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ProteomicsDLX2-FLAG IP-MS in embryonic bodies (EBs): Protein complexes identification
The ectomesenchyme generates much of the craniofacial skeleton, sutures, and diverse connective tissues in the mammalian head, yet its derivation from embryonic stem cells (ESCs) and the underlying molecular drivers remain poorly defined. Here, we identified Dlx2 as a key regulator that efficiently ...
ORGANISM(S): Mus musculus (Mouse) 
2025-11-06 | PXD064236 | Pride
Embryonic bodies Ip-ms Dlx2-flag 
ProteomicsIdentification of Sh3rf3-interacting proteins in mouse prefrontal cortex by immunoprecipitation mass spectrometry
Sh3rf3 is an ASD-associated gene,Sh3rf3 deficiency reduces excitatory synaptic strength in prefrontal cortex and decreases the readily releasable vesicle pool and attenuated vesicle replenishment.To delve into the underlying mechanisms for impaired excitatory transmission, we performed immunoprecipi...
ORGANISM(S): Mus musculus (Mouse) 
2026-03-23 | PXD061685 | Pride
Prefrontal cortex Mouse Ip-ms Sh3rf3 
UnknownElucidating the origins of multimode vibrational coherences of polyatomic molecules induced by intense laser fields.
Not available
S-EPMC5622070 | biostudies-literature
ProteomicscTAGE5/MEA6 regulates LBR transport to maintain nuclear envelope integrity and safeguard against aging
IP-MS of fused MEA6-GFP and the control sample were performed. For MS analyses, peptides were resuspended in 0.1% FA and analyzed by LTQ Orbitrap Elite mass spectrometer (ThermoFisher Scientific) coupled online to an Easy-nLC 1000 (Thermo Fisher Scientific) in the data-dependent mode.
ORGANISM(S): Homo Sapiens 
2025-04-24 | PXD063263 |
ProteomicsQuantitative proteomic and phosphoproteomic profiling of Sh3rf3-deficient ASD mouse model via 6Plex-TMT and phosphoproteomic
This study aims to systematically investigate the molecular mechanisms underlying autism spectrum disorder (ASD) by analyzing the proteome and phosphoproteome of a Sh3rf3-deficient mouse model. SH3RF3 (SH3 domain-containing RING finger protein 3) is implicated in synaptic regulation pathways, yet it...
ORGANISM(S): Mus musculus (Mouse) 
2026-03-23 | PXD061722 | Pride
Prefrontal cortex Mouse Ms Sh3rf3 
ProteomicsFunctional identification of protocadherin alpha 9 (PCDHA9) as a candidate causative gene for amyotrophic lateral sclerosis
Mice were sacrificed after anesthesia by isoflurane following neck cutting. The spinal cord L3-L5 was taken and frozen in liquid nitrogen immediately and the ventral horn of the bilateral spinal cord (about 400um thick in gray matter area) was collected at low temperature. The samples were digested ...
ORGANISM(S): Mus Musculus 
2023-06-12 | PXD042929 |
ProteomicsiTRAQ-based Proteome Profiling of Differentially Expressed Proteins in Insulin-resistant Human Hepatocellular Carcinoma
Comparison of Proteomics Changes in hepatocellular carcinoma cells and insulin resistant hepatocellular carcinoma cells
ORGANISM(S): Homo Sapiens 
2022-02-22 | PXD031820 |
ProteomicsLoss of Necdin causes social deficit and aberrant synaptic function through destabilization of SynGAP
The Ras GTPase-activating protein SynGAP interacts with PSD95 to regulate synaptic morphology and function at the postsynaptic density in neurons. Haploinsufficiency of SYNGAP1 has been linked to autism spectrum disorders (ASD) and intellectual disability (ID). While transcriptional and translationa...
ORGANISM(S): Mus Musculus 
2025-05-17 | PXD064040 |
ProteomicsTransfer of the high-quality sugar metabolic model of Aspergillus niger is reliable within the same fungal phylum, but limited for fungi of other phyla
Validation of metabolic models, extrapolated from the reference sugar catabolism genetic network of Aspergillus niger by using an orthology-based approach, of evolutionarily diverse fungi.
ORGANISM(S): Trichoderma Reesei (ncbitaxon:51453) Penicillium Subrubescens (ncbitaxon:1316194) Aspergillus Niger (ncbitaxon:5061) Phanerochaete Chrysosporium Rp-78 (ncbitaxon:273507) Aspergillus Nidulans (ncbitaxon:162425) 
MSV000090441 | MassIVE
ProteomicsShigella induces stress granule formation by ADP-riboxanation of the eIF3 complex
We utilized a large-scale proteomic profiling strategy to quantitatively measure ADP-riboxanation (and classical ADP-ribosylation) levels of host proteins upon introduction of bacterial effectors. Notably, we identified the eukaryotic translation initiation factor 3 (eIF3) complex as a novel target ...
ORGANISM(S): Homo Sapiens 
2024-01-18 | PXD048666 |
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