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Structures reveal how SGLT inhibitors work.
Sun, Zejian; Cui, Wenhao; Chen, Lei.
Affiliation
  • Sun Z; State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China; Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China; Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, China.
  • Cui W; State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China.
  • Chen L; State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China; Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China; Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, China; National Biomedical Imaging Center, Peking University, Beijing, 100871, China. Electronic address: chenlei2016@pku.ed
Trends Pharmacol Sci ; 45(9): 760-763, 2024 Sep.
Article in En | MEDLINE | ID: mdl-38897851
ABSTRACT
Sodium glucose cotransporters (SGLTs) transport glucose against its concentration gradient by harnessing the electrochemical potential gradient of sodium ions. SGLT inhibitors are widely prescribed to treat diabetes and other conditions. Recent structural studies have uncovered how chemically diverse SGLT inhibitors bind and inhibit the transporter at the atomic level.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Sodium-Glucose Transport Proteins Limits: Animals / Humans Language: En Journal: Trends Pharmacol Sci Year: 2024 Document type: Article Affiliation country: China Country of publication: United kingdom
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Sodium-Glucose Transport Proteins Limits: Animals / Humans Language: En Journal: Trends Pharmacol Sci Year: 2024 Document type: Article Affiliation country: China Country of publication: United kingdom