Results 21 to 30 of about 3,349,944 (177)

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

Plant 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, Maclean AE, Franceschetti M, Liebsch D, Vignols F, Keech O, Rouhier N, Balk J.   +7 more
europepmc   +10 more sources

Pan-cancer analysis of the upstream regulator FDX1 in cuproptosis [PDF]

Discover Oncology
The global incidence and mortality of cancer continue to rise rapidly, and cancer remains one of the most severe challenges in the field of public health.
Yan Xue, Qiong Tang, Wu Liu, Baoqing Zhao, Wanwan Jia   +4 more
doaj   +2 more sources

Role of ferredoxin 1 (FDX1) in cancer and its therapeutic potential [PDF]

Cancer Pathogenesis and Therapy
Ferredoxin 1 (FDX1) is a small iron-sulfur (Fe–S) cluster protein localized to the mitochondria. It functions as an electron carrier in diverse metabolic pathways and is critically involved in the regulation of protein lipoylation Accumulating evidence ...
Fen He, Hongyan Zhao, Ruixin Gao, Maoyou Lu, Siqi Wang, Yu Chen, Lijun Peng, Jiliang Xia   +7 more
doaj   +2 more sources

Ferredoxins: master regulators in mitochondrial redox homeostasis and programmed cell death [PDF]

Redox Biology
Ferredoxins (FDXs) are evolutionarily conserved iron-sulfur (Fe–S) proteins that serve as master regulators of mitochondrial redox homeostasis, governing critical processes including electron transfer, energy metabolism, Fe–S cluster biogenesis, and ...
Yajuan Lu, Yunyi Wu, Chen Yang, Yi Zhou, Xueying Ren, Haoran Li, Hangqi Huang, Feifan Pan, Aoli Deng, Yi Lu, Jiayi Yang, Xiangmin Tong, Yanchun Li, Jing Du   +13 more
doaj   +2 more sources

Cuproptosis key gene FDX1 is a prognostic biomarker and associated with immune infiltration in glioma

Frontiers in Medicine, 2022
Recent studies have found that the protein encoded by the FDX1 gene is involved in mediating Cuproptosis as a regulator of protein lipoylation and related to immune response process of tumors.
Hanwen Lu, Hanwen Lu, Liwei Zhou, Liwei Zhou, Bingchang Zhang, Bingchang Zhang, Yuanyuan Xie, Yuanyuan Xie, Huiyin Yang, Huiyin Yang, Zhanxiang Wang, Zhanxiang Wang, Zhanxiang Wang   +12 more
doaj   +1 more source

Chemical Probes Reveal Sirt2’s New Function as a Robust “Eraser” of Lysine Lipoylation

, 2019
Lysine lipoylation, a highly conserved lysine post-translational modification, plays a critical role in regulating cell metabolism. The catalytic activity of a number of vital metabolic proteins, such as pyruvate dehydrogenase (PDH), depends on lysine ...
Hongyan Sun (327879), Rui Wang (52434), Yusheng Xie (2186521), Wei Xu (28953), Yingxue Li (705766), Jingyu Li (324429), Lanfang Chen (3355439), Shao Q. Yao (1525546), Liang Zhang (41392), Quan Hao (67204), Jigang Wang (730916)   +10 more
core   +6 more sources

A unique lipoylation system in the Archaea [PDF]

The FEBS Journal, 2009
Members of the 2-oxoacid dehydrogenase multienzyme complex family play a key role in the pathways of central metabolism. Post-translational lipoylation of the dihydrolipoyl acyltransferase component of these complexes is essential for their activity, the lipoyllysine moiety performing the transfer of substrates and intermediates between the different ...
Mareike G, Posner, Abhishek, Upadhyay, Stefan, Bagby, David W, Hough, Michael J, Danson   +4 more
openaire   +2 more sources

Loss of the mitochondrial SAM transporter reveals a lipoylation-dependent metabolic vulnerability in the postnatal heart. [PDF]

Sci Adv
The neonatal heart experiences rapid metabolic growth after birth to meet increasing energetic and biosynthetic demands. How mitochondrial cofactor availability limits this transition remains unclear.
Rumyantseva A, Tippetts TS, Wilhalm A, Carter W, Moedas M, Rosenberger FA, Moore D, Végvári Á, Hinze Y, Muellner-Wong L, Alsina D, Wibom R, Winston R, Mathews TP, Lund LH, Andersson DC, Pironti G, Wedell A, DeBerardinis RJ, Freyer C, Wredenberg A.   +20 more
europepmc   +2 more sources

Evidence for two protein‐lipoylation activities in Escherichia coli [PDF]

FEBS Letters, 1991
The lipoate acyltransferase subunits of the 2‐oxo acid dehydrogenase complexes are post‐translationally modified with one or more covalently‐bound lipoyl cofactors. Two distinct lipoate‐protein ligase activities, LPL‐A and LPL‐B, have been detected in E. coli by their ability to modify purified lipoyl apo‐domains of the bacterial pyruvate dehydrogenase
Brookfield, Dawn E., Green, Jeffrey, Ali, Sohail T., Machado, Rosane S., Guest, John R.   +4 more
openaire   +2 more sources

Lipoylation Mechanism of P. Falciparum Mitochondrial Proteins [PDF]

Biophysical Journal, 2015
Lipoate is an essential cofactor for the aerobic metabolism in oxidative decarboxylation reactions of 2-oxoacid complexes. Malaria parasite survival is highly dependent on scavenging this essential cofactor from the human host. Scavenged lipoate is subsequently attached to the α-ketoglutarate dehydrogenase (KDH), the branched chain α-ketoacid ...
Guerra, Alfredo J., Afandor, Gustavo A., Swift, Russell P., Prigge, Sean T.   +3 more
openaire   +1 more source