Chloroquine and amodiaquine enhance AMPK phosphorylation and improve mitochondrial fragmentation in diabetic tubulopathy
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2045-2322
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Chloroquine and amodiaquine enhance AMPK phosphorylation and improve mitochondrial fragmentation in diabetic tubulopathy ; volume:8 ; number:1 ; day:8 ; month:6 ; year:2018 ; pages:1-13 ; date:12.2018
Scientific reports ; 8, Heft 1 (8.6.2018), 1-13, 12.2018
- Creator
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Jeong, Hye Yun
- Contributor
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Kang, Jun Mo
Jun, Hak Hoon
Kim, Dong-Jin
Park, Seon Hwa
Sung, Min Ji
Heo, Jin Hyung
Yang, Dong Ho
Lee, Sang Ho
Lee, So-Young
SpringerLink (Online service)
- DOI
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10.1038/s41598-018-26858-8
- URN
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urn:nbn:de:101:1-2018081020384804054998
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:29 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Jeong, Hye Yun
- Kang, Jun Mo
- Jun, Hak Hoon
- Kim, Dong-Jin
- Park, Seon Hwa
- Sung, Min Ji
- Heo, Jin Hyung
- Yang, Dong Ho
- Lee, Sang Ho
- Lee, So-Young
- SpringerLink (Online service)
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Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation
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AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules
FAK tyrosine phosphorylation is regulated by AMPK and controls metabolism in human skeletal muscle
Phosphorylation of INF2 by AMPK promotes mitochondrial fission and oncogenic function in endometrial cancer
Cellular energy stress induces AMPK-mediated regulation of glioblastoma cell proliferation by PIKE-A phosphorylation
Inhibitors of oxidative phosphorylation modulate astrocyte inflammatory responses through AMPK-dependent Ptgs2 mRNA stabilization
Interaction between rifampicin, amodiaquine and artemether in mice infected with chloroquine resistant Plasmodium berghei
Polymorphism in the Plasmodium falciparum chloroquine-resistance transporter protein links verapamil enhancement of chloroquine sensitivity with the clinical efficacy of amodiaquine
Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation
Phosphorylation of PLIN3 by AMPK promotes dispersion of lipid droplets during starvation
Post-translational regulation of lipogenesis via AMPK-dependent phosphorylation of insulin-induced gene
Phosphorylation of PHF2 by AMPK releases the repressive H3K9me2 and inhibits cancer metastasis
Fixed dose artesunate amodiaquine – a phase IIb, randomized comparative trial with non-fixed artesunate amodiaquine
AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules
FAK tyrosine phosphorylation is regulated by AMPK and controls metabolism in human skeletal muscle
Phosphorylation of INF2 by AMPK promotes mitochondrial fission and oncogenic function in endometrial cancer
Cellular energy stress induces AMPK-mediated regulation of glioblastoma cell proliferation by PIKE-A phosphorylation
Inhibitors of oxidative phosphorylation modulate astrocyte inflammatory responses through AMPK-dependent Ptgs2 mRNA stabilization
Interaction between rifampicin, amodiaquine and artemether in mice infected with chloroquine resistant Plasmodium berghei
Polymorphism in the Plasmodium falciparum chloroquine-resistance transporter protein links verapamil enhancement of chloroquine sensitivity with the clinical efficacy of amodiaquine
Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation
Phosphorylation of PLIN3 by AMPK promotes dispersion of lipid droplets during starvation
Post-translational regulation of lipogenesis via AMPK-dependent phosphorylation of insulin-induced gene
Phosphorylation of PHF2 by AMPK releases the repressive H3K9me2 and inhibits cancer metastasis
Fixed dose artesunate amodiaquine – a phase IIb, randomized comparative trial with non-fixed artesunate amodiaquine
AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules
FAK tyrosine phosphorylation is regulated by AMPK and controls metabolism in human skeletal muscle
Phosphorylation of INF2 by AMPK promotes mitochondrial fission and oncogenic function in endometrial cancer
Cellular energy stress induces AMPK-mediated regulation of glioblastoma cell proliferation by PIKE-A phosphorylation