Publications by authors named "D Alamo"
One hundred and forty bitches and their offspring (689 puppies) were involved in this study. The influence of different maternal features such as age, breed (brachycephalic/non-brachycephalic), previous births (primiparous/multiparous), health status (complete/incomplete) and litter size over the type of cesarean sections (scheduled/emergency), the neonatal survival, and the incidence of congenital malformations were also examined. Scheduled cesareans were predominant (104/140), of which 90 % were brachycephalic breeds and females were mostly between 2 and 4 years old (54.
View Article and Find Full Text PDFThe Amino Acid-Polyamine-Organocation (APC) transporter GadC contributes to the survival of pathogenic bacteria under extreme acid stress by exchanging extracellular glutamate for intracellular γ-aminobutyric acid (GABA). Its structure, determined in an inward-facing conformation at alkaline pH, consists of the canonical LeuT-fold with a conserved five-helix inverted repeat, thereby resembling functionally divergent transporters such as the serotonin transporter SERT and the glucose-sodium symporter SGLT1. However, despite this structural similarity, it is unclear if the conformational dynamics of antiporters such as GadC follow the blueprint of these or other LeuT-fold transporters.
View Article and Find Full Text PDFArticle Synopsis
- LeuT-fold transporters play a crucial role in moving hydrophilic and charged substances like amino acids and sugars across cell membranes, with extensive research on the LeuT transporter providing valuable insights.
- The review compares different models and mechanisms of transport for LeuT and its relatives, noting both similarities and differences in their function and energy dynamics.
- It underscores the conservation of structural features in the LeuT fold while also pointing out gaps in understanding that limit the application of current research to practical knowledge about membrane protein transport.
Article Synopsis
- Conformational changes are crucial for the function of many proteins, and their study often requires a comprehensive structural biology approach.
- The new method, ConfChangeMover (CCM), integrated into the Rosetta modeling suite, effectively models these changes using limited experimental data.
- Benchmark tests showed CCM outperformed existing Rosetta methods, demonstrating its ability to model various conformational changes and integrate diverse experimental data for better understanding of protein dynamics.
Article Synopsis
- Membrane proteins, like transporters and receptors, undergo conformational changes critical for their functions, which has complicated traditional structure predictions.
- Recent advancements in AlphaFold2 (AF2) have shown promise in modeling these proteins in multiple conformations, although AF2 was originally designed for static structures.
- By adjusting the input for the AF2 algorithm, researchers successfully generated multiple accurate conformations of diverse transporters and receptors, indicating a need for future AI tools to better predict a range of functional protein states.