DnaJ/Hsc70 chaperone complexes control the extracellular release of neurodegenerative-associated proteins.
about
Roles of tau protein in health and disease.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesTau secretion is correlated to an increase of Golgi dynamics.Soluble phospho-tau from Alzheimer's disease hippocampus drives microglial degeneration.Expression and purification of tau protein and its frontotemporal dementia variants using a cleavable histidine tagProtein misfolding in neurodegenerative diseases: implications and strategies.Primary fibroblasts from CSPα mutation carriers recapitulate hallmarks of the adult onset neuronal ceroid lipofuscinosis.Possible Function of Molecular Chaperones in Diseases Caused by Propagating Amyloid Aggregates.Internalization, axonal transport and release of fibrillar forms of alpha-synuclein.Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds.Potential Modes of Intercellular α-Synuclein Transmission.Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism.Propagation of Tau aggregates.The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease.Neurons Export Extracellular Vesicles Enriched in Cysteine String Protein and Misfolded Protein Cargo.The Evidence for the Spread and Seeding Capacities of the Mutant Huntingtin Protein in in Vitro Systems and Their Therapeutic Implications.Extracellular Tau and Its Potential Role in the Propagation of Tau Pathology.HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.Enhanced tau pathology via RanBP9 and Hsp90/Hsc70 chaperone complexes.Tau Spreading Mechanisms; Implications for Dysfunctional Tauopathies.DNAJC5 facilitates USP19-dependent unconventional secretion of misfolded cytosolic proteins.Preparation of organotypic brain slice cultures for the study of Alzheimer's disease.Import and Export of Misfolded α-Synuclein.Targeting prion-like protein spreading in neurodegenerative diseases
P2860
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P2860
DnaJ/Hsc70 chaperone complexes control the extracellular release of neurodegenerative-associated proteins.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
DnaJ/Hsc70 chaperone complexes ...... enerative-associated proteins.
@en
type
label
DnaJ/Hsc70 chaperone complexes ...... enerative-associated proteins.
@en
prefLabel
DnaJ/Hsc70 chaperone complexes ...... enerative-associated proteins.
@en
P2093
P2860
P50
P356
P1433
P1476
DnaJ/Hsc70 chaperone complexes ...... generative-associated proteins
@en
P2093
Andrew R Stothert
April Darling
April Lussier
Bryce A Nordhues
Dale Chaput
Jeremy Baker
Jonathan J Sabbagh
Justin H Trotter
Lindsey Shelton
Mahnoor Kahn
P2860
P304
P356
10.15252/EMBJ.201593489
P407
P577
2016-06-03T00:00:00Z