Publications by authors named "C A Goulding"
(Mtb) is the causative agent of tuberculosis, the world's deadliest infectious disease. Mtb uses a variety of mechanisms to evade the human host's defenses and survive intracellularly. Mtb's oxidative stress response enables Mtb to survive within activated macrophages, an environment with reactive oxygen species and low pH.
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- Advanced glycation end-products (AGE) are harmful protein modifications linked to serious health issues like neurodegenerative diseases, heart disease, and diabetes, caused by toxic byproducts of glucose metabolism.
- Research reveals that AGE crosslinking activates a specific antibacterial enzyme in the bacteria Enterobacter cloacae, which is linked through a unique interaction between two amino acids.
- The study highlights that glycation can stabilize protein structures, especially in environments where traditional stabilizing methods (like disulfide bonds) are not effective, suggesting broader implications for protein engineering.
The tuberculosis (TB) emergency has been a pressing health threat for decades. With the emergence of drug-resistant TB and complications from the COVID-19 pandemic, the TB health crisis is more serious than ever. Mycobacterium tuberculosis (Mtb), the causative agent of TB, requires iron for its survival.
View Article and Find Full Text PDFPlants are sessile organisms that constantly adapt to their changing environment. The root is exposed to numerous environmental signals ranging from nutrients and water to microbial molecular patterns. These signals can trigger distinct responses including the rapid increase or decrease of root growth.
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- Mycobacterium tuberculosis (Mtb) is a major health threat, especially with rising drug-resistant strains, making it crucial to find new treatments targeting its iron acquisition mechanisms.
- This study investigates the roles of two periplasmic binding proteins, FecB and FecB2, in Mtb's ability to acquire iron, finding that FecB specifically binds to the Mtb siderophore and has a crucial interaction with the iron acquisition system.
- The researchers determined the 3D structures of FecB and FecB2, revealing different binding features, and identified key interactions that suggest FecB is important for both siderophore and heme uptake in Mtb.