Sort   by:  
 Page size 
DSSO as linker, study of protein-protein interaction by LC-MSMS
ORGANISM(S): Streptococcus pyogenes STAB901 
2020-04-15 | PXD012466 | Pride
DSSO as linker, study of protein-protein interaction by LC-MSMS
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD019713 | Pride
The associated files are mass spec data from size exclusion chromatography fractions that were subsequently crosslinked with DSSO. The starting material was a native extract prepared from soy sprouts (Glycine max). The mass spectrometry used a data-dependent MS2-MS3 method to identify crosslinks.
ORGANISM(S): Glycine max 
2019-10-28 | PXD013704 | Pride
Cross-linking mass spectrometry (XL-MS) has become a valuable tool for investigating the structural morphology and plasticity of proteins. Traditional cross-linkers contain two N-hydroxy succinimide (NHS) esters that mainly react with lysine residues. In this work, we optimized the in-solution react...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2026-03-30 | PXD069252 | Pride
The project aimed to profile the cell surface proteins of Nomo-1 (AML cell line) using structural surfaceomics for identification of protein conformation-based cancer antigens thereby expanding the toolkit for cancer target discovery for immunotherapeutic targeting. To achieve the goal, cell surface...
ORGANISM(S): Homo sapiens (Human) 
2023-10-04 | PXD035589 | Pride
Here we use an optimization cross-linking mass spectrometry (XL-MS) pipeline for the structural characterization of a dynamic HIV-host protein complex. Using DSSO-based XL-MS analysis, residue-protein proximity restraints based on functional genetics, and integrative modeling, we define the structu...
ORGANISM(S): Homo sapiens (Human) Human immunodeficiency virus 
2021-11-03 | PXD025391 | Pride
DSSO as linker, study of protein-protein interaction by LC-MSMS
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD019868 | Pride
DSSO as linker, study of protein-protein interaction by LC-MSMS
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD019944 | Pride
Chemical cross-linking/mass spectrometry (XL-MS) has emerged as a complementary tool for mapping interaction sites within protein networks as well as gaining moderate-resolution native structurale insight with minimal interference. XL-MS technology mostly relies on chemoselective reactions (crosslin...
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD051742 | Pride
Human A2M was cross-linked with DSSO in its native, methylamine-treated, and trypsin-cleaved conformations. The monomer, dimer, and tetramer SDS-PAGE gel bands of native A2M were analyzed by in-gel digest. Total protein digests of all three conformations were analyzed and compared.
ORGANISM(S): Homo sapiens (Human) 
2021-05-21 | PXD019101 | Pride
Sort   by:  
 Page size