Sort   by:  
 Page size 
In this study, we profiled the precision N-glycoproteome of the murine peritoneal macrophage under different stimulation.
ORGANISM(S): Mus musculus (Mouse) 
2021-06-12 | PXD026629 | Pride
Prostate cancer is a leading cause of cancer-related deaths of men in the U.S. While localized disease is highly treatable by surgical resection and radiation, cancer that has metastasized remains incurable. Immune cells that primarily scavenge debris, promote prostate cancer angiogenesis and woun...
ORGANISM(S): Homo sapiens (Human) 
2017-03-31 | PXD005080 | Pride
In this work, we conducted an in-depth characterization of protein glycosylation including total glycoproteins and surface ones across different macrophage phenotypes using mass spectrometry (MS)-based proteomics. The global analysis of glycoproteins was performed using the boronic acid-conjugated d...
ORGANISM(S): Homo sapiens (Human) 
2024-08-08 | PXD053647 | Pride
Tuberculosis (TB) remains a prevalent and lethal infectious disease. The glycobiology associated with Mycobacterium tuberculosis infection of frontline alveolar macrophages is still unresolved. Herein, we investigated the regulation of protein N-glycosylation in human macrophages and their secreted ...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD005169 | Pride
In this study, we performed site-specific N-glycoproteomic analysis of THP-1 derived four M2 macrophage subtypes (M2a, M2b, M2c, and M2d) by StrucGP method combined with 2D-LC-MS/MS analysis, and revealed the distribution regularities and characters of N-glycans.
ORGANISM(S): Homo sapiens (Human) 
2025-12-23 | PXD048964 | Pride
Here, we present a simple and robust N-linked glycoproteome enrichment protocol optimized for deep coverage of the plasma membrane proteome. The procedure was applied to characterize the cell surface proteome of 15 standard laboratory human cell lines and three primary cell types. We observed signif...
ORGANISM(S): Homo sapiens (Human) 
2017-03-27 | PXD005846 | Pride
Glycosylation, the posttranslational linking of sugar molecules to proteins, is notoriously altered during tumor transformation. More specifically in carcinomas, GalNAc-type O-glycosylation, is characterized by biosynthetically immature truncated glycans present on the cancer cell surface which prof...
ORGANISM(S): Homo sapiens (Human) 
2020-10-19 | PXD017510 | Pride
Targeting tumor-associated macrophages (TAMs) holds great promise for cancer immunotherapy. Surface glycoproteins in macrophages regulate their interactions with tumor cells and represent emerging therapeutic targets. Given the crucial roles of protein glycosylation in immune function and cancer, we...
ORGANISM(S): Homo sapiens (Human) 
2026-08-22 | PXD071681 | Pride
Sort   by:  
 Page size