In Saccharomyces cerevisiae, each FG Nup contains a large natively unfolded domain that is punctuated by FG repeats. These FG repeats are surrounded by hydrophilic amino acids (AAs) common to disordered protein domains. Here we show that the FG domain o...