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TranscriptomicsChIP-chip study aimed at the identification of the repertoire of FOXC2 binding sites affected by the loss of FOXC2 phosphorylation in primary human lymphatic endothelial cells (LECs)
Chromatin immunoprecipitation microarray (ChIP-chip) study using anti-Myc (9E10) antibodies and primary human lymphatic endothelial cells (LECs) transduced with recombinant adenoviruses expressing wild type or phosphorylation-deficient Myc-tagged FOXC2.
ORGANISM(S): Homo sapiens 
2013-07-13 | E-MTAB-596 | biostudies-arrayexpress
ModelsPandey2018-reversible transition between quiescence and proliferation
Cells switch between quiescence and proliferation states for maintaining tissue homeostasis and regeneration. At the restriction point (R-point), cells become irreversibly committed to the completion of the cell cycle independent of mitogen. The mechanism involving hyper-phosphorylation of retinobla...
2024-09-02 | BIOMD0000000954 | BioModels
ProteomicsSequential enrichment of phosphorylation on reversibly oxidized proteoforms – part 2
Post-translational modifications (PTMs) are necessary for the regulation of critical processes including metabolism, signaling, and overall homeostasis. While proteins PTMs have been largely investigated independently in bottom-up proteomics methodologies, examination into how different PTMs interac...
ORGANISM(S): Chlamydomonas reinhardtii 
2018-04-23 | PXD008371 | Pride
Chlamydomonas reinhardtii Phosphorylation Cross-talk Redox proteomics Redox regulation 
ProteomicsSequential enrichment of phosphorylation on reversibly oxidized proteoforms – part 1
Post-translational modifications (PTMs) are necessary for the regulation of critical processes including metabolism, signaling, and overall homeostasis. While proteins PTMs have been largely investigated independently in bottom-up proteomics methodologies, examination into how different PTMs interac...
ORGANISM(S): Chlamydomonas reinhardtii 
2018-04-23 | PXD008370 | Pride
Chlamydomonas reinhardtii Phosphorylation Cross-talk Redox proteomics Redox regulation 
ProteomicsReversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function
The fundamental importance of the 26S proteasome in health and disease suggests that its function must be finely controlled, and yet our knowledge about proteasome regulation remains limited. Posttranslational modifications, especially phosphorylation, of proteasome subunits have been shown to impac...
ORGANISM(S): Homo Sapiens 
2019-12-08 | PXD016643 |
UnknownReversible phosphorylation of the 26S proteasome.
Not available
S-EPMC5359188 | biostudies-literature
ProteomicsQuantitative proteomic and phosphoproteomic analysis of the liver of the Xizang plateau frog
Protein abundance changes and reversible protein phosphorylation (RPP) play important roles in regulating hypometabolism but have never been documented in overwintering frogs at high altitudes. To test the hypothesis that protein abundance and protein phosphorylation change in response to winter hib...
ORGANISM(S): Nanorana parkeri 
2024-05-22 | PXD042165 | Pride
Metabolism Reversible protein phosphorylation Phosphoproteomic Nanorana parkeri Proteomic Hibernation 
ProteomicsIdentification of differential phosphoproteins reveled complex responses of soybean to phosphate starvation through reversible protein phosphorylation
Phosphorus (P) deficiency is considered as a major constraint on crop production. Although a set of adaptative strategies are extensively suggested in soybean (Glycine max) to phosphate(Pi) deprivation, molecular mechanisms underlying reversible protein phosphorylation in soybean responses to P defi...
ORGANISM(S): Glycine max 
2021-06-13 | PXD025771 | Pride
Soybean roots Phosphorylation Phosphate starvation Differential phosphoproteins 
TranscriptomicsGlobal impact of protein arginine phosphorylation on the physiology of Bacillus subtilis
Reversible protein phosphorylation is an important and ubiquitous protein modification in all living cells. We report that protein arginine phosphorylation plays a physiological significant role for the regulation of protein activity. We detected 121 arginine phospho-sites for 87 proteins in the Gra...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 
2012-03-31 | E-GEOD-31249 | biostudies-arrayexpress
ProteomicsRapid and reversible knockdown of endogenously tagged endosomal proteins via an optimized HaloPROTAC degrader
Combining pharmacologic and genetic tools to induce post-translational protein knockdown is an emerging approach to probe biology and validate potential drug targets. A powerful strategy involves expression of a protein of interest fused to an exogenous tag, allowing tag-directed chemical degraders ...
ORGANISM(S): Homo sapiens (Human) 
2019-11-13 | PXD012828 | Pride
Haloprotac Vps34 Degradation 
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