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ProteomicsIdentification of novel Kv1.3 channel dependent mechanisms in microglial activation
Pro-inflammatory microglia contribute to disease progression in neuroinflammatory and neurodegenerative diseases. We identify novel Kv1.3 channel-dependent molecular and cellular mechanisms during microglial activation and unravel a Kv1.3-dependent pathway for MHCI-restricted antigen presentation by...
ORGANISM(S): Mus musculus (Mouse) 
2018-10-24 | PXD006753 | Pride
Inflammation Potassium channel Systems pharmacology Microglia Bv2 
ProteomicsMapping Ubiquitination Sites in Alzheimer's Disease
Alzheimer’s Disease (AD) is characterized by the deposition of protein aggregates such as neurofibrillary tangles (NFTs) and amyloid (Aβ) plaques in the brain. Post-translational modification through ubiquitylationplays critical roles in clearing misfolded protein aggregates. Investig...
ORGANISM(S): Homo sapiens (Human) 
2019-06-25 | PXD009199 | Pride
Ubiquitylome Ad Gg remnant peptides 
ProteomicsMiddle-down proteomics reveals RNA binding proteins harbor dense sites of methylation and phosphorylation
Arginine (Arg)-rich RNA-binding proteins play an integral role in RNA metabolism. Post-translational modifications (PTMs) within Arg-rich domains, such as phosphorylation and methylation, regulate multiple steps in RNA metabolism. However, the identification of PTMs within Arg-rich domains with comp...
ORGANISM(S): Homo sapiens (Human) 
2020-01-31 | PXD015208 | Pride
Middle-down Rs protein Etd Decision tree Basic-acidic domains 
ProteomicsTargeted quantification of detergent-insoluble RNA-binding proteins in Alzheimer’s disease reveals disease-specific coaggregation signatures
Core spliceosome and related RNA-binding proteins aggregate in Alzheimer’s disease (AD) brain even in early asymptomatic stages (AsymAD) of disease. To assess the specificity of RNA-binding protein aggregation in AD, we developed a targeted mass spectrometry approach to quantify broad classes of RNA...
ORGANISM(S): Homo sapiens (Human) 
2021-03-17 | PXD022144 | Pride
Parkinson’s disease Alzheimer’s disease Insoluble proteins Rna-binding proteins Parallel reaction monitoring (prm) mass spectrometry Human brains 
ProteomicsPosttranslational modifications mediate the structural diversity of tauopathy strains
Tau aggregation is the defining pathological hallmark of tauopathies, but structural insights are revealing key differences between filaments across this class of disorders. Using cryo-electron microscopy, we identify a 107-residue fragment, K274-E380, which forms the insoluble core of tau filaments...
ORGANISM(S): Homo sapiens (Human) 
2020-02-14 | PXD016862 | Pride
Cbd Tau Mass spectrometry 
ProteomicsMembrane-Enriched Brain Proteome Across Stages of Alzheimer's Disease
Previous systems-based proteomic approaches have characterized alterations in protein co-expression networks of unfractionated asymptomatic (AsymAD) and symptomatic Alzheimer’s disease (AD) brains. However, it remains unclear how sample fractionation and sub-proteomic analysis influences the organi...
ORGANISM(S): Homo sapiens (Human) 
2019-09-02 | PXD014376 | Pride
Ad Synaptic proteome Transmembrane proteins 
ProteomicsQuantitative Proteomics of Acutely Isolated Mouse Microglia Identifies Novel Immune Alzheimer's Disease-related Proteins
Microglia are innate immune cells of the brain that perform phagocytic and inflammatory functions in disease conditions. Transcriptomic studies of acutely-isolated microglia have provided novel insights into their molecular and functional diversity in homeostatic and neurodegenerative disease states...
ORGANISM(S): Mus musculus (Mouse) 
2018-09-18 | PXD009137 | Pride
Cd11b-positive Brain resident microglia 
ProteomicsA U1-70K Protein Interaction Network Reveals a Functional Class of RNA Binding Proteins with Mixed Charge Domains
U1 small nuclear ribonucleoprotein 70 kDa (U1-70K) and other proteins of the spliceosome complex are mislocalized to cytoplasmic aggregates in Alzheimer’s disease (AD) brain, yet understanding of the specific mechanisms that cause their aggregation is limited. Many of the RNA binding proteins (RBPs)...
ORGANISM(S): Homo sapiens (Human) 
2018-06-21 | PXD008260 | Pride
U1-70k 
ProteomicsTBK1 interacts with tau and enhances neurodegeneration in tauopathy
One of the defining pathological features of Alzheimer’s Disease (AD) is the deposition of neurofibrillary tangles (NFTs) composed of hyperphosphorylated tau in the brain. Aberrant activation of kinases in AD has been suggested to enhance phosphorylation and toxicity of tau, making the responsible t...
ORGANISM(S): Homo sapiens (Human) 
2022-03-01 | PXD025301 | Pride
Coip Ikk Tbk1 mapt tau phosphorylation 
ProteomicsPhosphorylation regulates arginine-rich RNA-binding protein solubility and oligomerization
Post-translational modifications (PTMs) within splicing factor RNA-binding proteins (RBPs), such as phosphorylation, regulate several critical steps in RNA metabolism including spliceosome assembly, alternative splicing and mRNA export. Notably, the arginine-/serine-rich (RS) domains in SR proteins ...
ORGANISM(S): Homo sapiens (Human) 
2021-11-02 | PXD026894 | Pride
Post-translational modifications Protein interactions Srsf2 Mass spectrometry Phosphorylation Rna-binding proteins Sc35 
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