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ProteomicsHDX-MS of Immobilized Staph Enterotoxin B with Neutralizing Serum
Elucidating the interactions that drive antigen recognition is central to understanding antibody-based protection and is vital for the rational design of immunogens. Often, structural knowledge of epitopes targeted by antibodies is derived from isolated studies of monoclonal antibodies, for which nu...
ORGANISM(S): Mus musculus (Mouse) 
2025-10-27 | PXD051156 | Pride
Hdx-ms Serum hdx Seb Immobilized hdx 
ProteomicsDefining the Structural Features of Complement-Active IgM: 3-state comparison
Immunoglobulin mu (IgM) is a class of mammalian antibodies that are critical for the early stages of adaptive immunity and are the most potent activators of the classical complement cascade. While the relationship between IgM and complement has been appreciated for decades, the structural transition...
ORGANISM(S): Mus musculus (Mouse) 
2025-04-02 | PXD056897 | Pride
Igm Hdx-ms Antibody-antigen interaction 
ProteomicsDefining the Structural Features of Complement-Active IgM: 3-state comparison of IgG
Immunoglobulin mu (IgM) is a class of mammalian antibodies that are critical for the early stages of adaptive immunity and are the most potent activators of the classical complement cascade. While the relationship between IgM and complement has been appreciated for decades, the structural transition...
ORGANISM(S): Mus musculus (Mouse) 
2025-04-02 | PXD056918 | Pride
Igm Hdx-ms Antibody-antigen interaction Igg 
ProteomicsDefining the Structural Features of Complement-Active IgM: Surface Ag linker comparison
Immunoglobulin mu (IgM) is a class of mammalian antibodies that are critical for the early stages of adaptive immunity and are the most potent activators of the classical complement cascade. While the relationship between IgM and complement has been appreciated for decades, the structural transition...
ORGANISM(S): Mus musculus (Mouse) 
2025-04-02 | PXD056670 | Pride
Igm Hdx-ms Antibody-antigen interaction 
ProteomicsHDX of SEB and Neutralizing mAbs
Elucidating the interactions that drive antigen recognition is central to understanding antibody-based protection and is vital for the rational design of immunogens. Often, structural knowledge of epitopes targeted by antibodies is derived from isolated studies of monoclonal antibodies, for which nu...
ORGANISM(S): Mus musculus (Mouse) 
2025-10-27 | PXD051141 | Pride
Hdx-ms Hydorgen deuterium exchange Seb 
ProteomicsGermline encoded residues dominate the interaction of a human monoclonal antibody with Decorin binding protein A (DbpA) of Borrelia burgdorferi
During the course of Lyme disease, humans mount a robust and sustained antibody response against dozens of Borrelia burgdorferi outer surface lipoproteins. Identifying which antibodies are associated with spirochete clearance and disease resolution is of paramount importance in therapeutic developme...
ORGANISM(S): Homo sapiens (Human) 
2025-07-28 | PXD062826 | Pride
Monoclonal Borrelia Dbpa Hdx-ms 
ProteomicsDistinct Perception Mechanisms of BACH1 Quaternary Structure Degrons by Two F-box Proteins under Oxidative Stress
Ubiquitin-dependent proteolysis regulates diverse cellular functions with high substrate specificity. The precision of this regulatory mechanism hinges on the ability of ubiquitin E3 ligases to decode the targets’ degradation signals, i.e. degrons, which canonically present as short linear motifs. H...
ORGANISM(S): Homo sapiens (Human) 
2025-12-29 | PXD053923 | Pride
Oxidative stress Ubiquitination Protein degradation Ubiquitin ligase Bach1 Fbxl17 Transcription repressor Fbxo22 Btb domain Scf Degron Cryo-em Hdx-ms 
ProteomicsDefining the Structural Features of Complement-Active IgM: 3-state comparison
Immunoglobulin mu (IgM) is a class of mammalian antibodies that are critical for the early stages of adaptive immunity and are the most potent activators of the classical complement cascade. While the relationship between IgM and complement has been appreciated for decades, the structural transition...
ORGANISM(S): Mus musculus (Mouse) 
2025-10-14 | PXD056697 | Pride
Igm Hdx-ms Antibody-antigen interaction 
ProteomicsChinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 2
Chinese Hamster Ovary (CHO) cells are frequently used to produce recombinant HIV envelope protein gp120. In this study, we characterized the CHO proteins that become co-purified with gp120 when lectin affinity chromatography is used. Many of co-purified CHO proteins identified were extracellular m...
ORGANISM(S): Cricetulus Griseus (ncbitaxon:10029) 
2018-01-25 | MSV000081975 | MassIVE
ProteomicsChinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 3
Chinese Hamster Ovary (CHO) cells are frequently used to produce recombinant HIV envelope protein gp120. In this study, we characterized the CHO proteins that become co-purified with gp120 when lectin affinity chromatography is used. Many of co-purified CHO proteins identified were extracellular m...
ORGANISM(S): Cricetulus Griseus (ncbitaxon:10029) 
2018-02-14 | MSV000082065 | MassIVE
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