Results 31 to 40 of about 3,037 (136)

Proteome-wide analyses reveal diverse functions of protein acetylation and succinylation modifications in fast growing stolons of bermudagrass (Cynodon dactylon L.)

BMC Plant Biology, 2022
Background Bermudagrass (Cynodon dactylon L.) is an important warm-season turfgrass species with well-developed stolons, which lay the foundation for the fast propagation of bermudagrass plants through asexual clonal growth.
Bing Zhang, Zhuoting Chen, Qixue Sun, Jianxiu Liu   +3 more
doaj   +1 more source

Coenzyme A binding sites induce proximal acylation across protein families

Scientific Reports, 2023
Lysine Nɛ-acylations, such as acetylation or succinylation, are post-translational modifications that regulate protein function. In mitochondria, lysine acylation is predominantly non-enzymatic, and only a specific subset of the proteome is acylated ...
Chris Carrico, Andrew Cruz, Marius Walter, Jesse Meyer, Cameron Wehrfritz, Samah Shah, Lei Wei, Birgit Schilling, Eric Verdin   +8 more
doaj   +1 more source

Unlocking the Hidden Potential of Cancer Therapy Targeting Lysine Succinylation. [PDF]

J Cancer
Lysine succinylation is an emerging post-translational modification of proteins. It involves the addition of the succinyl group to lysine residues of target proteins through both enzymatic and non-enzymatic pathways. This modification can alter the structure of the target protein, which, in turn, impacts protein activity and function and is involved in
Zheng Z, Xiao P, Kuang J, Wang Z, Wang X, Huang D, Guo Y, Zhou L, Yang Y, Ding S, Zheng C, Wang Y, Fu S, Deng X.   +13 more
europepmc   +2 more sources

Lysine Succinylation and Lysine Malonylation in Histones

Molecular & Cellular Proteomics, 2012
Histone protein post-translational modifications (PTMs) are significant for gene expression and DNA repair. Here we report the identification and validation of a new type of PTM in histones, lysine succinylation. The identified lysine succinylated histone peptides were verified by MS/MS of synthetic peptides, HPLC co-elution, and isotopic labeling.
Zhongyu, Xie, Junbiao, Dai, Lunzhi, Dai, Minjia, Tan, Zhongyi, Cheng, Yeming, Wu, Jef D, Boeke, Yingming, Zhao   +7 more
openaire   +2 more sources

Lysine-222 succinylation reduces lysosomal degradation of lactate dehydrogenase a and is increased in gastric cancer

Journal of Experimental & Clinical Cancer Research, 2020
Background Lysine succinylation is an emerging posttranslational modification that has garnered increased attention recently, but its role in gastric cancer (GC) remains underexplored.
Xiang Li, Chen Zhang, Ting Zhao, Zhongping Su, Mengjing Li, Jiancheng Hu, Jianfei Wen, Jiajia Shen, Chao Wang, Jinshun Pan, Xianmin Mu, Tao Ling, Yingchang Li, Hao Wen, Xiaoren Zhang, Qiang You   +15 more
doaj   +1 more source

SuccSite: Incorporating Amino Acid Composition and Informative k-spaced Amino Acid Pairs to Identify Protein Succinylation Sites

Genomics, Proteomics & Bioinformatics, 2020
Protein succinylation is a biochemical reaction in which a succinyl group (-CO-CH2-CH2-CO-) is attached to the lysine residue of a protein molecule. Lysine succinylation plays important regulatory roles in living cells. However, studies in this field are
Hui-Ju Kao, Van-Nui Nguyen, Kai-Yao Huang, Wen-Chi Chang, Tzong-Yi Lee   +4 more
doaj   +1 more source

Protocol for the preparation of site-specific succinylated histone mimics to investigate the impact on nucleosome dynamics

STAR Protocols, 2021
Summary: Lysine succinylation is a recently discovered posttranslational modification that plays critical roles in metabolism, epigenetic signaling, and human diseases.
Yihang Jing, Zheng Liu, Xiang David Li
doaj   +1 more source

Identification of lysine succinylation as a new post-translational modification [PDF]

Nature Chemical Biology, 2010
Of the 20 ribosomally coded amino acid residues, lysine is the most frequently post-translationally modified, which has important functional and regulatory consequences. Here we report the identification and verification of a previously unreported form of protein post-translational modification (PTM): lysine succinylation.
Zhihong, Zhang, Minjia, Tan, Zhongyu, Xie, Lunzhi, Dai, Yue, Chen, Yingming, Zhao   +5 more
openaire   +2 more sources

Acetylome and Succinylome Profiling of Edwardsiella tarda Reveals Key Roles of Both Lysine Acylations in Bacterial Antibiotic Resistance

Antibiotics, 2022
The antibiotic resistance of Edwardsiella tarda is becoming increasingly prevalent, and thus novel antimicrobial strategies are being sought. Lysine acylation has been demonstrated to play an important role in bacterial physiological functions, while its
Yuying Fu, Lishan Zhang, Huanhuan Song, Junyan Liao, Li Lin, Wenjia Jiang, Xiaoyun Wu, Guibin Wang   +7 more
doaj   +1 more source

Succinyl-proteome profiling of Dendrobium officinale, an important traditional Chinese orchid herb, revealed involvement of succinylation in the glycolysis pathway

BMC Genomics, 2017
Background Lysine succinylation is a ubiquitous and important protein post-translational modification in various eukaryotic and prokaryotic cells. However, its functions in Dendrobium officinale, an important traditional Chinese orchid herb with high ...
Shangguo Feng, Kaili Jiao, Hong Guo, Mengyi Jiang, Juan Hao, Huizhong Wang, Chenjia Shen   +6 more
doaj   +1 more source