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ProteomicsSynechocystis 6803 LC-MS/MS - Systematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins
Identification of the membrane and the soluble proteins in Synechocystis sp. PCC6803
ORGANISM(S): Synechocystis sp. PCC 6803 
2015-01-16 | PXD001246 | Pride
Soluble Synechocystis Membrane 
ProteomicsEvaluation of the potential risk of Easy-nLC 1200 in phosphoproteomics
Liquid chromatography-mass spectrometry (LC-MS) is a major tool for large scale qualitative and/or quantitative analysis of protein phosphorylation in cells or tissues. Performance of LC is pivotal for the success of phosphoprotemics in both sensitivity and reproducibility. Here we report that the w...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Homo sapiens (Human) 
2023-03-10 | PXD034396 | Pride
Phosphoproteomics Lc-ms Phosphorylation 
MetabolomicsNQO1 protects obese mice through improvements in glucose and lipid metabolism.
Chronic nutrient excess leads to metabolic disorders and insulin resistance. Activation of stress-responsive pathways via Nrf2 activation contributes to energy metabolism regulation. Here, inducible activation of Nrf2 in mice and transgenesis of the Nrf2 target, NQO1, conferred protection from diet-...
2024-05-23 | MTBLS2085 | MetaboLights
OtherSystematically Ranking the Tightness of Membrane Association for Peripheral Membrane Proteins.
Data from ProteomeXchange, PXD ID: PXD001246. File: GLY_M11_20140408.mzml. Published as part of Mol Cell Proteomics. 2014 Dec 13 . From the Abstract: {{i}} Large scale quantitative evaluation of the tightness of membrane association for non-transmembrane proteins is important for identifying true p...
ORGANISM(S): Synechococcus_phage_p60_uid14628, Synechococcus_phage_syn5_uid19763, Synechococcus_phage_syn9_uid17541, Synechococcus_phage_s_pm2_uid15223, Synechococcus_phage_s_rsm4_uid39923, Synechocystis_pcc_6803 
GPM32320007112 | GPMDB
Resource Reanalysis 
ProteomicsProfiling of spreading- coupled protein tyrosine phosphorylation
Protein tyrosine phosphorylation is an important mechanism that regulates cytoskeleton reorganization and cell spreading of migratory cells. A number of cytoskeletal proteins are known to be tyrosine phosphorylated (pY) in different cellular processes. However, the profile of pY proteins during diff...
ORGANISM(S): Homo sapiens (Human) 
2016-09-28 | PXD004340 | Pride
Spreading Fibronectin Ecv304 
ProteomicsSynechocystis spatial proteome LC-MS/MS
We treated a unicellular photosynthetic model cyanobacterium, Synechocystis sp. PCC 6803, with five different types of abiotic stresses including nitrogen starvation, iron deficiency, cold, heat, and darkness, and systematically identified proteins showing stress-induced differential expression and/...
ORGANISM(S): Synechocystis sp. PCC 6803 
2023-03-20 | PXD035771 | Pride
Synechocystis total membrane soluble lc-ms/ms 
ProteomicsSynechocystis sp. PCC 6803 WT and Δhik33 (sll0698) proteomic research, proteomic data of normal culture conditions.
In this study, by using shotgun LC-MS/MS approach with the Tandem Mass Tag (TMTs) isobaric labelling technique we show that proteins in photosystem, inorganic carbon uptake and CO2 fixation systems are significantly changed in Δhik33 cells compared with WT cells.This is the normal culture condition ...
ORGANISM(S): Synechocystis sp. PCC 6803 
2017-05-19 | PXD005085 | Pride
Synechocystis sp. pcc 6803  hik33 mutant  lc-msms 
ProteomicsProximity labeling facilitates defining neighborhood proteome of photosystem II oxygen evolution complex in a model cyanobacterium
APEX2-based proximity labeling coupled with mass spectrometry have great potential for spatiotemporal identification of proteins proximal to a protein complex of interest. Using this approach it is feasible to define the proteome neighborhood of important protein complexes in a popular photosyntheti...
ORGANISM(S): Synechocystis sp. PCC 6803 
2023-02-17 | PXD036113 | Pride
Proximity labeling Synechocystis Apex Proteomics Cyanobacteria 
ProteomicsCoordination of cyanobacterial nitrate assimilation and photosynthesis by a novel PsbO-interacting protein PirN
Nitrogen assimilation relies on photosynthetically-produced energy and reducing equivalents. Here, we identify a small protein, PsbO-interacting regulator of nitrate assimilation (PirN), as a key coordinator of photosynthesis and nitrate assimilation in Synechocystis sp. PCC 6803 (Synechocystis). Pi...
ORGANISM(S): Synechocystis sp. PCC 6803 substr. GT-T 
2026-06-08 | PXD066894 | Pride
Cyanobacteria Photosynthesis Psbo Nitrate assimilation Pirn 
ProteomicsParallel comparison of mutant proteomes with altered carbon metabolism reveals Hik8 regulates PII phosphorylation and the basal level glycogen accumulation in a cyanobacterium
To understand the specificity and the cross-talk of such regulations, we simultaneously and quantitatively compared the proteomes of the gene knockout mutants for the regulators. A number of proteins showing differential expression in one or more mutants were identified, including four proteins that...
ORGANISM(S): Synechocystis sp. PCC 6803 
2023-07-20 | PXD035898 | Pride
Carbon metabolism Cyanobacteria Synechocystis Proteomics Glycogen 
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