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Academic Journal

Activation of STING by targeting a pocket in the transmembrane domain.

  • Authors : Lu D; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, USA.; Shang G

Subjects: Membrane Proteins*/Membrane Proteins*/Membrane Proteins*/metabolism ; Nucleotides, Cyclic*/Nucleotides, Cyclic*/Nucleotides, Cyclic*/metabolism; Cell Cycle Proteins

  • Source: Nature [Nature] 2022 Apr; Vol. 604 (7906), pp. 557-562. Date of Electronic Publication: 2022 Apr 06.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 0410462 Publication Model: Print-Electronic Cited

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Academic Journal

Structural basis of STING binding with and phosphorylation by TBK1.

  • Authors : Zhang C; Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA.; Shang G

Subjects: Cryoelectron Microscopy*; Membrane Proteins/Membrane Proteins/Membrane Proteins/*chemistry ; Membrane Proteins/Membrane Proteins/Membrane Proteins/*ultrastructure

  • Source: Nature [Nature] 2019 Mar; Vol. 567 (7748), pp. 394-398. Date of Electronic Publication: 2019 Mar 06.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 0410462 Publication Model: Print-Electronic Cited

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Academic Journal

Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP.

  • Authors : Shang G; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX, USA.; Zhang C

Subjects: Chickens* ; Cryoelectron Microscopy*; Membrane Proteins/Membrane Proteins/Membrane Proteins/*metabolism

  • Source: Nature [Nature] 2019 Mar; Vol. 567 (7748), pp. 389-393. Date of Electronic Publication: 2019 Mar 06.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 0410462 Publication Model: Print-Electronic Cited

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