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ProteomicsQuantification of amyloid protein enrichment by mass spectrometry improves typing of amyloidosis
Amyloidosis typing is crucial to determine the best therapeutic strategy for patients. Since conventional histological techniques often fail, the identification of amyloid precursors by mass spectrometry became the new standard. However, without quantification, selecting the amyloid precursor from p...
ORGANISM(S): Homo sapiens (Human) 
2026-05-25 | PXD039814 | Pride
Proteomics Mass spectrometry Label-free quantification Amyloidosis typing 
ProteomicsPrecise diagnosis and typing of early-stage renal immunoglobulin-derived amyloidosis by label-free quantification of parallel reaction monitoring-based targeted proteomics
Untargeted proteomics based precise diagnosis and typing of amyloid deposits are crucial for guiding patient management. However, it may not be suitable for early-stage renal amyloidosis with minor damages. Here, we aimed to develop parallel reaction monitoring (PRM)-based targeted proteomics to ach...
ORGANISM(S): Homo sapiens (Human) 
2023-03-10 | PXD038265 | Pride
Laser microdissection Amyloidosis Kidney Parallel reaction monitoring Targeted proteomics 
ProteomicsMatrix-Assisted Laser Desorption Ionization Mass Spectrometry Imaging: a novel Tool for the Identification and Classification of Amyloidosis
Amyloidosis is a group of diseases caused by extracellular accumulation of fibrillar polypeptide aggregates. So far, diagnosis is performed by Congo red staining of tissue sections in combination with polarization microscopy. Subsequent identification of the causative protein by immunohistochemistry...
ORGANISM(S): Homo sapiens (Human) 
2017-10-16 | PXD005960 | Pride
Formalin-fixed and paraffin-embedded Amyloidosis Ion mobility separation Maldi ms imaging 
ProteomicsMS-based amyloidosis typing in FFPE tissue samples
Amyloidoses are characterized by the pathological deposition of non-degradable misfolded protein fibrils. Precise identification of the fibril-forming protein is crucial for prognosis and correct therapeutic intervention. Here, we present a reproduceable method for amyloid typing using relative quan...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2025-03-06 | MSV000097248 | MassIVE
ProteomicsInsight into the protein composition of immunoglobulin light chain deposits of eyelid, orbital, and conjunctival amyloidosis.
Amyloidosis is a disorder characterized by the formation of extracellular amyloid deposits. Immunoglobulin light-chain amyloidosis the most common form of amyloidosis can appear as a local disorder presented with mild symptoms or as a life threatening systemic disease. Identification of the protein...
ORGANISM(S): Homo sapiens (Human) 
2014-05-29 | PXD000743 | Pride
Mass spectrometry Orbit Amyloidosis Conjunctiva Laser capture microdissection Eyelid 
UnknownIncreasing the accuracy of proteomic typing by decellularisation of amyloid tissue biopsies.
Not available
S-EPMC5571436 | biostudies-literature
UnknownAmyloid detection and typing yield of skin biopsy in systemic amyloidosis and polyneuropathy.
Not available
S-EPMC10723241 | biostudies-literature
UnknownTyping of hereditary renal amyloidosis presenting with isolated glomerular amyloid deposition.
Not available
S-EPMC6929319 | biostudies-literature
UnknownHow to Image Cardiac Amyloidosis: A Practical Approach.
Not available
S-EPMC7148180 | biostudies-literature
UnknownNew developments in diagnosis, risk assessment and management in systemic amyloidosis.
Not available
S-EPMC7124973 | biostudies-literature
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