Results 271 to 280 of about 168,834 (385)

Hyperpolarized NMR study of the impact of pyruvate dehydrogenase kinase inhibition on the pyruvate dehydrogenase and TCA flux in type 2 diabetic rat muscle. [PDF]

open access: yesPflugers Arch, 2021
Park JM   +9 more
europepmc   +1 more source

Pharmacological manipulation of liver fibrosis progression using novel HDAC6 inhibitors

open access: yesThe FEBS Journal, EarlyView.
Chronic liver injury can lead to severe conditions such as cirrhosis and liver cancer. Unfortunately, there are no effective treatments to halt or reverse liver fibrosis, which makes new therapeutic strategies essential. This study focuses on the role of histone deacetylases (HDACs) in liver fibrosis, particularly HDAC6.
Maria Teresa Borrello   +25 more
wiley   +1 more source

Y12C mutation disrupts IMPDH cytoophidia and alters cancer metabolism

open access: yesThe FEBS Journal, EarlyView.
IMPDH, the rate‐limiting enzyme for de novo GTP synthesis, can form polymers and cytoophidia to enhance activity by reducing GTP inhibition. In this study, a Y12C mutation in IMPDH2 was introduced via ABEmax base‐editing in human cancer cell lines to disrupt IMPDH polymerisation.
Chia‐Chun Chang   +7 more
wiley   +1 more source

Targeting pyruvate dehydrogenase kinase 1 overcomes EGFR C797S mutation-driven osimertinib resistance in non-small cell lung cancer. [PDF]

open access: yesExp Mol Med
Park W   +12 more
europepmc   +1 more source

Allosteric modulation of protein kinase A in individuals affected by NLPD‐PKA, a neurodegenerative disease in which the PRKAR1B L50R variant is expressed

open access: yesThe FEBS Journal, EarlyView.
In healthy neurons, Protein kinase A (PKA) forms a tetrameric holoenzyme enabling precise allosteric regulation. We characterized a novel neurodegenerative disease, neuronal loss, and parkinsonism driven by PRKAR1B mutation (NLPD‐PKA), demonstrating disrupted holoenzyme assembly, reduced cooperativity, and increased catalytic subunit nuclear ...
Tal Benjamin‐Zukerman   +13 more
wiley   +1 more source

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