Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteomic changes linked to the limbic stage of AD

ABSTRACT: Alzheimer's disease (AD) is a neurodegenerative disorder and the most common cause of dementia worldwide. In AD, neurodegeneration spreads throughout the brain cortex in a gradual and predictable pattern, causing progressive memory decline and cognitive impairment. Here, we conducted proteomic, acetylomic and phosphoproteomic analyses of human postmortem tissue samples from AD (Braak stage III-IV) and control brains, covering all anatomical areas affected during the limbic stage of the disease (total hippocampus, CA1, entorhinal and perirhinal cortices). A total of 58 tissues were analyzed by nanoLC-MS/MS.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

DISEASE(S): Alzheimer's Disease

SUBMITTER: Melinda Rezeli

LAB HEAD: Gyorgy Marko-Varga

PROVIDER: PXD027173 | Pride | 2021-12-30

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	180718_B598_1_phospho.raw	Raw
	180718_C635_phospho.raw	Raw
	180718_D803_phospho.raw	Raw
	180802_P350_phospho.raw	Raw
	180802_P599_1_phospho.raw	Raw

Items per page:

1 - 5 of 136

Publications

Topological Dissection of Proteomic Changes Linked to the Limbic Stage of Alzheimer's Disease.

Velásquez Erika E Szeitz Beáta B Gil Jeovanis J Rodriguez Jimmy J Palkovits Miklós M Renner Éva É Hortobágyi Tibor T Döme Péter P Nogueira Fábio Cs FC Marko-Varga György G Domont Gilberto B GB Rezeli Melinda M

Frontiers in immunology 20211012

Alzheimer's disease (AD) is a neurodegenerative disorder and the most common cause of dementia worldwide. In AD, neurodegeneration spreads throughout different areas of the central nervous system (CNS) in a gradual and predictable pattern, causing progressive memory decline and cognitive impairment. Deposition of neurofibrillary tangles (NFTs) in specific CNS regions correlates with the severity of AD and constitutes the basis for disease classification into different Braak stages (I-VI). Early ...[more]

PMID: 34712240

Similar Datasets

Human brain Alzheimer's - Proteomic signatures of brain regions affected by tau pathology in early and late stages of Alzheimer's disease

Project description:Alzheimer’s disease (AD) is the most common neurodegenerative disorder being characterized by progressive impairment of memory and cognition, resulting in dementia. To investigate brain region vulnerability to AD and which pathways are altered in certain areas in AD, we performed proteomic profiling of human brain samples during AD progression in regions early (medial temporal lobe - MTL) and late affected (neocortex) by tau pathology. We employed a mass spectrometry-based approach to interrogate the human brain proteome during AD progression (B/B stages) in four distinct brain regions: entorhinal cortex (EC), parahippocampal cortex (PHC), temporal cortex (TC) and frontal cortex (FC). Importantly, we wanted to evaluate brain areas that are affected by tau pathology in different disease stages, in order to gain insights if there are common mechanisms or patterns shared between different brain regions during disease progression. A total of 103 samples were analyzed by nanoLC-MS/MS.

2019-07-01 | PXD010138 | Pride

RNA-seq of human plasma microRNAs in Alzheimer Disease

Project description:MicroRNAs (miRNAs) could play an important role as potential Alzheimer Disease (AD) biomarkers. Plasma samples were collected from participants: Mild cognitive impairment (MCI) due to AD patients (n= 20), preclinical AD patients (n= 8) and healthy controls (n= 20). Then, small RNA sequencing analysis, followed by miRNA differential expression analysis comparing different methods (DESeq2, edgeR, NOISeq) were carried out.

2022-05-08 | E-MTAB-11103 | biostudies-arrayexpress

Large scale investigation of the phage Vp16 PDF activity

Project description:Prokaryotic proteins must be deformylated before the removal of their first methionine. Peptide deformylase (PDF) is indispensable and guarantees this cotranslational mechanism. Recent genome sequencing and annotation studies highlighted over 2x104 putative peptide deformylase sequences. Furthermore, unpredicted modified bacterial PDF genes have been retrieved from many phages. Sequence comparisons with other known PDFs reveal that viral PDFs are devoid of the key ribosome-interacting C-terminal region. Little is known regarding these viral PDFs, including the capacity of the corresponding encoded proteins to ensure deformylase activity in vitro or in vivo. This investigation determines the activity of the recombinant Vp16 PDF in E. coli PDF defective cell to remove the N-formyl group at the protein N-terminus.

2017-09-25 | PXD006008 | Pride

Reference dataset for EnCOUNTer tool development

Project description:Reference dataset used for the development of the EnCOUNTEr tool to both (i) score all characterized peptides using discriminant parameters to evidence mature protein N-termini and (ii) determine the N-terminus acetylation yield for the most reliable ones.

