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The low abundance and hydrophobicity of plasma membrane proteome relative to soluble proteins makes it difficult to characterize. Here, we apply the peptidisc membrane mimetic to purify the cell membrane proteome. We used HeLa cells as a reference to establish the method, and compared the plasma mem...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD039990 | Pride
The low abundance and hydrophobicity of plasma membrane proteome relative to soluble proteins makes it difficult to characterize. Here, we apply the peptidisc membrane mimetic to purify the cell membrane proteome. We used HeLa cells as a reference to establish the method, and compared the plasma mem...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD041913 | Pride
Integral membrane proteins (IMPs) are key targets for small-molecule therapeutics. However, robust, unbiased, and detergent-free methods to probe on- and off-target interactions within this protein class remain underdeveloped. Previously, we introduced the Peptidisc membrane mimetic (MM) for water-s...
ORGANISM(S): Mus musculus (Mouse) 
2025-11-17 | PXD068828 | Pride
Many soluble proteins interact with membranes to perform important biological functions, including signal transduction, regulation, transport, trafficking and biogenesis. Despite their importance, these protein-membrane interactions are difficult to characterize due to their often-transient nature a...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-12-30 | PXD027992 | Pride
The outer membrane of gram-negative bacteria plays a critical role in protecting the cell against external stressors, including antibiotics. Given its importance to the resistance mechanisms, the outer membrane is a prime target for antimicrobial drug discovery. To facilitate discovery efforts, howe...
ORGANISM(S): Escherichia coli 
2023-03-11 | PXD036749 | Pride
The peptidisc membrane mimetic enables global reconstitution of the bacterial membrane proteome into water-soluble detergent-free particles, termed peptidisc libraries. We present here a method that combines peptidisc libraries and chromosomal-level gene tagging technology with affinity purification...
ORGANISM(S): Escherichia coli 
2022-06-09 | PXD032315 | Pride
Membrane proteins (MPs) are vital to cellular signaling, metabolism, and disease pathology, yet remain underrepresented in proteomics. To address this, several independent workflows have been developed to enable the profiling of the membrane proteome, however the relative advantages and limitations ...
ORGANISM(S): Mus musculus (Mouse) 
2026-01-01 | PXD070243 | Pride
We combine the membrane mimetic (MM) Peptidisc with thermal proteome profiling (TPP) to screen membrane proteomes in detergent-free environments. Using whole mouse liver, we demonstrate the stabilization of integral membrane proteins (IMPs), specifically ATP-binding cassette transporters, through in...
ORGANISM(S): Mus musculus (Mouse) Escherichia coli 
2025-11-17 | PXD055093 | Pride
Alcohol consumption and high-fat diets often coincide in Western society, exerting negative synergistic effects on the liver. While many studies have demonstrated the impact of ALD and NAFLD on protein expression, none have offered a comprehensive view of the dysregulation at the level of the membra...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-06 | PXD050825 | Pride
We reconstituted the total E. coli membrane proteome into His-tagged peptidiscs. We then performed an affinity purification to enrich the bona fide membrane proteome away from soluble contaminants which co-sediment with cellular membranes after cell lysis. As a case study, we employ this method to s...
ORGANISM(S): Escherichia coli 
2022-04-11 | PXD017242 | Pride
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