NMR assignments for the C-terminal domain of human TDP-43

Solid-State NMR Reveals the Structural Transformation of the TDP-43 Amyloidogenic Region upon Fibrillation

(2020) Xiao-Feng Zhuo et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

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

Cellular stress leads to the formation of membraneless stress assemblies in eukaryotic cells

(2019) Wessel van Leeuwen et al.   TRAFFIC

A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing

(2018) Ailin Wang et al.   EMBO JOURNAL

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

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

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

(2017) Tariq Afroz et al.   Nature Communications

The TDP-43 N-terminal domain structure at high resolution

(2016) Miguel Mompeán et al.   FEBS Journal

The Nearest-Neighbor Effect on Random-Coil NMR Chemical Shifts Demonstrated Using a Low-Complexity Amino-Acid Sequence

(2016) Tsai-Chen Chen et al.   PROTEIN AND PEPTIDE LETTERS

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

NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy

(2014) Woonghee Lee et al.   BIOINFORMATICS

TDP-43 aggregation in neurodegeneration: Are stress granules the key?

(2012) Colleen M. Dewey et al.   BRAIN RESEARCH

The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies

(2012) I.-Fan Wang et al.   Nature Communications

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

Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo

(2009) A. D'Ambrogio et al.   NUCLEIC ACIDS RESEARCH