Results 1 to 10 of about 4,054 (130)

Compromised mitochondrial fatty acid synthesis in transgenic mice results in defective protein lipoylation and energy disequilibrium. [PDF]

open access: yesPLoS One, 2012
A mouse model with compromised mitochondrial fatty acid synthesis has been engineered in order to assess the role of this pathway in mitochondrial function and overall health.
Smith S   +27 more
europepmc   +20 more sources

FDX1 regulates cellular protein lipoylation through direct binding to LIAS. [PDF]

open access: yesJ Biol Chem, 2023
AbstractFerredoxins are a family of iron-sulfur (Fe-S) cluster proteins that serve as essential electron donors in numerous cellular processes that are conserved through evolution. The promiscuous nature of ferredoxins as electron donors enables them to participate in many metabolic processes including steroid, heme, vitamin D and Fe-S cluster ...
Dreishpoon MB   +8 more
europepmc   +4 more sources

Protein lipoylation in mitochondria requires Fe-S cluster assembly factors NFU4 and NFU5. [PDF]

open access: yesPlant Physiol, 2022
Abstract Plants have evolutionarily conserved NifU (NFU)-domain proteins that are targeted to plastids or mitochondria. “Plastid-type” NFU1, NFU2, and NFU3 in Arabidopsis (Arabidopsis thaliana) play a role in iron–sulfur (Fe–S) cluster assembly in this organelle, whereas the type-II NFU4 and NFU5 proteins have not been subjected to ...
Przybyla-Toscano J   +7 more
europepmc   +9 more sources

Glycine decarboxylase maintains mitochondrial protein lipoylation to support tumor growth. [PDF]

open access: yesCell Metab, 2022
The folic acid cycle mediates the transfer of one-carbon (1C) units to support nucleotide biosynthesis. While the importance of serine as a mitochondrial and cytosolic donor of folate-mediated 1C units in cancer cells has been thoroughly investigated, a potential role of glycine oxidation remains unclear.
Mukha D   +10 more
europepmc   +3 more sources

Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease. [PDF]

open access: yesCurr Opin Chem Biol, 2018
Lipoylation is a rare, but highly conserved lysine posttranslational modification. To date, it is known to occur on only four multimeric metabolic enzymes in mammals, yet these proteins are staples in the core metabolic landscape. The dysregulation of these mitochondrial proteins is linked to a range of human metabolic disorders.
Rowland EA, Snowden CK, Cristea IM.
europepmc   +4 more sources

Protein lipoylation in cancer: metabolic reprogramming and therapeutic potential. [PDF]

open access: yesCell Death Discov
Abstract Protein lipoylation, a mitochondria-specific post-translational modification (PTM) evolutionarily conserved from bacteria to mammals, plays critical role in metabolic processes. In humans, four identified lipoylated proteins serve as essential components of key enzymes involved in glycolysis, the tricarboxylic acid (TCA) cycle, and ...
Li S   +12 more
europepmc   +3 more sources

Mitochondrial Protein Lipoylation and the 2-Oxoglutarate Dehydrogenase Complex Controls HIF1α Stability in Aerobic Conditions. [PDF]

open access: yesCell Metab, 2016
Hypoxia-inducible transcription factors (HIFs) control adaptation to low oxygen environments by activating genes involved in metabolism, angiogenesis, and redox homeostasis. The finding that HIFs are also regulated by small molecule metabolites highlights the need to understand the complexity of their cellular regulation.
Burr SP   +10 more
europepmc   +3 more sources

Engineered bacterial lipoate protein ligase A (lplA) restores lipoylation in cell models of lipoylation deficiency. [PDF]

open access: yesJ Biol Chem
Protein lipoylation, a vital lysine post-translational modification, plays a crucial role in the function of key mitochondrial tricarboxylic acid cycle enzymatic complexes. In eukaryotes, lipoyl post-translational modification synthesis occurs exclusively through de novo pathways, relying on lipoyl synthesis/transfer enzymes, dependent upon ...
Bick NR   +7 more
europepmc   +3 more sources

Chemoselective and laser cleavable probes for <i>in situ</i> protein lipoylation detection by laser desorption/ionization mass spectrometry. [PDF]

open access: yesChem Sci
Chemoselective probe is connected with gold nanoparticles modified with laser cleavable mass tags by click chemistry for in situ protein lipoylation detection by laser desorption/ionization mass spectrometry.
Du Q   +8 more
europepmc   +3 more sources

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