Sort   by:  
 Page size 
We investigated the N- and C-terminome of the LCs proteoforms in fibrils extracted from the hearts of a patient affected by AL amyloidosis, using a proteomic approach based on N- and C-terminal residues derivatization, followed by mapping of fragmentation sites on the structures of fibrillar LCs
ORGANISM(S): Homo sapiens (Human) 
2024-07-02 | PXD049301 | Pride
In this study we aimed to provide a detailed comparative description of the fragmentation sites of amyloid LCs in multiple organs of an individual patient.
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD025185 | Pride
Amyloid fibrils are polymeric structures originating from aggregation of misfolded proteins. In vivo, proteolysis may modulate amyloidogenesis and fibril stability. In light chain (AL) amyloidosis, fragmented light chains (LCs) are abundant components of amyloid deposits; however, site and timing of...
ORGANISM(S): Homo sapiens (Human) 
2020-10-15 | PXD020858 | Pride
We present the 3.3 Å cryo-EM structure of an AA amyloid extracted post-mortem from the diseased kidney of a DSH cat with renal failure. The structure reveals a cross-beta architecture assembled from two 76-residue long proto-filaments. Despite >70% sequence homology to mouse and human SAA, the cat S...
ORGANISM(S): Felis catus (Cat) (Felis silvestris catus) 
2022-11-18 | PXD035851 | Pride
we investigated the N-glycosylation of the amyloid fibrils extracted from the heart of a patient affected by AL amyloidosis, using a proteomic approach to evaluate indirectly the presence of glycans in immunoglobulin light chains.
ORGANISM(S): Homo sapiens (Human) 
2024-07-02 | PXD049369 | Pride
Sort   by:  
 Page size