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ProteomicsTop-down mass spectrometry analysis of capsid proteins of recombinant adeno-associated virus using multiple ion activations and proton transfer charge reduction
Here, we present our investigation of the viral proteins of the capsid of adeno-associated viruses via top-down mass spectrometry on the LC timescale. Characterization was improved through the use of proton transfer charge reduction
ORGANISM(S): Human Aav 
2024-06-14 | MSV000095045 | MassIVE
ProteomicsOrbitrap mass spectrometry and high-field asymmetric waveform ion mobility spectrometry (FAIMS) enable the indepth analysis of human serum proteoforms
In this study, we describe a straightforward protocol for intact proteoform sample preparation based on depletion of albumin and immunoglobulins followed by simplified fractionation of remaining serum proteins via polyacrylamide gel electrophoresis. After molecular weight-based fractionation, we sup...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-08-02 | MSV000092574 | MassIVE
ProteomicsOrbitrap mass spectrometry and high-field asymmetric waveform ion mobility spectrometry (FAIMS) enable the in-depth analysis of human serum proteoforms
After molecular weight-based fractionation, we supplemented the traditional liquid chromatography tandem mass spectrometry (LC-MS2) data acquisition with high-field asymmetric waveform ion mobility spectrometry (FAIMS), which served as an additional separation dimension to further simplify serum pro...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-02-16 | MSV000091309 | MassIVE
ProteomicsTargeted Quantification of Proteoforms in Human Samples by Proteoform Reaction Monitoring
Here, we describe an approach based on the principle of PRM for the measurement of intact proteoforms by targeted top-down proteomics termed Proteoform Reaction Monitoring (PfRM). We explore the ability of our method to circumvent traditional limitations of top-down proteomics such as sensitivity an...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-04-21 | MSV000091774 | MassIVE
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