The Molecular Chaperone DNAJB6, but Not DNAJB1, Suppresses the Seeded Aggregation of Alpha-Synuclein in Cells
Published 2019 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
The Molecular Chaperone DNAJB6, but Not DNAJB1, Suppresses the Seeded Aggregation of Alpha-Synuclein in Cells
Authors
Keywords
-
Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 20, Issue 18, Pages 4495
Publisher
MDPI AG
Online
2019-09-11
DOI
10.3390/ijms20184495
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Dysfunction of Cellular Proteostasis in Parkinson’s Disease
- (2019) Šárka Lehtonen et al. Frontiers in Neuroscience
- Conserved S/T-residues of the human chaperone DNAJB6 are required for effective inhibition of Aβ42 amyloid fibril formation
- (2018) Cecilia Månsson et al. BIOCHEMISTRY
- Parkinson’s disease-linked DNAJC13 mutation aggravates alpha-synuclein-induced neurotoxicity through perturbation of endosomal trafficking
- (2018) Shun Yoshida et al. HUMAN MOLECULAR GENETICS
- α-synuclein aggregation and its modulation
- (2017) Dhiman Ghosh et al. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
- Zeroing in on neurodegenerative α-synuclein
- (2017) Katie Kingwell NATURE REVIEWS DRUG DISCOVERY
- DNAJ Proteins in neurodegeneration: essential and protective factors
- (2017) Christina Zarouchlioti et al. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
- SUMOylation and ubiquitination reciprocally regulate α-synuclein degradation and pathological aggregation
- (2017) Ruth Rott et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Exploring Braak’s Hypothesis of Parkinson’s Disease
- (2017) Carmen D. Rietdijk et al. Frontiers in Neurology
- The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress α-synuclein aggregation
- (2017) Francesco A. Aprile et al. Scientific Reports
- Genetics of Parkinson's disease
- (2016) Christina M. Lill MOLECULAR AND CELLULAR PROBES
- The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model
- (2016) Vaishali Kakkar et al. MOLECULAR CELL
- Versatile members of the DNAJ family show Hsp70 dependent anti-aggregation activity on RING1 mutant parkin C289G
- (2016) Vaishali Kakkar et al. Scientific Reports
- A Rational Design Strategy for the Selective Activity Enhancement of a Molecular Chaperone toward a Target Substrate
- (2015) Francesco A. Aprile et al. BIOCHEMISTRY
- Parkinson's disease
- (2015) Lorraine V Kalia et al. LANCET
- Human Hsp70 Disaggregase Reverses Parkinson’s-Linked α-Synuclein Amyloid Fibrils
- (2015) Xuechao Gao et al. MOLECULAR CELL
- Polyglutamine aggregation in Huntington's disease and spinocerebellar ataxia type 3: similar mechanisms in aggregate formation
- (2015) K. Seidel et al. NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY
- Evaluation of the amyloid beta-GFP fusion protein as a model of amyloid beta peptides-mediated aggregation: a study of DNAJB6 chaperone
- (2015) Rasha M. Hussein et al. Frontiers in Molecular Neuroscience
- Interaction of the Molecular Chaperone DNAJB6 with Growing Amyloid-beta 42 (Aβ42) Aggregates Leads to Sub-stoichiometric Inhibition of Amyloid Formation
- (2014) Cecilia Månsson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Proteopathic tau seeding predicts tauopathy in vivo
- (2014) B. B. Holmes et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Alpha-synuclein spreading in Parkinson’s disease
- (2014) Ariadna Recasens et al. Frontiers in Neuroanatomy
- Models of α-synuclein aggregation in Parkinson’s disease
- (2014) Rosa María Giráldez-Pérez et al. Acta Neuropathologica Communications
- DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios
- (2013) Cecilia Månsson et al. CELL STRESS & CHAPERONES
- DNAJ Proteins and Protein Aggregation Diseases
- (2013) Vaishali Kakkar et al. CURRENT TOPICS IN MEDICINAL CHEMISTRY
- DNAJC13 mutations in Parkinson disease
- (2013) Carles Vilariño-Güell et al. HUMAN MOLECULAR GENETICS
- Applying chaperones to protein-misfolding disorders: Molecular chaperones against α-synuclein in Parkinson's disease
- (2013) Ali Chaari et al. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
- The DNAJB6 and DNAJB8 Protein Chaperones Prevent Intracellular Aggregation of Polyglutamine Peptides
- (2013) Judith Gillis et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Genome engineering using the CRISPR-Cas9 system
- (2013) F Ann Ran et al. Nature Protocols
- The prion hypothesis in Parkinson's disease: Braak to the future
- (2013) Naomi P Visanji et al. Acta Neuropathologica Communications
- HSP DNAJB8 Controls Tumor-Initiating Ability in Renal Cancer Stem-like Cells
- (2012) S. Nishizawa et al. CANCER RESEARCH
- Molecular Chaperones, Alpha-Synuclein, and Neurodegeneration
- (2012) Stephan N. Witt MOLECULAR NEUROBIOLOGY
- The many faces of α-synuclein: from structure and toxicity to therapeutic target
- (2012) Hilal A. Lashuel et al. NATURE REVIEWS NEUROSCIENCE
- Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death
- (2011) Laura A. Volpicelli-Daley et al. NEURON
- A DNAJB Chaperone Subfamily with HDAC-Dependent Activities Suppresses Toxic Protein Aggregation
- (2010) Jurre Hageman et al. MOLECULAR CELL
- Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones
- (2009) Daniel W. Summers et al. TRENDS IN BIOCHEMICAL SCIENCES
- Computational analysis of the human HSPH/HSPA/DNAJ family and cloning of a human HSPH/HSPA/DNAJ expression library
- (2008) Jurre Hageman et al. CELL STRESS & CHAPERONES
- DnaJB6 is present in the core of Lewy bodies and is highly up-regulated in parkinsonian astrocytes
- (2008) P.F. Durrenberger et al. JOURNAL OF NEUROSCIENCE RESEARCH
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExplorePublish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn More