Results 31 to 40 of about 3,788 (176)

Proteomic analysis reveals a novel function of the kinase Sat4p in Saccharomyces cerevisiae mitochondria. [PDF]

open access: yesPLoS ONE, 2014
The Saccharomyces cerevisiae kinase Sat4p has been originally identified as a protein involved in salt tolerance and stabilization of plasma membrane transporters, implicating a cytoplasmic localization. Our study revealed an additional mitochondrial (mt)
Uta Gey   +4 more
doaj   +1 more source

Mitochondrial fatty acid synthesis coordinates oxidative metabolism in mammalian mitochondria

open access: yeseLife, 2020
Cells harbor two systems for fatty acid synthesis, one in the cytoplasm (catalyzed by fatty acid synthase, FASN) and one in the mitochondria (mtFAS).
Sara M Nowinski   +18 more
doaj   +1 more source

LipoSVM: Prediction of Lysine lipoylation in Proteins based on the Support Vector Machine [PDF]

open access: yesCurrent Genomics, 2019
Background:Lysine lipoylation which is a rare and highly conserved post-translational modification of proteins has been considered as one of the most important processes in the biological field. To obtain a comprehensive understanding of regulatory mechanism of lysine lipoylation, the key is to identify lysine lipoylated sites. The experimental methods
Wu, Meiqi   +6 more
openaire   +3 more sources

A Lipoylated Metabolic Protein Released by Staphylococcus aureus Suppresses Macrophage Activation [PDF]

open access: yesCell Host & Microbe, 2017
The virulence factors of pathogenic microbes often have single functions that permit immune suppression. However, a proportion possess multiple activities and are considered moonlighting proteins. By examining secreted virulence factors of Staphylococcus aureus, we determine that the bacterial lipoic acid synthetase LipA suppresses macrophage ...
James P, Grayczyk   +3 more
openaire   +2 more sources

Pathogenic variants in GCSH encoding the moonlighting H-protein cause combined Nonketotic Hyperglycinemia and Lipoate Deficiency [PDF]

open access: yes, 2023
Maintaining protein lipoylation is vital for cell metabolism. The H-protein encoded by GCSH has a dual role in protein lipoylation required for bioenergetic enzymes including pyruvate dehydrogenase and 2-ketoglutarate dehydrogenase, and in the one-carbon
Koutsoukos, Stefanos   +31 more
core   +2 more sources

Ilipo-pseaac: Identification of lipoylation sites using statistical moments and general pseaac

open access: yes, 2022
Lysine Lipoylation is a protective and conserved Post Translational Modification (PTM) in proteomics research like prokaryotes and eukaryotes. It is connected with many biological processes and closely linked with many metabolic diseases.
Gillani, Durdana Qaiser   +5 more
core   +1 more source

Ferroptosis inducers enhanced cuproptosis induced by copper ionophores in primary liver cancer

open access: yesJournal of Experimental & Clinical Cancer Research, 2023
Introduction Cuproptosis and ferroptosis are the two newly defined metal-related regulated cell death. However, the crosstalk between cuproptosis and ferroptosis is obscure.
Weikai Wang   +7 more
doaj   +1 more source

Sirtuin Lipoamidase Activity Is Conserved in Bacteria as a Regulator of Metabolic Enzyme Complexes

open access: yesmBio, 2017
Lipoic acid is an essential metabolic cofactor added as a posttranslational modification on several multimeric enzyme complexes. These protein complexes, evolutionarily conserved from bacteria to humans, are core regulators of cellular metabolism.
Elizabeth A. Rowland   +5 more
doaj   +1 more source

[32] Assay for protein lipoylation reaction

open access: yesThe Journal of biological chemistry, 1995
Publisher Summary This chapter discusses the assay for protein lipoylation reaction. Lipoate attaches to the ɛ -amino group of the specific lysine residue of the proteins via an amide linkage. The lipoyllysine residue functions as a carrier of intermediates of the reactions and reducing equivalents between the active sites of the components of the ...
Kazuko Fujiwara   +2 more
openaire   +2 more sources

Redox‐dependent lipoylation of mitochondrial proteins in Plasmodium falciparum [PDF]

open access: yesMolecular Microbiology, 2014
SummaryLipoate scavenging from the human host is essential for malaria parasite survival. Scavenged lipoate is covalently attached to three parasite proteins: the H‐protein and the E2 subunits of branched chain amino acid dehydrogenase (BCDH) and α‐ketoglutarate dehydrogenase (KDH). We show mitochondrial localization for the E2 subunits of BCDH and KDH,
Gustavo A, Afanador   +6 more
openaire   +2 more sources

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