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TranscriptomicsExpression data from hESCs expressing RB7LP or T121
We used microarray analysis to study the expression differences between controls and hESCs expressing RB7LP for 3 days, and controls and hESCs expressing T121 for 3 days. RB7LP is the large pocket fragment of the retinoblastoma protein (RB) fused to GFP, in which seven phosphorylation sites for Cdk ...
ORGANISM(S): Homo sapiens 
2012-06-29 | GSE29783 | GEO
TranscriptomicsExpression data from hESCs expressing RB7LP or T121
We used microarray analysis to study the expression differences between controls and hESCs expressing RB7LP for 3 days, and controls and hESCs expressing T121 for 3 days. RB7LP is the large pocket fragment of the retinoblastoma protein (RB) fused to GFP, in which seven phosphorylation sites for Cdk ...
ORGANISM(S): Homo sapiens 
2012-06-28 | E-GEOD-29783 | biostudies-arrayexpress
ProteomicsComprehensive analysis of proteomic landscape remodeling during carcinogenesis
We have performed a comprehensive analysis of how oncogenic transformation induced by v-Src kinase remodels the proteomic landscape of human breast epithelial (MCF10A) cells. We characterised the proteome of untransformed cells to a depth of ~14,000 proteins, spanning a wide dynamic range of express...
ORGANISM(S): Homo sapiens (Human) 
2018-04-12 | PXD009270 | Pride
Epithelial Src kinase Mcf10a Human breast Half-life 
ProteomicsA quantitative spatial proteomics analysis of proteome turnover in human cells
Measuring the properties of endogenous cell proteins, such as expression level, subcellular localization and turnover rates, on a whole proteome level remains a major challenge in the post-genome era. Quantitative methods for measuring mRNA expression do not reliably predict corresponding protein le...
ORGANISM(S): Homo sapiens (Human) 
2015-12-01 | PXD003258 | Pride
Hela Subcellular Silac 
ProteomicsGlobal proteomics analysis reveals a role for histone variant H3.3 in the response to starvation
Periodic starvation of animals induces large shifts in metabolism, but may also influence many other cellular systems and can lead to adaption to prolonged starvation conditions. To date, there is limited understanding of how starvation affects gene expression, particularly at the protein level. Her...
ORGANISM(S): Caenorhabditis elegans 
2015-06-17 | PXD001723 | Pride
C. elegans Starvation Histone 
ProteomicsHuman Plasma from non-Hispanic White and African American Sepsis Survivors and Non-Survivors with Primary Intra-Abdominal Infection LC-MS/MS
This study examined global proteomic changes in blood plasma from non-Hispanic White and African American sepsis patients with primary intra-abdominal infection using LC-MS/MS on a Q-Exactive HF. Proteins were quantified in the LC-MS/MS experiments using Tandem Mass Tags 16-plex (TMTpro).
ORGANISM(S): Homo sapiens (Human) 
2022-09-13 | PXD030476 | Pride
Human Sepsis Tmt Plasma Lc-ms/ms 
GenomicsHomo sapiens
Expression data from hESCs expressing RB7LP or T121
PRJNA141057 | ENA
OtherCharacterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics.
Data from ProteomeXchange, PXD ID: PXD001220. File: PT1541S1F02.mzml. Published as part of Mol Cell Proteomics. 2013 Dec;12(12):3851-73 . From the Abstract: {{i}} Proteins form a diverse array of complexes that mediate cellular function and regulation. A largely unexplored feature of such protein c...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
GPM32310002912 | GPMDB
Resource Reanalysis 
ProteomicsProteomic analysis of the cell cycle of procylic form Trypanosoma brucei
We describe a single-step centrifugal elutriation method to produce synchronous G1-phase procyclic trypanosomes at a scale amenable for proteomic analysis of the cell cycle. Using ten-plex tandem mass tag technology, we quantified 5,325 proteins across the cell cycle in this parasite, providing a us...
ORGANISM(S): Trypanosoma brucei 
2018-03-21 | PXD008741 | Pride
Procyclic Tmt Cell cycle Trypanosoma brucei Proteomics 
ProteomicsGlobal Subcellular Characterization of Protein Degradation Using Quantitative Proteomics
Protein degradation provides an important regulatory mechanism used to control cell cycle progression and many other cellular pathways. To comprehensively analyze the spatial control of protein degradation in U2OS osteosarcoma cells, we have combined drug treatment and SILAC-based quantitative mass ...
ORGANISM(S): Homo sapiens (Human) 
2015-11-27 | PXD003239 | Pride
Cytosolic U2os Cytoskeletal Prr11 Osteosarcoma cells Nuclear Membrane 
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