Large-Scale Assessment of Bioinformatics Tools for Lysine Succinylation Sites [PDF]
Cells, 2019 Lysine succinylation is a form of posttranslational modification of the proteins that play an essential functional role in every aspect of cell metabolism in both prokaryotes and eukaryotes.
Md. Mehedi Hasan +2 more
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Lysine succinylation precisely controls normal erythropoiesis
HaematologicaLysine succinylation (Ksu) has recently emerged as a protein modification that regulates diverse functions in various biological processes. However, the systemically and precise role of lysine succinylation in erythropoiesis remains to be fully ...
Bin Hu +19 more
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Succinylation: A Functional Nexus Between Metabolic Reprogramming and Epigenetic Modifications in Cancer [PDF]
MoleculesMetabolic reprogramming and epigenetic remodeling are critical features of tumorigenesis. The process of metabolic reprogramming causes metabolites like Succinyl-CoA to accumulate.
Dan Liu +5 more
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The Mystery of Extramitochondrial Proteins Lysine Succinylation. [PDF]
Int J Mol Sci, 2021 Lysine succinylation is a post-translational modification which alters protein function in both physiological and pathological processes. Mindful that it requires succinyl-CoA, a metabolite formed within the mitochondrial matrix that cannot permeate the inner mitochondrial membrane, the question arises as to how there can be succinylation of proteins ...
Chinopoulos C.
europepmc +4 more sources
The emerging role of lysine succinylation in ovarian aging. [PDF]
Reprod Biol Endocrinol, 2023 Abstract Background Ovarian aging is a process of decline in its reserve leading to ovary dysfunction and even reduced health quality in offspring. However, aging-related molecular pathways in the ovary remain obscure. Lysine succinylation (Ksuc), a newly post-translational modification (PTM), has been found to be broadly conserved in both ...
Le M +9 more
europepmc +4 more sources
Comprehensive analysis of the lysine acetylome in Aeromonas hydrophila reveals cross-talk between lysine acetylation and succinylation in LuxS [PDF]
Emerging Microbes and Infections, 2019 Lysine acetylation and succinylation are both prevalent protein post-translational modifications (PTMs) in bacteria species, whereas the effect of the cross-talk between both PTMs on bacterial biological function remains largely unknown.
Lina Sun +8 more
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Succinylation: novel molecular mechanisms and prospects for targeted therapy in liver diseases [PDF]
Frontiers in Molecular BiosciencesSuccinylation is a novel post-translational modification involving the attachment of a negatively charged succinyl group to lysine residues, which fundamentally alters the structure and function of substrate proteins.
Jie Zhou +4 more
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Impact of Lysine Succinylation on the Biology of Fungi. [PDF]
Curr Issues Mol BiolPost-translational modifications (PTMs) play a crucial role in protein functionality and the control of various cellular processes and secondary metabolites (SMs) in fungi. Lysine succinylation (Ksuc) is an emerging protein PTM characterized by the addition of a succinyl group to a lysine residue, which induces substantial alteration in the chemical ...
Adejor J +5 more
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The enzyme activity of mitochondrial trifunctional protein is not altered by lysine acetylation or lysine succinylation. [PDF]
PLoS One, 2021 Mitochondrial trifunctional protein (TFP) is a membrane-associated heterotetramer that catalyzes three of the four reactions needed to chain-shorten long-chain fatty acids inside the mitochondria. TFP is known to be heavily modified by acetyllysine and succinyllysine post-translational modifications (PTMs), many of which are targeted for reversal by ...
Zhang Y, Goetzman E.
europepmc +5 more sources
Lysine succinylation and SIRT5 couple nutritional status to glutamine catabolism. [PDF]
Mol Cell Oncol, 2020 The metabolic microenvironment of tumors is characterized by fluctuating and limited nutrient availability. To survive these conditions, cancer cell-intrinsic mechanisms sense and signal nutritional status. We describe how glutaminase (GLS) is destabilized by lysine succinylation and stabilized by the NAD+-dependent desuccinylase sirtuin 5 (SIRT5 ...
Lukey MJ, Greene KS, Cerione RA.
europepmc +5 more sources