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ProteomicsFirst comprehensive proteome analysis of lysine crotonylation in Streptococcus agalactiae, a pathogen causing meningoencephalitis in teleosts
In Homo sapiens, Streptococcus agalactiae is a common colonizer of the rectovaginal tract and a fundamental cause of neonatal and non-pregnant adults infectious diseases. It also causes infectious disease in fish which compromises food safety as well as possesses a zoonotic risk. Lysine crotonylatio...
ORGANISM(S): Enterococcus faecalis (Streptococcus faecalis) 
2021-12-30 | PXD026445 | Pride
Streptococcus agalactiae  crotonylation  virulence factors  proteomics 
ProteomicsSystematic Analysis of the Lysine Crotonylome and multiple PTM analysis (acetylation, succinylation and crotonylation) in Candida albicans
LC-MS/MS was used to carry out the analysis of the crotonylome in C. albicans (Candida albicans) comprehensively in our study. Generally, 5242 specific crotonylated sites of 1584 crotonylated proteins were detected among 9038 proteins in C. albicans. The crotonylome involved in the regulation of met...
ORGANISM(S): Candida albicans (Yeast) 
2021-01-08 | PXD018848 | Pride
C. albicans  crotonylome  histone  lysine crotonylation motif  ppi 
ProteomicsGlobal Proteomic Analysis of Lysine crotonylation in The Plant Pathogen Botrytis cinerea
Lysine crotonylation (Kcr), a recently discovered post-translational modification, plays a key role in the regulation of diverse cellular processes. Botrytis cinerea is a destructive necrotrophic fungal pathogen distributed worldwide with broad ranging hosts. However, the functions of Kcr are unknow...
ORGANISM(S): Caenorhabditis elegans 
2020-09-07 | PXD019358 | Pride
Lc-ms/ms Botrytis cinerea Lysine crotonylation 
ProteomicsQualitative Proteome-wide Analysis Reveal the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense C. Z. Tang et S. J. Cheng
Lysine crotonylation of histone proteins is a newly identified post-translational modification with diversified cellular functions. However, there’s few reports on lysine crotonylation of non-histone proteins in fruit plant cells. By using high-resolution LC-MS coupled with highly sensitive specific...
ORGANISM(S): Dendrobium huoshanense 
2021-11-29 | PXD028293 | Pride
Dendrobium huoshanense  lysine crotonylation  polysaccharide biosythesis 
ProteomicsGlobal involvement of lysine crotonylation in protein modification and transcription regulation in rice
Lysine crotonylation (Kcr) is a newly discovered post-translational modification (PTM) existing in mammals. A global crotonylome analysis was undertaken in rice (Oryza sativa L. japonica) using high accuracy nano-LC-MS/MS in combination with crotonylated peptide enrichment. A total of 1,265 lysine c...
ORGANISM(S): Oryza sativa (Rice) 
2018-09-20 | PXD010376 | Pride
Oryza sativa Post-translational Histone lysine crotonylation Crotonyl lysine 
ProteomicsCrotonylome profiling reveals extensive lysine crotonylation in common wheat
Histone lysine crotonylation (Kcr) is a newly discovered protein post-translational modification (PTM), which was detected from yeast to humans and is mainly related with active transcription. With the development of proteomics technologies, high abundance of non-histone proteins modified by Kcr was...
ORGANISM(S): Triticum aestivum (Wheat) 
2023-07-20 | PXD008483 | Pride
Triticum aestivum l.  post-translational modification  lysine crotonylation  proteomics  mass spectrometry 
ProteomicsLarge-Scale Analysis of Protein Crotonylation Reveals Its Diverse Functions in Pinellia ternate
We generated a global crotonylome analysis of the leaves in Pinellia ternata. We found 4509 crotonylated sites on 1757 proteins totally, and three specific amino acids surrounding crotonylation sites were identified in Pinellia ternata: KcrF, K***Y**Kcr and Kcr****R. Gene Ontology (GO) and KEGG pat...
ORGANISM(S): Homo sapiens (Human) Pinellia ternata 
2022-07-31 | PXD033142 | Pride
Post-translational modification Lysine crotonylation Crotonylome Pinellia ternata 
ProteomicsA proteomic analysis of lysine crotonylation in systemic lupus erythematosus patients
Posttranslational modification (PTM) refers to the process of the covalent processing of translated proteins, as well as the activities and functions of proteins, and it is involved in almost all cellular pathways and processes. Lysine crotonylation (Kcr) is a recently identified PTM and plays a key...
ORGANISM(S): Homo sapiens (Human) 
2023-03-10 | PXD012966 | Pride
Posttranslational modification Lysine crotonylation Lc-ms/ms 
ProteomicsLarge-Scale Analysis of Protein Crotonylation Reveals Its Diverse Functions in Pinellia ternate
We generated a global crotonylome analysis of the leaves in Pinellia ternata. We found 4509 crotonylated sites on 1757 proteins totally, and three specific amino acids surrounding crotonylation sites were identified in Pinellia ternata: KcrF, K***Y**Kcr and Kcr****R. Gene Ontology (GO) and KEGG pat...
ORGANISM(S): Pinellia ternata 
2022-04-13 | PXD033154 | Pride
Post-translational modification Lysine crotonylation Crotonylome Pinellia ternata 
ProteomicsCrotonylation versus acetylation in PaACL-silenced corollas in petunia
Protein acetylation and crotonylation are important post-translational modifications (PTMs) of lysine. In animal cells, histone lysines are crotonylated or acetylated depends on the relative intracellular concentrations of crotonyl-CoA and acetyl-CoA, and adding crotonate to cell cultures, or reduci...
ORGANISM(S): Petunia hybrid cultivar 
2022-10-12 | PXD023270 | Pride
Crotonylation Paacl Petunia  crotonylome Gene silencing Acetylation 
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