Publications by authors named "G Schnapp"
Article Synopsis
- Ceramides are important sphingolipids that play a crucial role in managing cellular metabolism, and six specific enzymes (CerS) are responsible for their synthesis.
- C16 ceramide, linked to obesity and insulin resistance, has CerS6 as a potential drug target due to its specific action in these conditions.
- New research using cryo-electron microscopy reveals how CerS6 works, showing that it uses a unique reaction mechanism and interacts with substances like the mycotoxin fumonisin B1, paving the way for future drug development.
Protons taken hostage: Dynamic H-bond networks of the pH-sensing GPR68.
Comput Struct Biotechnol J
September 2023
Proton-sensing G Protein Coupled Receptors (GPCRs) sense changes in the extracellular pH to effect cell signaling for cellular homeostasis. They tend to be overexpressed in solid tumors associated with acidic extracellular pH, and are of direct interest as drug targets. How proton-sensing GPCRs sense extracellular acidification and activate upon protonation change is important to understand, because it may guide the design of therapeutics.
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- PHT1 is a histidine/oligopeptide transporter that plays a crucial role in immune responses by interacting with the adaptor protein TASL, leading to type I interferon production.
- Chronic activation of this pathway is linked to systemic lupus erythematosus (SLE), highlighting the importance of understanding the PHT1-TASL interaction for developing treatments for autoimmune diseases.
- The study presents the Cryo-EM structure of PHT1 and suggests a model for the PHT1-TASL complex, where the first 16 residues of TASL form a helix that interacts with PHT1, providing insights into their functional relationship in immune signaling.
Background: Airway inflammation in chronic inflammatory lung diseases (e.g. bronchiectasis) is partly mediated by neutrophil-derived serine protease (NSP)/antiprotease imbalance.
View Article and Find Full Text PDFNeuromedin U receptor 2 (NMU2), an emerging attractive target for treating obesity, has shown the capability in reducing food intake and regulating energy metabolism when activated. However, drug development of NMU2 was deferred partially due to the lack of structural information. Here, we present the cryo-electron microscopy (cryo-EM) structure of NMU2 bound to the endogenous agonist NmU-25 and G at 3.
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