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ProteomicsIdentification of SENP3 and SENP5 target proteins by endogenous SUMO2/3 IP-MS
Ribosome biogenesis is a complex and energy demanding process requiring tight coordination with cell growth and proliferation. Impairment of ribosome biogenesis activates a well-defined cell-cycle checkpoint that primarily relies on the activation of p53 signaling. However, there is mounting evidenc...
ORGANISM(S): Homo sapiens (Human) 
2023-10-28 | PXD037793 | Pride
Sumo Human Senp Lc-ms/ms 
ProteomicsIdentification of SENP5 target proteins by endogenous SUMO2/3 IP-MS
Ribosome biogenesis is a complex and energy demanding process requiring tight coordination with cell growth and proliferation. Impairment of ribosome biogenesis activates a well-defined cell-cycle checkpoint that primarily relies on the activation of p53 signaling. However, there is mounting evidenc...
ORGANISM(S): Homo sapiens (Human) 
2023-10-28 | PXD037796 | Pride
Sumo Human Senp Lc-ms/ms 
ProteomicsWhole cell proteome of U2OS cells or Saos-2 cells depleted for SENP3
Ribosome biogenesis is a complex and energy demanding process requiring tight coordination with cell growth and proliferation. Impairment of ribosome biogenesis activates a well-defined cell-cycle checkpoint that primarily relies on the activation of p53 signaling. However, there is mounting evidenc...
ORGANISM(S): Homo sapiens (Human) 
2023-10-28 | PXD037800 | Pride
Sumo Human Senp Lc-ms/ms 
TranscriptomicsTranscription analysis of E. coli processed at persistent and decreasing glucose limitation in a fed-batch cultivation
A time series of whole-genome transcription profiling of E. coli K-12 W3110 was performed to study the dynamic physiological response of E. coli K-12 W3110 to limited carbon conditions. cDNA from eight time intervals after glucose limitation, representing different stages of glucose depletion, along...
ORGANISM(S): Escherichia coli W3110 
2010-05-19 | E-GEOD-10307 | biostudies-arrayexpress
ProteomicsIdentification of UTP14A interactors by endogenous UTP14A IP-MS
Ribosome biogenesis is a complex and energy demanding process requiring tight coordination with cell growth and proliferation. Impairment of ribosome biogenesis activates a well-defined cell-cycle checkpoint that primarily relies on the activation of p53 signaling. However, there is mounting evidenc...
ORGANISM(S): Homo sapiens (Human) 
2023-10-28 | PXD043556 | Pride
Sumo Human Senp Lc-ms/ms 
ProteomicsProteomes of chromatin fractions derived from SU-DHL-5 cells
SU-DHL-5 cells display limited expression of the SUMO isopeptidase SENP6. In this experiment, the chromatin associated fraction of SU-DHL-5 cells was analysed by mass spectrometry. SU-DHL-5 cells were either stably transfected with an empty vector or with a SENP6 expression construct. Changes in pro...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027355 | Pride
Su-dhl-5 cells (b-cell lymphoma) 
ProteomicsThe coupling of transcriptome and proteome adaptation during development and heat stress response of tomato pollen
Pollen development is central for plant reproduction and is assisted by changes of the transcriptome and the proteome. At the same time, pollen is largely heat sensitive, particularly at early developmental stages. To define the changes during development and the response of different stages to elev...
ORGANISM(S): Solanum lycopersicum 
2015-05-15 | PXD008762 | Pride
Pollen development Proteomics Heat stress Transcriptomics 
UnknownInside a Shell-Organometallic Catalysis Inside Encapsulin Nanoreactors.
Not available
S-EPMC8596989 | biostudies-literature
TranscriptomicsGene expression data from Wilms tumor samples
Wilms tumor (nephroblastoma) is a pediatric kidney tumor that arises from renal progenitor cells. Since the blastemal type is associated with adverse prognosis, we characterized such Wilms tumors by exome and transcriptome analysis. We detected novel, recurrent somatic mutations affecting the SIX1/2...
ORGANISM(S): Homo sapiens 
2015-02-18 | E-GEOD-53224 | biostudies-arrayexpress
ProteomicsIdentification of novel natural substrates of fibroblast activation protein by differential degradomics and proteomics (TAILS dataset)
Fibroblast Activation Protein (FAP) is a cell-surface transmembrane-anchored anchored dimeric protease. This unique constitutively active serine protease has both dipeptidyl aminopeptidase and endopeptidase activities, and can hydrolyse post-proline bonds. FAP expression is very low in adult organs,...
ORGANISM(S): Mus musculus (Mouse) 
2018-12-19 | PXD004757 | Pride
Seprase Proteolysis 
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