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ProteomicsConformational differences in the light chain constant domain of immunoglobulin G and free light chain may influence proteolysis in AL amyloidosis
Immunoglobulin light chain amyloidosis (AL) is a life-threatening disease caused by the deposition of monoclonal light chain (LC) and its fragments containing variable (VL) and portions of constant (CL) domains. AL patients feature either monoclonal free LCs circulating as covalent and noncovalent h...
ORGANISM(S): Homo sapiens (Human) 
2025-12-08 | PXD055570 | Pride
Igg  amyloid light chain hdx-ms  al amyloidosis  hydrogen/deuterium exchange mass spectrometry 
GenomicsRNA-based full length immunoglobulin light chain sequencing reveals lambda constant domain mutations with potential implications for thermodynamic stability in light chain amyloidosis
RNA-based full length immunoglobulin light chain sequencing
PRJEB109785 | ENA
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 
TranscriptomicsHigh throughput sequencing of immunoglobulin (Ig) heavy (IgH) and light (IgL) chain repertoires
We used 454 sequencing to assess the repertoire of B cell subsets from bone marrow, spleen, and small intestinal lamina propria from two mouse strains. We used a RAG2-GFP reporter mouse strain (129Sve background) to isolate CD19+ RAG2+ B lineage cells from bone marrow and small intestinal lamina pro...
ORGANISM(S): Mus musculus 
2013-07-16 | E-GEOD-48870 | biostudies-arrayexpress
ProteomicsHelical superstructures between amyloid and collagen VI in heart derived fibrils from a patient with Light Chain Amyloidosis
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
Immunoglobulin light chains  n-glycosylation  amyloid fibrils 
UnknownComparison of serum free light chain and urine electrophoresis for the detection of the light chain component of monoclonal immunoglobulins in light chain and intact immunoglobulin multiple myeloma.
Not available
S-EPMC4815727 | biostudies-literature
ProteomicsRNA-based full length immunoglobulin light chain sequencing reveals lambda constant domain mutations with potential implications for thermodynamic stability in light chain amyloidosis
Background: Systemic light chain amyloidosis is a protein misfolding disorder characterized by deposition of clonal immunoglobulin light chains in vital organs. To date, little is known about the contribution of light chain constant domain mutations in thermodynamic stability and amyloidogenicity.Me...
ORGANISM(S): Homo sapiens (Human) 
2026-05-06 | PXD077140 | Pride
UnknownMutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis.
Not available
S-EPMC2664898 | biostudies-literature
UnknownSerological Immunoglobulin-Free Light Chain Profile in Myasthenia Gravis Patients.
Not available
S-EPMC5889870 | biostudies-literature
UnknownConformational Differences in the Light Chain Constant Domain of Immunoglobulin G and Free Light Chain May Influence Proteolysis in AL Amyloidosis.
Not available
S-EPMC11636358 | biostudies-literature
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