2017-03-14 | PXD005720 | Pride

Searching N-terminal modifications of proteins starting with Gly in Arabidopsis thaliana

Project description:Characterization of Myristoylated proteins in Arabidopsis thaliana Col 0 wild type

2018-06-18 | PXD008663 | Pride

Integrated lysine acetylation stoichiometry and proteomics analysis in human cells

Project description:Lysine acetylation is a widespread posttranslational modification that targets a large number of biological pathways. Recent studies reveal that lysine acetylation sites exhibit mainly low stoichiometry. Here we explored three sample preparation methods, the use of detergents for the chemical acetylation reaction in combination with stable and efficient alkylating reagent, to analyze the stoichiometry of acetylation in three human cell lines. We identified and determined the acetylation occupancy in about 1500 protein in each cell line. Lysine acetylation is highly dynamic, we determined variations in the acetylation stoichiometry when nearby residues are phosphorylated. The stoichiometric analysis in combination with quantitative proteomics allowed us to better understand the role of this PTM in different cells. We found that high abundance of the deacetylase SIRT1 correlates with less acetylation occupancy and abundance of ribosomes, proteins involved in ribosome biogenesis, rRNA processing, among others. We confirmed through the inhibition of SIRT1 with EX-527, followed by quantitative proteomics and acetylation stoichiometry analyzes, the negative role of this deacetylase on transcription and translation pathways. In addition, we found that SIRT1 positively regulates several metabolic pathways.

2017-09-12 | PXD005903 | Pride

Positional proteomics identification of the natural substrates of cytosolic carboxypeptidases

Project description:Cytosolic carboxypeptidases (CCPs) constitute a new subfamily of M14 metallocarboxypeptidases associated to axonal regeneration and neuronal degeneration, amongst others. CCPs are deglutamylating enzymes, able to catalyze the shortening of polyglutamate side-chains and the gene-encoded C-termini of tubulin, telokin and myosin light chain kinase. The functions of these enzymes are not entirely understood, in part due to lack of information about C-terminal protein processing in the cell and its functional implications. By means of C-terminal COFRADIC, a positional proteomics approach, we searched for cellular substrates targets of CCP1, the most relevant member of this family. We here identified 7 new putative CCP1 protein substrates, including ribosomal proteins, translation factors and high mobility group proteins.

2014-12-02 | PXD000834 | Pride

Chromatin immunoprecipitation to map nucleosomes and H3 lysine 14 acetylation in two unrelated strains of yeast

Project description:Nucleosome mapping and histone H3 lysine 14 acetylation chromatin immuno-precipitation in two unrelated strains of yeast (BY and RM).

2009-08-29 | E-MEXP-1777 | biostudies-arrayexpress

An organellar Nα-acetyltransferase Naa60 acetylates cytosolic N-termini of transmembrane proteins and maintains Golgi integrity

Project description:N-terminal acetylation is a major and vital protein modification catalysed by N-terminal acetyltransferases (NATs). NatF or Nα-acetyltransferase 60 (Naa60) was recently identified as a NAT in higher eukaryotes. Here, we found that Naa60 differs from all other known NATs by its Golgi localization. A new membrane topology assay named PROMPT and a selective membrane permeabilization assay established Naa60 to face the cytosolic side of intracellular membranes. An Nt-acetylome analysis of NAA60 knockdown cells revealed that Naa60, as opposed to other NATs, specifically acetylates transmembrane proteins, and that is has a preference for N-termini facing the cytosol. Moreover, NAA60 knockdown caused Golgi fragmentation, indicating an important role in maintenance of Golgi structural integrity. This work uncovers the first NAT associated with membranous compartments and establishes N-terminal acetylation as a common modification among transmembrane proteins, a thus far poorly characterized part of the N-terminal acetylome.

2019-06-04 | PXD001155 | Pride

Naa30 is critically involved in maintaining mitochondrial and Golgi integrity

Project description:N-terminal acetylation is one of the most common protein modifications in eukaryotes, with emerging roles in regulating protein quality and stoichiometry and targeting and complex formation. The NatC complex is one of the three major N-terminal acetyltransferases (NATs). Here, we partially defined the in vivo human NatC Nt-acetylome by combining siNAA30 mediated knockdown with positional proteomics. We identified 51 human NatC substrates and expanded our current knowledge on the substrate repertoire of NatC which now includes proteins harboring Met-Leu, Met-Ile, Met-Phe, Met-Trp, Met-Tyr, Met-Trp, Met-Met, Met-His and Met-Lys N-termini. Next to cytosolic proteins, several organellar proteins were identified as NatC substrates. Interestingly, upon Naa30 depletion, the levels of several organellar proteins were reduced, in particular those of mitochondrial proteins. Further, knockdown of Naa30 induced the loss of membrane potential, clearing and fragmentation of mitochondria. Naa30 depletion also led to disassembly of the Golgi apparatus. However, Naa30 depletion did not affect ER morphology, endosome or peroxisome distribution or microtubule and actin cytoskeletal architecture, suggesting that the observed mitochondrial fragmentation and clearance and Golgi scattering are not due to general disruption of organelles or microtubules. In conclusion, NatC Nt-acetylates a large variety of cytosolic and organellar proteins and is essential for cis-Golgi integrity and mitochondrial function.

2016-10-05 | PXD000930 | 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