XRD1 Highlights
- XRD1 Highlights
- C1–C4 alcohol–cavitand complexes
- Cuprate Superconductor
- Jack Bean Urease
- XRD1 Sample Changer
- Carbonic Anhydrase
- PDI8CN2
- Human Legumain
- Structure of Human NAPE-PLD
- beta-Chitin in Squid Pen
- Enhanced Green Fluorescent Protein
- Multitarget drug design strategy
- Hydrogen-bonded Organic Pigments
- Selectivity of CNG channels
- Polycyclic Aromatic Hydrocarbons
- Cisplatin Encapsulation within the Ferritin Nanocage
- Crystal structure of the earthworm toxin
- Chemistry at the protein–mineral interface in L-ferritin
- Porous N-doped graphene
- Sliding of the human DNA clamp PCNA
- S1′ Pocket of Thermolysin
- microbial NLP cytolysins
- Human ubiquitin
- Photosynthesis
- Nanoparticles
- Anode Materials
- Stone Materials
- Sensor humidity
- Xe shell
- OSC
- Peptide nanotubes
- Amyloid aggregates
- Perovskites optimization
- Hydrocarbons
- CO2 separation
- Flexibility
- All Pages
Page 9 of 36
Structure of Human NAPE-PLD: Regulation of Bioactive Lipids Biosynthesis by Bile Acids
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NAPE-PLD (N-acyl phosphatidylethanolamine phospholipase D) is a key membrane-bound enzyme involved in the biosynthesis of endocannabinoids and other bioactive lipid signaling amides. Highly detailed structural findings, obtained on XRD1, provide the structural basisto understand how this protein is tightly connected to mammal’s neurotransmission and a variety of pathophysiological processes, including gastrointestinal motility, synaptic plasticity, appetite and mood. |
Retieve Article
Structure of human NAPE-PLD: regulation of fatty-acid ethanolamide biosynthesis by bile acids; Magotti P, Bauer I, Igarashi M, Babagoli M, Marotta R, Piomelli D, Garau G, Structure 23, 3 (2015) doi:10.1016/j.str.2014.12.018 |
Last Updated on Monday, 22 May 2023 15:31