Phe-Gly motifs drive fibrillization of TDP-43’s prion-like domain condensates
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Title
Phe-Gly motifs drive fibrillization of TDP-43’s prion-like domain condensates
Authors
Keywords
Amyloid proteins, Fluorescence imaging, DNA-binding proteins, Electron cryo-microscopy, Imidazole, RNA structure, Centrifugation, Urea
Journal
PLOS BIOLOGY
Volume 19, Issue 4, Pages e3001198
Publisher
Public Library of Science (PLoS)
Online
2021-04-29
DOI
10.1371/journal.pbio.3001198
References
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Note: Only part of the references are listed.- TDP-43 α-helical structure tunes liquid–liquid phase separation and function
- (2020) Alexander E. Conicella et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Valence and patterning of aromatic residues determine the phase behavior of prion-like domains
- (2020) Erik W. Martin et al. SCIENCE
- Optogenetic modulation of TDP-43 oligomerization accelerates ALS-related pathologies in the spinal motor neurons
- (2020) Kazuhide Asakawa et al. Nature Communications
- Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death
- (2019) Fatima Gasset-Rosa et al. NEURON
- The role of liquid-liquid phase separation in aggregation of the TDP-43 low complexity domain
- (2019) W. Michael Babinchak et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report
- (2019) Peter T Nelson et al. BRAIN
- Chronic optogenetic induction of stress granules is cytotoxic and reveals the evolution of ALS-FTD pathology
- (2019) Peipei Zhang et al. eLife
- Cryo-EM structures of four polymorphic TDP-43 amyloid cores
- (2019) Qin Cao et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly
- (2019) Xinrui Gui et al. Nature Communications
- TDP-43 Regulates Coupled Dendritic mRNA Transport-Translation Processes in Co-operation with FMRP and Staufen1
- (2019) Jen-Fei Chu et al. Cell Reports
- The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43
- (2018) Hao-Ru Li et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex
- (2018) Miguel Mompeán et al. CELL
- TAR DNA-binding protein 43 (TDP-43) liquid–liquid phase separation is mediated by just a few aromatic residues
- (2018) Hao-Ru Li et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Nuclear pores: the gate to neurodegeneration
- (2018) Nan Li et al. NATURE NEUROSCIENCE
- TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
- (2018) Ching-Chieh Chou et al. NATURE NEUROSCIENCE
- TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle
- (2018) Thomas O. Vogler et al. NATURE
- TDP-43 shapeshifts to encipher FTD severity
- (2018) Edward M. Barbieri et al. NATURE NEUROSCIENCE
- TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates
- (2018) Florent Laferrière et al. NATURE NEUROSCIENCE
- Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes
- (2017) Wei Qiang et al. NATURE
- The TDP-43 N-terminal domain structure at high resolution
- (2016) Miguel Mompeán et al. FEBS Journal
- Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
- (2016) Marielle Aulikki Wälti et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain
- (2016) Alexander E. Conicella et al. STRUCTURE
- ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
- (2016) Liangzhong Lim et al. PLOS BIOLOGY
- An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds
- (2016) Miguel Mompeán 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
- A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
- (2015) Avinash Patel et al. CELL
- NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy
- (2014) Woonghee Lee et al. BIOINFORMATICS
- Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue
- (2013) Jun-Xia Lu et al. CELL
- Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion
- (2013) Lei-Lei Jiang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Signals from the lysosome: a control centre for cellular clearance and energy metabolism
- (2013) Carmine Settembre et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
- (2013) Peter J Lukavsky et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
- (2011) Magnus Kjaergaard et al. JOURNAL OF BIOMOLECULAR NMR
- Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH
- (2011) Magnus Kjaergaard et al. JOURNAL OF BIOMOLECULAR NMR
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