Results 141 to 150 of about 3,788 (176)

Copper Homeostasis and Cuproptosis in Neurological Disorders. [PDF]

Drug Des Devel Ther
Liu W, Xue Y, Cao C, Yang L, Zhang L.
europepmc   +1 more source

METTL3-mediated m6A modification of FDX1 confers resistance to cuproptosis and promotes hepatocellular carcinoma progression. [PDF]

Commun Biol
Jiang Q, Peng C, Mao W, Yu Z, Feng Y, Li Y, Zhu J, Zhao J, Liao D, Sun T.   +9 more
europepmc   +1 more source

Mycobacterium tuberculosis assembles a unique hexameric E2p core of the pyruvate dehydrogenase complex. [PDF]

J Biol Chem
Hsu HC, Bonnet I, Bryk R, Li H.
europepmc   +1 more source

Aging at the Crossroads of Cuproptosis and Ferroptosis: From Molecular Pathways to Age-Related Pathologies and Therapeutic Perspectives. [PDF]

Int J Mol Sci
Gromadzka G, Tarnacka B, Cieślik M.
europepmc   +1 more source

Quantitative Site-Specific Chemoproteomic Profiling of Protein Lipoylation

Journal of the American Chemical Society, 2022
Protein lipoylation is an evolutionarily conserved post-translational modification from prokaryotes to eukaryotes. Lipoylation is implicated with several human diseases, including metabolic disorders, cancer, and Alzheimer's disease. While individual lipoylated proteins have been biochemically studied, a strategy for globally quantifying lipoylation ...
Weidi Xiao, Yuan Liu, Chu Wang
exaly   +5 more sources

Activation and competition of lipoylation of H protein and its hydrolysis in a reaction cascade catalyzed by the multifunctional enzyme lipoate–protein ligase A

Biotechnology and Bioengineering, 2020
AbstractProtein lipoylation is essential for the function of many key enzymes but barely studied kinetically. Here, the two‐step reaction cascade of H protein lipoylation catalyzed by the multifunctional enzyme lipoate–protein ligase A (LplA) was quantitatively and differentially studied. We discovered new phenomena and unusual kinetics of the cascade:
Xinyi Zhang, Jinglei Nie, Jie Ren
exaly   +4 more sources

Poldip2 is an oxygen-sensitive protein that controls PDH and αKGDH lipoylation and activation to support metabolic adaptation in hypoxia and cancer [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2018
Significance The present work establishes that the addition of the prosthetic group lipoic acid to catabolic enzymes is a dynamically regulated posttranslational modification that increases metabolic plasticity under hypoxia and in cancer cells.
Felipe Paredes, Bernard Lassegue, Samantha M Yeligar   +2 more
exaly   +4 more sources