Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration.
Amino Acid Sequence
Amyotrophic Lateral Sclerosis
/ genetics
Chromatography, Gel
Circular Dichroism
Cloning, Molecular
DNA-Binding Proteins
/ chemistry
Dynamic Light Scattering
Frontotemporal Lobar Degeneration
/ genetics
Humans
Mass Spectrometry
Neurodegenerative Diseases
/ genetics
Protein Folding
Protein Stability
Protein Structure, Quaternary
Recombinant Proteins
/ chemistry
Solubility
RNA binding protein
TDP-43 proteinophaties
neurodegenerative diseases
protein refolding
stress granules
Journal
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
ISSN: 1530-6860
Titre abrégé: FASEB J
Pays: United States
ID NLM: 8804484
Informations de publication
Date de publication:
10 2019
10 2019
Historique:
pubmed:
10
7
2019
medline:
2
6
2020
entrez:
10
7
2019
Statut:
ppublish
Résumé
The involvement of transactivation response (TAR) DNA-binding protein 43 (TDP-43) in neurodegenerative diseases was revealed in 2006, when it was first reported to be the main component of the intracellular inclusions in patients with amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration. After 12 yr it is not yet possible to purify to a reasonable yield and in a reproducible manner a stable full-length protein, which has limited so far the characterization of its structure, function, molecular interactors, and pathobiology. Using a novel protocol we have achieved the purification of the full-length TDP-43, with both a short pectate lyase B tag and a glutathione
Identifiants
pubmed: 31287959
doi: 10.1096/fj.201900474R
doi:
Substances chimiques
DNA-Binding Proteins
0
Recombinant Proteins
0
TARDBP protein, human
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM