Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Mouse mitochondrial CLPP substrate identification

ABSTRACT: 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

INSTRUMENT(S): maXis

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Heart

SUBMITTER: Pitter Huesgen

LAB HEAD: Pitter Huesgen

PROVIDER: PXD018194 | Pride | 2020-06-01

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	170118ClppHeartspreTAILS1_GA1_01_1406.d.7z	Other
	170118ClppHeartspreTAILS2_GA2_01_1407.d.7z	Other
	170118ClppHeartspreTAILS3_GA3_01_1408.d.7z	Other
	MQ_ClpP_preTAILS_QC.7z	Other
	MQ_ClpP_preTAILS_proteome.7z	Other

Items per page:

1 - 5 of 5

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

N-degradomic analysis of proteolytic processing in WT1 heterozygous mice

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

2021-02-15 | PXD023292 | 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

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

Exploring potential virulence regulators in Paracoccidioides brasiliensis isolates of varying virulence through quantitative proteomics

Project description:Paracoccidioides brasiliensis is the agent of paracoccidioidomycosis, an important systemic mycosis in Latin America. Few virulence factors have been identified for this pathogen. In this study, we quantitatively evaluated the protein composition of P. brasiliensis in the yeast phase using minimal and rich media to obtain a better understanding of its virulence and to gain new insights into pathogen adaptation strategies. This analysis was performed on two isolates of the Pb18 strain showing distinct infection profiles in B10.A mice. Using liquid chromatography/tandem mass spectrometry (LC-MS/MS) analysis, we identified and quantified 317 proteins in minimal medium, 29 of which were overexpressed in virulent Pb18. In rich medium, 29 out of 214 identified proteins were over-expressed in the virulent fungus. Alcohol dehydrogenase, mitochondrial peroxiredoxin PRX1 and protein vacuolar ATP synthase catalytic subunit A were up-regulated in virulent Pb18 in both media, suggesting potential roles of these proteins in virulence regulation in P. brasiliensis. Proteins up-regulated in both isolates were grouped according to their functional categories. Virulent Pb18 undergoes metabolic reorganization and increased expression of proteins involved in fermentative respiration. This approach allowed us to identify potential virulence regulators and to understand how Paracoccidioides modulates the host-pathogen interaction to its advantage. Data are available via ProteomeXchange Consortium with identifier PXD000804.

2014-08-28 | PXD000804 | 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

AIG1 and ADTRP are endogenous FAHFA hydrolases

Project description:Fatty acid esters of hydroxy fatty acids (FAHFAs) are a newly discovered class of signaling lipids with anti-inflammatory and anti-diabetic activities. However, the endogenous regulation of FAHFAs remains a pressing but unanswered question. Here, we find that androgen- induced gene 1 (AIG1) and androgen-dependent TFPI-regulating protein (ADTRP), two threonine hydrolases, control FAHFA levels in vivo. Tissues from mice lacking ADTRP (Adtrp-KO), AIG1 (Aig1-KO), and AIG1/ADTRP (DKO) have higher concentrations of FAHFAs, including 9-PAHSA, due to decreased FAHFA hydrolysis activity. No other lipids were changing in these samples to indicate that AIG1 and ADTRP are specific FAHFA hydrolases. To complement these genetic studies, we identified a dual AIG1/ADTRP inhibitor, ABD-110207, that is active in vivo. Acute treatment of wild-type mice with ABD-110207 results in elevated FAHFA levels further supporting AIG1 and ADTRP enzymatic activity in controlling endogenous FAHFAs. The loss of AIG1/ADTRP does not mimic the effects of pharmacologically administered FAHFAs on glucose tolerance or insulin sensitivity in mice, indicating that therapeutic strategies should continue to focus on FAHFA administration. Together, these studies designate AIG1 and ADTRP as the first endogenous FAHFA hydrolases identified and provide critical genetic and chemical tools for further characterization of these enzymes and endogenous FAHFAs.

2020-03-09 | PXD017539 | Pride

Root proteome of ASPR1- deficient Arabidopsis thaliana compared to wt

Project description:Seedlings lacking the atypical aspartic protease encoded by the gene At2g03200 exhibited shorter primary roots and a pronounced reduction in the number of lateral roots. The protease was therefore name ATYPICAL ASPARTIC PROTEASE IN ROOTS 1 (ASPR1). This project compared the root proteome of a T-DNA insertion line lacking ASPR1 with wild type seedlings.

2019-02-25 | PXD009580 | Pride

N-terminome analysis of pathogen-induced cell death in maize

Project description:Regulated cell death (RCD) is crucial for plant development, as well as in decision-making in plant-pathogen interactions. Previous studies revealed components of the molecular network controlling RCD, including different proteases. However, the identity, the proteolytic network as well as molecular components involved in the initiation and execution of distinct plant RCD processes, still remain largely elusive. We analyzed the N-terminome of Z. mays leaves treated with the Xanthomonas effector avrRxo1, the mycotoxin Fumonisin B1 (FB1), or the phytohormone salicylic acid (SA) to dissect plant cellular processes related to cell death and plant immunity. We found highly distinct and time-dependent biological processes being activated on N-terminome level in response to avrRxo1, FB1 and SA. This study characterizes distinct RCD responses in Z. mays and provides a framework for the mechanistic exploration of components involved in the initiation and execution of cell death.

2023-07-13 | PXD041656 | 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 ›

Tweets

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