Proteomics

Dataset Information

0

Tau interactome - The human tau interactome: binding to the ribonucleoproteome, and impaired binding of the P301L mutant to chaperones and the proteasome

ABSTRACT: The tau protein is central to the etiology of several neurodegenerative diseases, including Alzheimer’s disease, a subset of frontotemporal dementias, progressive supranuclear palsy and dementia following traumatic brain injury, yet the proteins it interacts with have not been studied using a systematic discovery approach. The study employed mild in vivo crosslinking, isobaric labeling and tandem mass spectrometry to characterize molecular interactions of human tau in a neuroblastoma cell model.

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Neuroblast

DISEASE(S): Alzheimer's Disease

SUBMITTER: Gerold Schmitt-Ulms  

LAB HEAD: Gerold Schmitt-Ulms

PROVIDER: PXD002058 | Pride | 2015-08-17

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
1_OF_SH-SY5Y_hTau1-441-EGFP_v_EGFP_interactome_6_7_8_9_0_1_C18_1-3_SCX_1-3_Percolator.msf Msf
1_OF_SH-SY5Y_hTau40_EGFP_interactome_6_7_8_9_0_1_C18_1.raw Raw
1_OF_SH-SY5Y_hTau40_EGFP_interactome_6_7_8_9_0_1_C18_2.raw Raw
1_OF_SH-SY5Y_hTau40_EGFP_interactome_6_7_8_9_0_1_C18_3.raw Raw
1_OF_SH-SY5Y_hTau40_EGFP_interactome_6_7_8_9_0_1_SCX_1.raw Raw
Items per page:
1 - 5 of 31
altmetric image

Publications

The Human Tau Interactome: Binding to the Ribonucleoproteome, and Impaired Binding of the Proline-to-Leucine Mutant at Position 301 (P301L) to Chaperones and the Proteasome.

Gunawardana C Geeth CG   Mehrabian Mohadeseh M   Wang Xinzhu X   Mueller Iris I   Lubambo Isabela B IB   Jonkman James E N JE   Wang Hansen H   Schmitt-Ulms Gerold G  

Molecular & cellular proteomics : MCP 20150811 11

The tau protein is central to the etiology of several neurodegenerative diseases, including Alzheimer's disease, a subset of frontotemporal dementias, progressive supranuclear palsy and dementia following traumatic brain injury, yet the proteins it interacts with have not been studied using a systematic discovery approach. Here we employed mild in vivo crosslinking, isobaric labeling, and tandem mass spectrometry to characterize molecular interactions of human tau in a neuroblastoma cell model.  ...[more]

Similar Datasets

Proteomics 0N4R Tau and 0N4R Tau P301L Neuronal Interactomes
2024-07-03 | PXD044959 | Pride
Proteomics Neuronal interactome changes upon aggregation of Tau
2020-01-30 | PXD015432 | Pride
Proteomics Truncated Tau - Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms
2015-05-15 | PXD001353 | Pride
Proteomics Tau molecular diversity mediates clinical heterogeneity in Alzheimer’s disease
2020-08-09 | PXD018855 | Pride
Proteomics Targeted mass spectrometry of Tau preparations purified from Alzheimer’s Disease brains plus either the deubiquitylase USP21 or its activity-dead mutant C221A.
2024-06-18 | PXD046645 | Pride
Proteomics Identification of proteins that interact with extracellularly applied fibrillar Tau assemblies
2019-01-09 | PXD009294 | Pride
Proteomics Simple, single-shot phosphoproteomic analysis of heat-stable tau
2021-11-25 | PXD027971 | Pride
Proteomics Specific post-translational modifications of the soluble tau protein distinguish between Alzheimer’s disease, 4R-, and 3R-tauopathies
2023-06-22 | PXD038901 | Pride
Proteomics Quantitative PTM Maps of Human Pathologic Tau Identify Patient Heterogeneity and Define Critical Steps in Alzheimer’s Disease Progression - angular gyrus
2020-12-04 | PXD020517 | Pride
Proteomics TBK1 interacts with tau and enhances neurodegeneration in tauopathy
2022-03-01 | PXD025301 | Pride