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Design typicality plays a major role in consumers’ reactions towards a product. Hence, assessing a product design’s typicality is vital to predicting consumers’ responses to a design. However, directly asking people for their subjective typicality experience may yield a biased measure as the rating arguably contains the overall aesthetic impression of the product. Against this background, we introduce four unbiased objective measures of design typicality (two based on feature points and two based on grids) and demonstrate their capability of capturing the subjective typicality experience. We validate the proposed measures in the context of automobile designs with ratings of aesthetic liking, processing fluency, and cumulative sales data by analysing 77 car models from four segments ranging from subcompact cars to SUVs. Our findings endorse the general notion that objective measures should be included in product design research; and the proposed objective approaches provide convenient means to easily assess design typicality.
In response to pathogen infection, gasdermin (GSDM) proteins form membrane pores that induce a host cell death process called pyroptosis1–3. Studies of human and mouse GSDM pores reveal the functions and architectures of 24–33 protomers assemblies4–9, but the mechanism and evolutionary origin of membrane targeting and GSDM pore formation remain unknown. Here we determine a structure of a bacterial GSDM (bGSDM) pore and define a conserved mechanism of pore assembly. Engineering a panel of bGSDMs for site-specific proteolytic activation, we demonstrate that diverse bGSDMs form distinct pore sizes that range from smaller mammalian-like assemblies to exceptionally large pores containing >50 protomers. We determine a 3.3 Å cryo-EM structure of a Vitiosangium bGSDM in an active slinky-like oligomeric conformation and analyze bGSDM pores in a native lipid environment to create an atomic-level model of a full 52-mer bGSDM pore. Combining our structural analysis with molecular dynamics simulations and cellular assays, our results support a stepwise model of GSDM pore assembly and suggest that a covalently bound palmitoyl can leave a hydrophobic sheath and insert into the membrane before formation of the membrane-spanning β-strand regions. These results reveal the diversity of GSDM pores found in nature and explain the function of an ancient post-translational modification in enabling programmed host cell death.
Background: To determine whether there is a significant saving of time when using a digital cataract workflow for digital data transfer compared to a manual approach of biometry assessment, data export, intraocular lens calculation, and surgery time.
Methods: In total, 48 eyes of 24 patients were divided into two groups: 24 eyes were evaluated using a manual approach, whereas another 24 eyes underwent a full digital lens surgery workflow. The primary variables for comparison between both groups were the overall time as well as several time steps starting at optical biometry acquisition until the end of the surgical lens implantation. Other outcomes, such as toric intraocular lens misalignment, reduction of cylinder, surgically induced astigmatism, prediction error, and distance visual acuity were measured.
Results: Overall, the total diagnostic and surgical time was reduced from 1364.1 ± 202.6 s in the manual group to 1125.8 ± 183.2 s in the digital group (p < 0.001). The complete time of surgery declined from 756.5 ± 82.3 s to 667.3 ± 56.3 (p < 0.0005). Compared to the manual approach of biometric data export and intraocular lens calculation (76.7 ± 12.3 s) as well as the manual export of the reference image to a portable external storage device (26.8 ± 5.5 s), a highly significant saving of time was achieved (p < 0.0001).
Conclusions: Using a software-based digital approach to toric intraocular lens implantation is convenient, more efficient, and thus more economical than a manual workflow in surgery practice.
In response to pathogen infection, gasdermin (GSDM) proteins form membrane pores that induce a host cell death process called pyroptosis1–3. Studies of human and mouse GSDM pores reveal the functions and architectures of 24–33 protomers assemblies4–9, but the mechanism and evolutionary origin of membrane targeting and GSDM pore formation remain unknown. Here we determine a structure of a bacterial GSDM (bGSDM) pore and define a conserved mechanism of pore assembly. Engineering a panel of bGSDMs for site-specific proteolytic activation, we demonstrate that diverse bGSDMs form distinct pore sizes that range from smaller mammalian-like assemblies to exceptionally large pores containing >50 protomers. We determine a 3.3 Å cryo-EM structure of a Vitiosangium bGSDM in an active slinky-like oligomeric conformation and analyze bGSDM pores in a native lipid environment to create an atomic-level model of a full 52-mer bGSDM pore. Combining our structural analysis with molecular dynamics simulations and cellular assays, we define a stepwise model of GSDM pore assembly and demonstrate that pore formation is driven by local unfolding of membrane-spanning β-strand regions and pre-insertion of a covalently bound palmitoyl into the target membrane. These results yield insights into the diversity of GSDM pores found in nature and the function of an ancient post-translational modification in enabling a programmed host cell death process.