Publications by authors named "H L Bruce"

Steak samples were collected from the longissimus lumborum muscles of beef carcasses (Canada AA, n = 1505; Canada AAA, n = 1363) over a 3-year period. Steaks were aged for 14 d, and tenderness was determined by slice shear force (SSF). Metabolomic profiling of beef samples was performed using rapid evaporative ionization mass spectrometry (REIMS) (N = 2853).

View Article and Find Full Text PDF

Background: Chronic traumatic encephalopathy (CTE) is a neurodegenerative tauopathy more frequently found in deceased former football players. CTE has heterogeneous clinical presentations with multifactorial causes. Previous literature has shown substance use (alcohol/drug) can contribute to Alzheimer's disease and related tauopathies pathologically and clinically.

View Article and Find Full Text PDF

Tenderness is considered a crucial attribute of postmortem meat quality, directly influencing consumers' preferences and industrial economic benefits. The degradation of myofibrillar proteins by endogenous enzymes within muscle fibers is believed to be the most effective pathway for meat tenderization. After animals are slaughtered and exsanguinated, there is a significant accumulation of reactive oxygen species (ROS), and a dramatic depletion of adenosine triphosphate (ATP) in muscle, leading to inevitable cell death.

View Article and Find Full Text PDF

The evolution of flight in an early winged insect ancestral lineage is recognized as a key adaptation explaining the unparalleled success and diversification of insects. Subsequent transitions and modifications to flight machinery, including secondary reductions and losses, also play a central role in shaping the impacts of insects on broadscale geographic and ecological processes and patterns in the present and future. Given the importance of insect flight, there has been a centuries-long history of research and debate on the evolutionary origins and biological mechanisms of flight.

View Article and Find Full Text PDF

It has been shown previously that a set of three modifications-termed S1, Crystal Kappa, and elbow-act synergistically to improve the crystallizability of an antigen-binding fragment (Fab) framework. Here, we prepared a phage-displayed library and performed crystallization screenings to identify additional substitutions-located near the heavy-chain elbow region-which cooperate with the S1, Crystal Kappa, and elbow modifications to increase expression and improve crystallizability of the Fab framework even further. One substitution (K141Q) supports the signature Crystal Kappa-mediated Fab:Fab crystal lattice packing interaction.

View Article and Find Full Text PDF