User contributions
From Proteopedia
(Newest | Oldest) View (Newer 50) (Older 50) (20 | 50 | 100 | 250 | 500)
- 18:21, 30 November 2025 (hist) (diff) STING Polymer Structure Reveals Mechanisms for Activation, Hyperactivation, and Inhibition (Bi3323) (top)
- 17:50, 30 November 2025 (hist) (diff) Image:4F5W.pse (uploaded a new version of "Image:4F5W.pse") (top)
- 17:50, 30 November 2025 (hist) (diff) Image:4F5W 2.pse (top)
- 17:37, 30 November 2025 (hist) (diff) STING Polymer Structure Reveals Mechanisms for Activation, Hyperactivation, and Inhibition (Bi3323) (I made mistake with loading PDB)
- 17:35, 30 November 2025 (hist) (diff) STING Polymer Structure Reveals Mechanisms for Activation, Hyperactivation, and Inhibition (Bi3323) (Revised the page to give clearer explanations of STING’s function, its role in disease, why this structure is relevant, and the key structural features of the apo form.)
- 17:28, 30 November 2025 (hist) (diff) STING Polymer Structure Reveals Mechanisms for Activation, Hyperactivation, and Inhibition (Bi3323) (The STING protein plays a central role in the innate immune response by sensing cytosolic DNA through the second messenger 2’3’-cGAMP. The structure represented by PDB: 4F5W captures STING in its apo)
- 17:21, 30 November 2025 (hist) (diff) Image:4F5W.pse (uploaded a new version of "Image:4F5W.pse": The 4F5W structure captures STING in its calm, inactive state. In this form, the protein sits as an open dimer, with the two arms of the molecule gently spread apart. Because no ligand is bound, STING isn’)
- 17:20, 30 November 2025 (hist) (diff) Image:4F5W.pse (The 4F5W structure captures STING in its calm, inactive state. In this form, the protein sits as an open dimer, with the two arms of the molecule gently spread apart. Because no ligand is bound, STING isn’t under any pressure to change shape—so it sta)
(Newest | Oldest) View (Newer 50) (Older 50) (20 | 50 | 100 | 250 | 500)
