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ProteomicsImproved protease digestion conditions for membrane protein detection
This work presents improved protease digestion conditions for membrane protein detection. Two improved conditions, 0.01% SDS or the combination of 10% MeOH and 0.01% RapiGest, were chosen and applied to proteins from Escherichia coli. The application of both improved conditions to a membrane protein...
ORGANISM(S): Escherichia coli 
2015-04-28 | PXD001824 | Pride
Proteomics Membrane protein E. coli 
ProteomicsHuman_MCF7_membrane - Searching Missing Proteins Based on the Optimization of Membrane Protein Enrichment and Digestion Process
MCF7 cell was an important stabilized breast cancer cell in cancer research. A membrane proteomic method was developed and compared in this study. A membrane protein enrichment method composed of ultra-centrifugation and detergent-based extraction was first developed. Then in-solution digestion with...
ORGANISM(S): Homo sapiens (Human) 
2016-10-07 | PXD004131 | Pride
Human Mcf7 Membrane 
ProteomicsStructure-guided development of chemically tailored peptide binders of RNF43/ZNRF3 to enable versatile design of membrane protein-targeting PROTACs
Targeted membrane protein degradation using cell surface E3 ligases RNF43/ZNRF3 via proteolysis targeting chimeras (PROTACs) represents an effective strategy for treating membrane drug targets that cannot be fully inhibited using traditional inhibitors. Several ingenious chimeras have been developed...
ORGANISM(S): Homo Sapiens 
2025-03-04 | PXD061425 |
ProteomicsDigestion time course of human liver plasma membrane
The selection of signature peptides is critical for reliable peptide quantification. The purpose of this study was to comprehensively assess the digestion efficiency and stability of tryptic peptides and to identify optimal signature peptides for human hepatic transporters and membrane marker protei...
ORGANISM(S): Homo Sapiens (human) 
2022-10-12 | PXD034402 | JPOST Repository
ProteomicsGlobal Subcellular Characterization of Protein Degradation Using Quantitative Proteomics
Protein degradation provides an important regulatory mechanism used to control cell cycle progression and many other cellular pathways. To comprehensively analyze the spatial control of protein degradation in U2OS osteosarcoma cells, we have combined drug treatment and SILAC-based quantitative mass ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080816 | MassIVE
ProteomicsProteomic Characterization of Human Milk Fat Globule Membrane Proteins during a 12 Month Lactation Period
The milk fat globule membrane (MFGM) contains proteins which have been implicated in a variety of health benefits. Milk fat globule membrane proteins were isolated from human milk during a 12 month lactation period and subjected to in solution digestion and liquid chromatography tandem mass spectrom...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-06-24 | MSV000089722 | MassIVE
ProteomicsOptimized Digestion Conditions for Membrane Protein Foot-printing and Mass Spectrometry Analysis
Integral membrane proteins (IMPs), which constitute 50–60% of drug targets, play essen-tial roles in numerous biological processes but remain underrepresented in conventional bottom-up and in structural proteomics owing to their hydrophobicity and resistance to proteolysis. Although advances in IMPs...
ORGANISM(S): Homo sapiens (Human) 
2026-07-02 | PXD072461 | Pride
Membrane protein  vitamin k epoxide reductase (vkor)  mass spectrometry  protein footprinting  filter-aided sample preparation (fasp) Membrane protein digestion 
UnknownImproved protease digestion conditions for membrane protein detection.
Not available
S-EPMC4739822 | biostudies-literature
TranscriptomicsProteolytic inactivation of the autoinhibitory prodomain is essential for the pro-tumorigenic function of membrane type-1 matrix metalloproteinase (MT1-MMP)
Invasive cancers employ pericellular proteolysis to breach the extracellular matrix and basement membrane barriers and invade the surrounding tissue. Pro-invasive, pro-tumorigenic MT1-MMP is the primary mediator of proteolytic events on the cancer cell surface. Cellular MT1-MMP is synthesized as a l...
ORGANISM(S): Homo sapiens 
2011-06-01 | E-GEOD-28655 | biostudies-arrayexpress
UnknownLess is More: Membrane Protein Digestion Beyond Urea-Trypsin Solution for Next-level Proteomics.
Not available
S-EPMC4563727 | biostudies-literature
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