TDP-43 aggregation inside micronuclei reveals a potential mechanism for protein inclusion formation in ALS
Published 2019 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
TDP-43 aggregation inside micronuclei reveals a potential mechanism for protein inclusion formation in ALS
Authors
Keywords
-
Journal
Scientific Reports
Volume 9, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2019-12-27
DOI
10.1038/s41598-019-56483-y
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Adult hippocampal neurogenesis is abundant in neurologically healthy subjects and drops sharply in patients with Alzheimer’s disease
- (2019) Elena P. Moreno-Jiménez et al. NATURE MEDICINE
- RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43
- (2019) Elsa Zacco et al. JOURNAL OF MOLECULAR BIOLOGY
- PARylation regulates stress granule dynamics, phase separation, and neurotoxicity of disease-related RNA-binding proteins
- (2019) Yongjia Duan et al. CELL RESEARCH
- RNA buffers the phase separation behavior of prion-like RNA binding proteins
- (2018) Shovamayee Maharana et al. SCIENCE
- Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization
- (2018) Leeanne McGurk et al. MOLECULAR CELL
- A novel overlapping NLS/NES region within the PH domain of Rho Guanine Nucleotide Exchange Factor (RGNEF) regulates its nuclear-cytoplasmic localization
- (2018) Michael V. Tavolieri et al. EUROPEAN JOURNAL OF CELL BIOLOGY
- Rho guanine nucleotide exchange factor (RGNEF) is a prosurvival factor under stress conditions
- (2017) Kevin Cheung et al. MOLECULAR AND CELLULAR NEUROSCIENCE
- Fate of micronuclei and micronucleated cells
- (2017) Henning Hintzsche et al. MUTATION RESEARCH-REVIEWS IN MUTATION RESEARCH
- Amyotrophic lateral sclerosis-linked mutations increase the viscosity of liquid-like TDP-43 RNP granules in neurons
- (2017) Pallavi P. Gopal et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Rebuilding Chromosomes After Catastrophe: Emerging Mechanisms of Chromothripsis
- (2017) Peter Ly et al. TRENDS IN CELL BIOLOGY
- Granulostasis: Protein Quality Control of RNP Granules
- (2017) Simon Alberti et al. Frontiers in Molecular Neuroscience
- Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization
- (2015) Amandine Molliex et al. CELL
- The I-TASSER Suite: protein structure and function prediction
- (2015) Jianyi Yang et al. NATURE METHODS
- Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?
- (2015) Anaïs Aulas et al. Frontiers in Cellular Neuroscience
- RNA-binding proteins as molecular links between cancer and neurodegeneration
- (2014) Danae Campos-Melo et al. BIOGERONTOLOGY
- RNA metabolism in ALS: When normal processes become pathological
- (2014) Cristian A. Droppelmann et al. Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration
- Stages of pTDP-43 pathology in amyotrophic lateral sclerosis
- (2013) Johannes Brettschneider et al. ANNALS OF NEUROLOGY
- Altered Ribostasis: RNA-Protein Granules in Degenerative Disorders
- (2013) Mani Ramaswami et al. CELL
- Catastrophic Nuclear Envelope Collapse in Cancer Cell Micronuclei
- (2013) Emily M. Hatch et al. CELL
- Stress granules as crucibles of ALS pathogenesis
- (2013) Yun R. Li et al. JOURNAL OF CELL BIOLOGY
- Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
- (2013) Hong Joo Kim et al. NATURE
- Co-aggregation of RNA binding proteins in ALS spinal motor neurons: evidence of a common pathogenic mechanism
- (2012) Brian A. Keller et al. ACTA NEUROPATHOLOGICA
- The RNA-binding motif 45 (RBM45) protein accumulates in inclusion bodies in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) patients
- (2012) Mahlon Collins et al. ACTA NEUROPATHOLOGICA
- TDP-43 aggregation in neurodegeneration: Are stress granules the key?
- (2012) Colleen M. Dewey et al. BRAIN RESEARCH
- Metabolic Dysfunction in Alzheimers Disease and Related Neurodegenerative Disorders
- (2012) Huan Cai et al. Current Alzheimer Research
- Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis
- (2012) Julien Couthouis et al. HUMAN MOLECULAR GENETICS
- Regulated protein aggregation: stress granules and neurodegeneration
- (2012) Benjamin Wolozin Molecular Neurodegeneration
- Rho guanine nucleotide exchange factor is an NFL mRNA destabilizing factor that forms cytoplasmic inclusions in amyotrophic lateral sclerosis
- (2012) Cristian A. Droppelmann et al. NEUROBIOLOGY OF AGING
- Massive Genomic Rearrangement Acquired in a Single Catastrophic Event during Cancer Development
- (2011) Philip J. Stephens et al. CELL
- An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
- (2011) Weirui Guo et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- A yeast functional screen predicts new candidate ALS disease genes
- (2011) J. Couthouis et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Impaired glucose tolerance in patients with amyotrophic lateral sclerosis
- (2010) Pierre-Francois Pradat et al. Amyotrophic Lateral Sclerosis
- TDP-43 Is Directed to Stress Granules by Sorbitol, a Novel Physiological Osmotic and Oxidative Stressor
- (2010) C. M. Dewey et al. MOLECULAR AND CELLULAR BIOLOGY
- Cellular Metabolic Stress: Considering How Cells Respond to Nutrient Excess
- (2010) Kathryn E. Wellen et al. MOLECULAR CELL
- Association of micronucleus frequency with neurodegenerative diseases
- (2010) L. Migliore et al. MUTAGENESIS
- I-TASSER: a unified platform for automated protein structure and function prediction
- (2010) Ambrish Roy et al. Nature Protocols
- Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue
- (2010) Liqun Liu-Yesucevitz et al. PLoS One
- Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
- (2009) Manuela Neumann et al. ACTA NEUROPATHOLOGICA
- TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity
- (2009) Brian S. Johnson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- TDP-43 is recruited to stress granules in conditions of oxidative insult
- (2009) Claudia Colombrita et al. JOURNAL OF NEUROCHEMISTRY
- The evidence for altered RNA metabolism in amyotrophic lateral sclerosis (ALS)
- (2009) Michael J. Strong JOURNAL OF THE NEUROLOGICAL SCIENCES
- Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6
- (2009) C. Vance et al. SCIENCE
- Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis
- (2009) T. J. Kwiatkowski et al. SCIENCE
- High metabolic level in patients with familial amyotrophic lateral sclerosis
- (2008) Benoit Funalot et al. Amyotrophic Lateral Sclerosis
- The leucine-rich repeat structure
- (2008) J. Bella et al. CELLULAR AND MOLECULAR LIFE SCIENCES
- Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS
- (2008) Yuki Inukai et al. FEBS LETTERS
Publish 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 MoreFind the ideal target journal for your manuscript
Explore over 38,000 international journals covering a vast array of academic fields.
Search