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ProteomicsA ternary Neurexin-T178-PTPR complex represents a core-module of neuronal synapse organization
Complexes of synaptic adhesion molecules instruct the formation, functional specification and plasticity of neuronal synapses. Proteomic and candidate gene studies have identified an array of synaptic adhesion molecules that may cooperate or provide independent columns connecting synaptic compartmen...
ORGANISM(S): Mus musculus (Mouse) Rattus norvegicus (Rat) 
2026-07-24 | PXD054017 | Pride
Mouse Synapse Neuron Brain Ap-ms. ms 
ProteomicsCryo-slicing BN-MS of rat brain mitochondrial proteins
Blue-native gel electrophoresis (BN) is a powerful method for protein separation. Combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS) it enables large-scale identification of protein complexes and their subunits. Current BN-MS approaches, however, are limited in size resolution, ...
ORGANISM(S): Rattus norvegicus (Rat) 
2015-12-01 | PXD002681 | Pride
Cryo-slicing bn-ms lc-ms/ms complexome proteine profiles 
ProteomicsThe molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics
The transient receptor potential cation channel, subfamily M, member 7 (TRPM7) is a ubiquitously expressed membrane protein consisting of an ion channel domain and an intracellularly located protein kinase domain. TRPM7 plays a fundamental role in the cellular uptake of divalent cations such as Zn2+...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) Rattus norvegicus (Rat) 
2021-11-29 | PXD025279 | Pride
Ap-ms Lc-ms Csbn-ms Magnesium Cnnm Calcium Trpm7 Arl15 Zinc 
ProteomicsSubunit composition, molecular environment and activation of native TRPC channels encoded by their interactomes
In the mammalian brain TRPC channels, a family of Ca2+-permeable cation channels, are involved in a variety of processes from neuronal growth and synapse formation to transmitter release, synaptic transmission and plasticity. The molecular appearance and operation of native TRPC channels, however, r...
ORGANISM(S): Mus musculus (Mouse) Rattus norvegicus (Rat) 
2024-07-17 | PXD036019 | Pride
Lc-msms Mouse Brain Rat Trpc 
ProteomicsHigh-Resolution Complexome-Profiling of Mitochondria Reveals Quality Control Pathways of Protein Import
Mitochondria contain ~1,000 different proteins that may assemble into larger entities such as respiratory (super)complexes and preprotein translocases. The molecular/structural organization of major parts of the mitochondrial proteome, however, has not yet been resolved. We report a quantitative map...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-02-03 | PXD029548 | Pride
Complexome Lc-ms Bn-ms Cryo-slicing Mitochondria Bn-page Yeast 
ProteomicsDynamics of AMPAR proteome across brain regions and in postnatal development
Native AMPA receptors (AMPAR) in the mammalian brain are macromolecular complexes whose functional characteristics vary across brain regions and postnatal development and change in response to neuronal activity. Both, structural and functional properties of the AMPARs are determined by their proteom...
ORGANISM(S): Rattus norvegicus (Rat) 
2016-07-06 | PXD001195 | Pride
Lc-msms Ap-ms Rat Development Ampa receptor Brain regions Proteome 
UnknownGSTM1 and GSTT1 polymorphisms associated with pain in a chemotherapy-induced peripheral neuropathy cohort.
Not available
S-EPMC10374820 | biostudies-literature
ProteomicsA Noelin-organized extracellular network of proteins required for constitutive and context-dependent anchoring of AMPA-receptors
Information processing and storage in the brain rely on AMPA-receptors (AMPARs) and their context-dependent dynamics in synapses and extra-synaptic sites. We found that distribution and dynamics of AMPARs in the plasma membrane are controlled by Noelins, a three-member family of conserved secreted p...
ORGANISM(S): Mus musculus (Mouse) Rattus norvegicus (Rat) 
2024-03-13 | PXD041655 | Pride
Ampa receptors Proteomics Molecular neuroscience 
ProteomicsA slit-diaphragm-associated protein network for dynamic control of renal filtration
The filtration of blood in the kidney which is crucial for mammalian life is determined by the slit-diaphragm (SD), a proteinaceous junction between the foot processes of renal podocytes. Based on studies of structure and function the SD has been hypothesized to operate as a final barrier or as a ‘m...
ORGANISM(S): Mus musculus (Mouse) Rattus norvegicus (Rat) 
2022-09-20 | PXD034356 | Pride
Ap-ms Kidney Podocytes Rat Neph1 Nephrin Podocin Mouse Slit-diaphragm Orbitrap Renal filtration Lc-ms/ms 
ProteomicsFlavonol-mediated stabilization of efflux complexes regulates polar auxin transport
The transport of auxin controls the rate, direction and localization of plant growth and development. The course of auxin transport is defined by the polar subcellular localization of the PIN proteins, a family of auxin efflux transporters. Using blue native PAGE and quantitative mass spectrometry, ...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-10-08 | PXD021543 | Pride
Arabidopsis thaliana Ap-ms Auxin transport 
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