Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

N-degradomic analysis of proteolytic processing in WT1 heterozygous mice

ABSTRACT: N-degradomic analysis of proteolytic processing in WT1 heterozygous mice, suffering from genetically induced chronic kidney injury, compared to wild type

INSTRUMENT(S): impact II

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Kidney

DISEASE(S): Chronic Kidney Disease

SUBMITTER: Pitter Huesgen

LAB HEAD: Pitter Huesgen

PROVIDER: PXD023292 | Pride | 2021-02-15

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Similar Datasets

PAN-treated rat model of kidney injury

Project description:N-degradomic analysis of proteolytic processing in rat glomeruli injured by PAN-treatment compared to control.

2021-02-15 | PXD023299 | Pride

Rat podocyte degradomics - N-Degradomic Analysis Reveals a Proteolytic Network Processing the Podocyte Cytoskeleton

Project description:Regulated intracellular proteolysis is essential in maintaining the integrity of podocytes and the glomerular filtration barrier of the kidney. Altered proteolytic substrate turnover has been associated with various glomerular diseases ranging from diabetic nephropathy to focal and segmental glomerulosclerosis. However, thus far it has not been possible to systematically identify proteolytically cleaved proteins although some of the proteases have been characterized. Here we applied TAILS to identify N-termini in rat glomeruli and their changes on PAN-induced injury.

2017-07-20 | PXD006356 | Pride

Podocyte degradomics - N-Degradomic Analysis Reveals a Proteolytic Network Processing the Podocyte Cytoskeleton

Project description:Regulated intracellular proteolysis is essential in maintaining the integrity of podocytes and the glomerular filtration barrier of the kidney. Altered proteolytic substrate turnover has been associated with various glomerular diseases ranging from diabetic nephropathy to focal and segmental glomerulosclerosis. However, thus far it has not been possible to systematically identify proteolytically cleaved proteins although some of the proteases have been characterized. Here we applied TAILS to map N-termini in the mouse glomeruli proteome and to determine and quantify N termini in podocyte cell cultures challenged with PAN.

2017-07-20 | PXD005139 | Pride

Mouse kidney cisplatin TAILS - The proteome microenvironment determines the protective effect of preconditioning in cisplatin-induced acute kidney injury

Project description:Profiling of proteolytic events mouse kidneys during cisplatin-induced kidney damage. Kidneys from vehicle-treated mice are compared to cisplatin-treated mice and cisplatin treatment in animals preconditioned by hypoxia or calory restriction regimes.

2018-10-29 | PXD007186 | Pride

Mouse mitochondrial CLPP substrate identification

Project description:Identification ofputative ClpXP substrates by combination of proteome analysis and TAILS N termini profiling from wt and ClpP-deficient mouse heart mitochondria, combined with substrate trapping using catalytically inactive ClpP expressed in MEF cell culture. This dataset provides the preTAILS proteomedata

2020-06-01 | PXD018194 | Pride

Human podocyte cell culture degradomics

Project description:Regulated intracellular proteolysis is essential in maintaining the integrity of podocytes and the glomerular filtration barrier of the kidney. Altered proteolytic substrate turnover has been associated with various glomerular diseases ranging from diabetic nephropathy to focal and segmental glomerulosclerosis. However, thus far it has not been possible to systematically identify proteolytically cleaved proteins although some of the proteases have been characterized. Here we applied TAILS to map N-termini in the mouse glomeruli proteome and to determine and quantify N termini in podocyte cell cultures challenged with PAN.

2017-07-20 | PXD005140 | Pride

AtLEGbeta / gamma protease specificity and putative substrate characterization by HUNTER

Project description:Arabidopsis thaliana Legumain (aka VPE) beta / gamma were characterized for their cleavage specificity and putative substrates were identified by the N-termini enrichment method HUNTER.

2020-07-29 | PXD019276 | Pride

The Paulinella chromatophore N-terminome

Project description:The cercozoan amoeba Paulinella chromatophora contains photosynthetic organelles - termed chromatophores - that evolved from a cyanobacterium ~100 million years ago, independently from plastids in plants and algae. Despite its more recent origin, at least one third of the chromatophore proteome consists of nucleus-encoded proteins that are imported by an unknown mechanism across the chromatophore double envelope membranes. Chromatophore-targeted proteins fall into two classes. Proteins exceeding 250 amino acids carry a conserved N-terminal sequence extension, termed the ‘chromatophore transit peptide’ (crTP), that is presumably involved in guiding these proteins into the chromatophore. Short imported proteins do not carry discernable targeting signals. To explore whether the import of protein is accompanied by their N-terminal processing, here we used a mass spectrometry-based approach to determine protein N-termini in Paulinella chromatophora and identified N-termini of 208 chromatophore-localized proteins. Our study revealed extensive N-terminal modifications by acetylation and proteolytic processing in both, the nucleus and chromatophore-encoded fraction of the chromatophore proteome. Mature N-termini of 37 crTP-carrying proteins were identified, of which 30 were cleaved in a common processing region. Our results imply that the crTP mediates trafficking through the Golgi, is bipartite and surprisingly only the N-terminal third (‘part 1’) becomes cleaved upon import, whereas the rest (‘part 2’) remains at the mature proteins. In contrast, short imported proteins remain largely unprocessed. Finally, this work sheds light on N-terminal processing of proteins encoded in an evolutionary-early-stage photosynthetic organelle and suggests host-derived post-translationally acting factors involved in dynamic regulation of the chromatophore-encoded chromatophore proteome.

2023-04-06 | PXD028527 | Pride

D. magna CT448 protease specificity

Project description:Mass developments of toxin-producing cyanobacteria are frequently observed in freshwater ecosystems due to eutrophication and global warming. These mass developments can partly be attributed to cyanobacterial toxins, such as protease inhibitors (PIs), which inhibit digestive serine proteases of Daphnia, the major herbivore of phytoplankton and cyanobacteria. To date, mechanisms of this inhibition in the gut of the crustacean Daphnia magna are not known. Here, we characterize a single serine protease, chymotrypsin 448 (CT448), which is present in the gut of the crustacean D. magna.

2018-10-04 | PXD010978 | Pride

Proteome Analysis of Arabidopsis thaliana PP7L mutants

Project description:Chloroplast biogenesis is indispensable for proper plant development. In a screen for photosynthesis affected mutants, we have identified the pp7l (serine/threonine-protein phosphatase7-like) mutant in which chloroplast development is delayed in cotyledons and young leaves. PP7L constitutes together with PP7 and PP7-long the type 7 subfamily of serine/threonine-specific phosphoprotein phosphatases (PPPs). Here we performed shotgun proteomic experiment in order to profile the changes in protein levels in the pp7l mutants in comparison to the wild-type (Col-0).

2019-02-19 | PXD012105 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data