Results 171 to 180 of about 4,831 (203)

Proteome-wide identification of lysine succinylation in thermophilic and mesophilic bacteria

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2017
Lysine succinylation, one of post-translational acylations conserved from eukaryotes to bacteria, plays regulatory roles in various cellular processes. However, much remains unknown about the general and specific characteristics of lysine succinylation among bacteria, and about its functions different from those of other acylations.
Hiroki, Okanishi, Kwang, Kim, Kenji, Fukui, Takato, Yano, Seiki, Kuramitsu, Ryoji, Masui   +5 more
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Regulation of urea cycle by reversible high stoichiometry lysine succinylation

2022
AbstractThe post-translational modification, lysine succinylation is implicated in the regulation of various metabolic pathways. However, its biological relevance remains uncertain due to methodological difficulties in determining high-impact succinylation sites.
Ran Zhang, Xueshu Xie, Chris Carrico, Jesse G. Meyer, Lei Wei, Joanna Bons, Jacob Rose, Rebeccah Riley, Ryan Kwok, Prasanna A. Kumaar, Wenjuan He, Yuya Nishida, Xiaojing Liu, Jason W. Locasale, Birgit Schilling, Eric Verdin   +15 more
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Global Proteomic Analysis of Lysine Succinylation in Zebrafish (Danio rerio)

Journal of Proteome Research, 2019
Lysine succinylation (Ksu) is a novel identified post-translational modification that is conserved from prokaryotes to eukaryotes. As a kind of acylation, Ksu was reported to have different functions than other acylations at lysine residues. However, recent studies on Ksu have mainly focused on plants and bacteria.
Yan Gao, Hyojin Lee, Oh Kwang Kwon, Minjia Tan, Ki-Tae Kim, Sangkyu Lee   +5 more
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Proteomic analysis of lysine succinylation of the human pathogen Histoplasma capsulatum

Journal of Proteomics, 2017
Histoplasma capsulatum, the causative agent of histoplasmosis (also called "Darling's disease"), can affect both immunocompetent and immunocompromised hosts. Post-translational protein modification by lysine succinylation (Ksuc) is a frequent occurrence in eukaryote and prokaryote.
Longxiang, Xie, Juan, Li, Wanyan, Deng, Zhaoxiao, Yu, Wenjie, Fang, Min, Chen, Wanqing, Liao, Jianping, Xie, Weihua, Pan   +8 more
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Vibrio alginolyticus PEPCK Mediates Florfenicol Resistance through Lysine Succinylation Modification

Journal of Proteome Research
Protein succinylation modification is a common post-translational modification (PTM) that plays an important role in bacterial metabolic regulation. In this study, quantitative analysis was conducted on the succinylated proteome of wild-type and florfenicol-resistant Vibrio alginolyticus to investigate the mechanism of succinylation regulating ...
Huanying Pang, Weijie Zhang, Xuelian Lin, Fuyuan Zeng, Xing Xiao, Zhiqing Wei, Shi Wang, Jichang Jian, Na Wang, Wanxin Li   +9 more
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Microbiota-derived succinate promotes enterohaemorrhagic Escherichia coli virulence via lysine succinylation

Nature Microbiology
Succinate upregulates enterohaemorrhagic Escherichia coli (EHEC) virulence. Lysine succinylation, a post-translational modification, regulates cellular function in eukaryotes but is less characterized in bacteria. We hypothesized that lysine succinylation regulates EHEC virulence.
Linxing Li, Yutao Liu, Dan Liu, Jing Wang, Min Wang, Binbin Xiang, Jingliang Qin, Ting Yao, Wanwu Li, Pan Wu, Qian Wang, Jianji Zhang, Yanli Xu, Miaomiao Liu, Yanling Wang, Guozhen Ma, Ruiying Liu, Xiaoya Li, Zimeng Huai, Yu Huang, Han Guo, Bin Yang, Lu Feng, Di Huang, Kai Zhang, Lei Wang, Bin Liu   +26 more
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A succinyl lysine-based photo-cross-linking peptide probe for Sirtuin 5

Org. Biomol. Chem., 2014
A succinylation-specific photo-cross-linking peptide probe has been developed for the NAD+-dependent hydrolase Sirtuin 5.
Karunakaran A, Kalesh, Edward W, Tate
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Prediction of Lysine Succinylation Sites by SVR and Weighted Down-sampling

Proceedings of the 2019 International Conference on Robotics Systems and Vehicle Technology, 2019
Succinylation is a post-translational modification (PTM), which changes the chemical structure of lysine and results in significant changes in the structure and function of proteins. Lysine succinylation plays an important role in coordinating various biological processes, and it isalso associated with some diseases.
Kai Wang, Ping Liang, Jun Sheng Hu
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An isotopic method for determining chemically reactive lysine based on succinylation

Journal of the Science of Food and Agriculture, 1984
AbstractA method is described for the routine succinylation of proteins using [14C]succinic anhydride as a means of measuring free ϵ‐amino groups. Maximal succinylation was achieved using 6M guanidine hydrochloride as protein solvent and an 80‐fold molar excess of succinic anhydride relative to total lysine residues. Treatment with hydroxylamine (pH 13,
Trevor R. Anderson, George V. Quicke
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The Synthesis of Poly-L-Lysine-Succinyl-Nadp: An Analogue for Nadp/H

The International Journal of Artificial Organs, 1980
Poly-L-lysine-succinyl-NADP, an analogue for nicotinamide adenine dinucleotide phosphate (NADP/H), has been synthesized by linking NADP/H to poly-L-lysine hydrobromide. This analogue (PL-SNP) was assayed with N, N dimethylaniline (DMA) in the presence of hepatic microsomal oxidase. A regeneration system of G-6-p and G-6-PD was used for reducing the PL-
R A, Wills, W M, Southard, S S, Sofer
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