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MASP-3 is the third protease of the lectin pathway of the complement system, but its biological function has remained obscure. To elucidate its role in complement activation, we developed a specific MASP-3 inhibitor (named TFMI-3). In this work we unambiguously demonstrate that MASP-3 acts as the ex...
ORGANISM(S): Homo sapiens (Human) 
2016-08-24 | PXD003666 | Pride
Spatial proteomics at whole-tissue level provides critical insights into region-specific biological regulations but remains challenging. Previously, we introduced the Micro-scaffold Assisted Spatial Proteomics (MASP) technique, permitting whole-tissue mapping. While promising, this prototype require...
ORGANISM(S): Mus musculus (Mouse) 
2026-08-24 | PXD068767 | Pride
Quantitative protein mapping on whole-tissue levels provides important insights into the spatially-organized regulatory processes/networks related to diseases and therapy, but remains a tremendous challenge. We describe a micro-scaffold assisted spatial proteomics(MASP) method, based on precise tiss...
ORGANISM(S): Mus musculus (Mouse) 
2023-03-11 | PXD037041 | Pride
Transcriptional profiling of human umbilical vein endothelial cells, treated with MASP-1, thrombin, LPS, histamine, TNFalpha, MASP-1+SB203580 (p38-MAPK inhibitor) or MASP-1+Bay-117082 (NFKB inhibitor). Goal was to determine the effect of MASP-1 on HUVECs, to compare this with the effect of other end...
ORGANISM(S): Homo sapiens 
2017-09-14 | GSE98114 | GEO
Transcriptome analysis of inflammation-related gene expression in endothelial cells activated by complement MASP-1
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