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ProteomicsUniversal Solid-Phase Protein Preparation (USP3) for bottom-up and top-down proteomics
Selecting a sample preparation strategy for mass spectrometry-based proteomics is critical to the success of quantitative workflows. Here we present a universal, solid-phase protein preparation (USP3) method which is rapid, robust and scalable, facilitating high-throughput protein sample preparation...
ORGANISM(S): Homo sapiens (Human) 
2019-06-05 | PXD011169 | Pride
Top-down proteomics Universal solid-phase protein preparation Bottom-up proteomics Intact mass spectrometry 
ProteomicsTowards a universal sample preparation method for denaturing top-down proteomics of complex proteomes
A universal and standardized sample preparation method becomes vital for denaturing top-down proteomics (dTDP) to advance the scale and accuracy of proteoform delineation in complex biological systems. It needs to have high protein recovery, minimum bias, good reproducibility, and compatibility with...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2020-05-22 | PXD018248 | Pride
Histone Ptms Membrane ultrafiltration Chloroform-methanol precipitation Membrane proteins Sp3 Denaturing top-down proteomics Cze-ms/ms Sds Sample preparation 
ProteomicsProtein aggregation capture on microparticles enables multi-purpose proteomics sample preparation
Universal proteomics sample preparation is challenging due to the high heterogeneity of biological samples. Here we describe a novel mechanism that exploits the inherent instability of denatured proteins for non-specific immobilization on microparticles by protein aggregation capture. To demonstrate...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2019-03-05 | PXD011677 | Pride
Microparticles Mass spectrometry Secretomics Proteomics Sample preparation Phosphoproteomics Magnetic beads 
UnknownToward a Universal Sample Preparation Method for Denaturing Top-Down Proteomics of Complex Proteomes.
Not available
S-EPMC7542658 | biostudies-literature
UnknownUniversal Solid-Phase Reversible Sample-Prep for Concurrent Proteome and N-Glycome Characterization.
Not available
S-EPMC5440117 | biostudies-literature
UnknownUniversal Pretreatment Development for Low-input Proteomics Using Lauryl Maltose Neopentyl Glycol.
Not available
S-EPMC10999711 | biostudies-literature
ProteomicsLow-input proteomics using lauryl maltose neopentyl glycol
We developed a sample preparation method for low-input proteomics using lauryl maltose neopentyl glycol. Using the developed method, we performed proteome analysis of coIP samples.
ORGANISM(S): Homo Sapiens (human) 
2024-03-06 | PXD048100 | JPOST Repository
ProteomicsLow-input proteomics using lauryl maltose neopentyl glycol
We developed a sample preparation method for low-input proteomics using lauryl maltose neopentyl glycol. Using the developed method, we performed proteome analysis of 100ng of HEK293T proteins, coIP samples, and serum extracellular vesicles, and further challenged label-free single-cell proteomics o...
ORGANISM(S): Homo Sapiens (human) Bos Taurus 
2024-03-06 | PXD044605 | JPOST Repository
ProteomicsPrevention of mitochondrial proteotoxicity by formation of a chaperone-dependent protective shell around aggregated polypeptides
The potential proteotoxicity of mitochondrial aggregates in yeast cells is reduced by a sequestration of affected polypeptides into a mitochondrial protein quality control compartment (IMiQ). Based on the expression of an aggregation-prone protein in the mitochondrial matrix, we determined the effec...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2025-08-21 | PXD059828 | Pride
Mitochondria Hsp70 Chaperone Protein aggregation Proteostasis Yeast 
UnknownGetting Ready for Large-Scale Proteomics in Crop Plants.
Not available
S-EPMC9921824 | biostudies-literature
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