Results 41 to 50 of about 3,037 (136)

Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways [PDF]

open access: yesMolecular & Cellular Proteomics, 2021
Lysine acylations are reversible and ubiquitous post-translational modifications that play critical roles in regulating multiple cellular processes. In the current study, highly abundant and dynamic acetylation, besides succinylation, was uncovered in a soil bacterium, Streptomyces coelicolor.
Yujiao Yang   +8 more
openaire   +2 more sources

Large-scale analysis of protein crotonylation reveals its diverse functions in Pinellia ternata

open access: yesBMC Plant Biology, 2022
Background Pinellia ternata is an important traditional medicine in China, and its growth is regulated by the transcriptome or proteome. Lysine crotonylation, a newly identified and important type of posttranslational modification, plays a key role in ...
Weiwei Guo   +4 more
doaj   +1 more source

Quantitative succinyl-proteome profiling of Chinese hickory (Carya cathayensis) during the grafting process

open access: yesBMC Plant Biology, 2019
Background Chinese hickory (Carya cathayensis) is a popular nut plant having high economic value. Grafting is applied to accelerate the transition from vegetative phase to reproductive phase.
Huwei Yuan   +8 more
doaj   +1 more source

Lysine Succinylation Contributes to Aflatoxin Production and Pathogenicity in Aspergillus flavus. [PDF]

open access: yesMol Cell Proteomics, 2018
Aspergillus flavus (A. flavus) is a ubiquitous saprophytic and pathogenic fungus that produces the aflatoxin carcinogen, and A. flavus can have tremendous economic and health impacts worldwide. Increasing evidence demonstrates that lysine succinylation plays an important regulatory role in metabolic processes in both bacterial and human cells. However,
Ren S   +9 more
europepmc   +3 more sources

Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation

open access: yesMolecular & Cellular Proteomics, 2015
Protein acetylation is a well-studied regulatory mechanism for several cellular processes, ranging from gene expression to metabolism. Recent discoveries of new post-translational modifications, including malonylation, succinylation, and glutarylation, have expanded our understanding of the types of modifications found on proteins.
Matthew D, Hirschey, Yingming, Zhao
openaire   +2 more sources

Quantitative Analysis of the Proteome and the Succinylome in the Thyroid Tissue of High-Fat Diet-Induced Hypothyroxinemia in Rats

open access: yesInternational Journal of Endocrinology, 2020
Hypothyroidism is a common disease, and its molecular mechanism still needs further investigation. Lysine succinylation is found to be involved in various metabolic processes associated with hypothyroidism.
Baoxiang Hu   +9 more
doaj   +1 more source

Changes in the Acetylome and Succinylome of Bacillus subtilis in Response to Carbon Source. [PDF]

open access: yesPLoS ONE, 2015
Lysine residues can be post-translationally modified by various acyl modifications in bacteria and eukarya. Here, we showed that two major acyl modifications, acetylation and succinylation, were changed in response to the carbon source in the Gram ...
Saori Kosono   +6 more
doaj   +1 more source

Characterization and Identification of Lysine Succinylation Sites based on Deep Learning Method. [PDF]

open access: yesSci Rep, 2019
AbstractSuccinylation is a type of protein post-translational modification (PTM), which can play important roles in a variety of cellular processes. Due to an increasing number of site-specific succinylated peptides obtained from high-throughput mass spectrometry (MS), various tools have been developed for computationally identifying succinylated sites
Huang KY, Hsu JB, Lee TY.
europepmc   +4 more sources

Identification of Lysine Succinylation Substrates and the Succinylation Regulatory Enzyme CobB in Escherichia coli

open access: yesMolecular & Cellular Proteomics, 2013
Lysine succinylation is a newly identified protein post-translational modification pathway present in both prokaryotic and eukaryotic cells. However, succinylation substrates and regulatory enzyme(s) remain largely unknown, hindering the biological study of this modification.
Gozde, Colak   +11 more
openaire   +2 more sources

KAT2A Deficiency Suppresses Lung Cancer Progression by Downregulating MYC Through Decreasing MYC Succinylation. [PDF]

open access: yesCancer Sci
ABSTRACT Succinylation has been shown to promote lung cancer development, but its mechanism remains incompletely understood. KAT2A, a succinyltransferase, acts as an oncogene in multiple cancers, but its role in mediating lung cancer progression is unclear.
Li J   +7 more
europepmc   +2 more sources

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