Structural basis for the binding of DNP and purine nucleotides onto UCP1

Uncoupling protein 1 (UCP1) conducts protons through the inner mitochondrial membrane to uncouple mitochondrial respiration from ATP production, thereby converting the electrochemical gradient of protons into heat 1 , 2 . The activity of UCP1 is activated by endogenous fatty acids and synthetic smal...

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Vydáno v:	Nature (London) Ročník 620; číslo 7972; s. 226 - 231
Hlavní autoři:	Kang, Yunlu, Chen, Lei
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	London Nature Publishing Group UK 03.08.2023 Nature Publishing Group
Témata:	101/28 2,4-Dinitrophenol 2,4-Dinitrophenol - chemistry 2,4-Dinitrophenol - metabolism 631/45/612/1237 631/535/1258/1259 82/80 82/83 Adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism ATP Binding sites Cell Membrane - metabolism Cytosol - metabolism Electrochemistry Electron transport Fatty acids Fatty Acids - metabolism Humanities and Social Sciences Humans Lipids multidisciplinary Nucleotides Permeability Protein Conformation Proteins Protons Respiration Science Science (multidisciplinary) Uncoupling protein 1 Uncoupling Protein 1 - chemistry Uncoupling Protein 1 - metabolism
ISSN:	0028-0836, 1476-4687, 1476-4687
On-line přístup:	Získat plný text
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