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ProteomicsAnalysis of the ubiquitinated peptides using the yeast Rpt2-normal, G2A and G2delta strains
Ubiquitinated peptides (KGG peptides) purified from the yeast strains with or without mutation on the N-myristoylation site of the proteasome Rpt2 subunit were analyzed by an LTQ-Orbitrap Velos. The MS data was analyzed by the Progenesis LC-MS software.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-08-25 | PXD002274 | Pride
Yeast Proteasome Ubiquitin Lc-ms/ms 
ProteomicsIdentification of Glycosylphosphatidylinositol Anchored Proteins and ω-sites Using TiO2-Based Affinity Purification
Glycosylphosphatidylinositol anchored proteins (GPI-APs) in the outer leaflet of the membrane microdomains, commonly referred to as lipid rafts, play important roles in many biological processes. To enable large-scale site-specific analysis of GPI anchoring, we developed a method for identification ...
ORGANISM(S): Homo sapiens (Human) 
2016-05-27 | PXD003105 | Pride
Gpi anchor 
ProteomicsProteomics data of mouse skeletal muscles (hypergravity exposure)
This project is “Medical proteome analysis of osteoporosis- and bone mass-related proteins using the Kibo Japanese Experiment Module of International Space Station (ISS)”. Applying proteomic technologies, this research aims to identify proteins involved in space flight-induced osteopenia as well as ...
ORGANISM(S): Mus Musculus (mouse) 
2020-02-20 | PXD017240 | JPOST Repository
TranscriptomicsExpression profiling of prostate cell lines by miRNA array
Prostate cancer (PCa) is the most common malignant carcinoma that develops in men in Western countries. Up to 30% of patients continue to suffer from disease progression following radical prostatectomy. Therefore, better prognostic markers and molecular targets for cancer treatment are needed. Micro...
ORGANISM(S): Homo sapiens 
2013-09-01 | E-GEOD-40026 | biostudies-arrayexpress
ProteomicsProteomic analysis using BRG1-phosphorylation mutants
Proteins extracted from stable clones expressing wild-type, phosphorylation-mimic (brg1-S1452D), or non-phosphorylatable BRG1 (brg1-S1452A) were trypsin-digested and analyzed by Q Exactive Quadrupole-Orbitrap LC-MS.
ORGANISM(S): Homo Sapiens (human) 
2021-11-24 | PXD022681 | JPOST Repository
ProteomicsMS analysis of phosphopeptides enriched from BRG1-phospho mutants
Phosphopeptides enriched from stable clones expressing wild-type, phosphorylation-mimic (brg1-S1452D), or non-phosphorylatable BRG1 (brg1-S1452A) were analyzed by Q Exactive Quadrupole-Orbitrap LC-MS.
ORGANISM(S): Homo Sapiens (human) 
2021-11-24 | PXD022680 | JPOST Repository
ProteomicsPlasminogen deficiency exacerbates skeletal muscle loss during mechanical unloading in developing mice
This project is “Medical proteome analysis of osteoporosis- and bone mass-related proteins using the Kibo Japanese Experiment Module of International Space Station (ISS)”. Applying proteomic technologies, this research aims to identify proteins involved in spaceflight-induced deterioration of muscul...
ORGANISM(S): Mus Musculus (mouse) 
2024-02-01 | PXD041806 | JPOST Repository
ProteomicsThe customized mouse serum spectral library for the DIA-MS
For a comprehensive analysis of the mouse serum proteome, a customized mouse serum spectral library was constructed and utilized for quantitative analysis using DIA-MS. Our spectral library contained information on 1,106 mouse serum proteins. Creation of the spectral library was performed using Spec...
ORGANISM(S): Mus Musculus (mouse) 
2024-03-16 | PXD041889 | JPOST Repository
ProteomicsIdentification of gravity-responsive serum proteins in spaceflight mice using a quantitative proteomic approach with data-independent acquisition mass spectrometry
Physical inactivity associated with gravity unloading, such as microgravity during spaceflight and hindlimb unloading (HU), can cause various physiological changes. In this study, we attempted to identify serum proteins whose levels fluctuated in response to gravity unloading. First, we quantitative...
ORGANISM(S): Mus Musculus (mouse) 
2024-03-16 | PXD041894 | JPOST Repository
ProteomicsCharacterization of phosphopeptide enrichment strategy for mass spectrometry-based proteomic analysis
We attempted to evaluate four strategies for phosphopeptide enrichment, using the titanium dioxide (TiO2) and Phos-tag ligand particles, from in-solution or in-gel digests prior to mass spectrometry-based proteomic analysis.
ORGANISM(S): Homo Sapiens (human) Cellular Organisms 
2021-12-24 | PXD026295 | JPOST Repository
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