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Large-scale isolation of protein N-terminal peptides from LysargiNase digests was achieved by one-step strong cation exchange chromatography with disposable and parallel-processable pipette-tip columns. Novel cleavage sites for signal or transit peptides and non-canonical translation initiation site...
ORGANISM(S): Homo Sapiens (human) 
Decoding protein C-termini is a challenging task in protein chemistry using conventional chemical/enzymatic approaches. With the rapid development in modern mass spectrometer, many advanced mass spectrometry (MS) based protein C-termini analysis approaches have been established. Although great progr...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) Caenorhabditis elegans 
2020-02-28 | PXD016317 | Pride
Two-dimensional (2D) liquid chromatography (LC)-tandem mass spectrometry (MS/MS) are typically employed for deep bottom-up proteomics, and the state-of-the-art 2D-LC-MS/MS has approached over 8,000 protein identifications (IDs) from mammalian cell lines or tissues in 1-3 days of mass spectrometer ti...
ORGANISM(S): Mus musculus (Mouse) 
2018-02-27 | PXD008432 | Pride
This dataset contains the raw data from the JASMS paper with the same title and DOI: 10.1007/s13361-012-0544-2. We compared the results of shotgun proteomic experiments of a trypsin digest of SUM52 cell lysate using 2D-LC fractionated (strong cation exchange and reversed phase of 6 SCX fractions) w...
ORGANISM(S): Homo sapiens (Human) 
2013-12-05 | PXD000596 | Pride
Chemical cross-linking in combination with mass spectrometry (XL-MS) has emerged as a useful method for structural elucidation of proteins and protein complexes. Efficient enrichment procedures are necessary to analyze cross-linked products due to their relatively low abundance. Currently, strong ca...
ORGANISM(S): Homo sapiens (Human) 
2022-06-16 | PXD023817 | Pride
A novel one-dimensional on-line pH gradient-eluted strong cation exchange (SCX)-nano-ESI-MS/MS method was developed for protein identification and tested with mixture of six standard proteins, total lysate of HuH7 and N2a cells, as well as membrane fraction of N2a cells. This method utilized an on-l...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2016-01-28 | PXD003438 | Pride
We report the proteomic analysis of the archetype B. burgdorferi B31 strain and two other strains (ND40, and JD-1) having different Borrelia pathotypes using strong cation exchange fractionation of proteolytic peptides followed by high-resolution, reversed phase capillary liquid chromatography coupl...
ORGANISM(S): Borreliella Burgdorferi (ncbitaxon:139) 
2020-05-29 | MSV000085503 | MassIVE
Protein methylation as one of the most important post-translational modifications of proteins has been under the spotlight due to its essential role in many important biological processes. To data, antibody-based enrichment strategy is the most used approach to enrich methylated peptides. Unfortunat...
ORGANISM(S): Homo Sapiens 
2021-10-18 | PXD029179 |
Development of an online peptide fractionation system comprising a multiphasic LC chip that integrates reversed phase and strong cation exchange chromatography upstream of the MS based on the multi-dimensional protein identification technology (mudPIT). Chips were assessed in terms of chromatographi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
HLA class Ι molecules on the cell surface enable CD8+ T lymphocytes to recognize cellular alterations in the form of antigens, including mutations, protein copy number alterations, aberrant post-translational modifications or pathogen proteins. At any given moment, tens of thousands of different sel...
ORGANISM(S): Homo sapiens (Human) 
2019-02-25 | PXD011257 | Pride
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