Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis.
Amino Acid Sequence
Amyloid
/ chemistry
Chromatography, High Pressure Liquid
Electrophoresis, Gel, Two-Dimensional
Humans
Immunoglobulin Light Chains
/ chemistry
Immunoglobulin Light-chain Amyloidosis
/ metabolism
Myocardium
/ metabolism
Peptides
/ analysis
Protein Structure, Secondary
Protein Structure, Tertiary
Proteolysis
Tandem Mass Spectrometry
amyloid
amyloid fibrils
cardiomyopathy
fibril
mass spectrometry (MS)
protein aggregation
protein conformation
protein structure
proteolysis
proteomics
structural biology
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
04 12 2020
04 12 2020
Historique:
received:
15
03
2020
revised:
04
09
2020
pubmed:
22
9
2020
medline:
5
5
2021
entrez:
21
9
2020
Statut:
ppublish
Résumé
Amyloid fibrils are polymeric structures originating from aggregation of misfolded proteins.
Identifiants
pubmed: 32952127
pii: S0021-9258(17)50476-7
doi: 10.1074/jbc.RA120.013461
pmc: PMC7864057
pii:
doi:
Substances chimiques
Amyloid
0
Immunoglobulin Light Chains
0
Peptides
0
Banques de données
PDB
['6MG4', '5MUH']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
16572-16584Informations de copyright
© 2020 Lavatelli et al.
Déclaration de conflit d'intérêts
Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.
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