Protonation–Deprotonation Switch Controls the Amyloid-like Misfolding of Nucleic-Acid-Binding Domains of TDP-43

Mapping OMIM Disease–Related Variations on Protein Domains Reveals an Association Among Variation Type, Pfam Models, and Disease Classes

(2021) Castrense Savojardo et al.   Frontiers in Molecular Biosciences

A pH-dependent protein stability switch coupled to the perturbed pKa of a single ionizable residue

(2021) Prajna Mishra et al.   BIOPHYSICAL CHEMISTRY

Early Metastable Assembly during the Stress-Induced Formation of Worm-like Amyloid Fibrils of Nucleic Acid Binding Domains of TDP-43

(2020) Meenakshi Pillai et al.   BIOCHEMISTRY

RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43

(2019) Jacob R. Mann et al.   NEURON

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

The debated toxic role of aggregated TDP-43 in amyotrophic lateral sclerosis: a resolution in sight?

(2019) Rudolf C Hergesheimer et al.   BRAIN

The protonation state of an evolutionarily conserved histidine modulates domainswapping stability of FoxP1

(2019) Exequiel Medina et al.   Scientific Reports

Structural Insights Into TDP-43 and Effects of Post-translational Modifications

(2019) Liberty François-Moutal et al.   Frontiers in Molecular Neuroscience

TDP-43 regulates the alternative splicing of hnRNP A1 to yield an aggregation-prone variant in amyotrophic lateral sclerosis

(2018) Jade-Emmanuelle Deshaies et al.   BRAIN

Phase separation of a yeast prion protein promotes cellular fitness

(2018) Titus M. Franzmann et al.   SCIENCE

Different Material States of Pub1 Condensates Define Distinct Modes of Stress Adaptation and Recovery

(2018) Sonja Kroschwald et al.   Cell Reports

Aggregation-phase diagrams of β2-microglobulin reveal temperature and salt effects on competitive formation of amyloids versus amorphous aggregates

(2018) Masayuki Adachi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Physiologically Important Electrolytes as Regulators of TDP-43 Aggregation and Droplet-Phase Behavior

(2018) Yulong Sun et al.   BIOCHEMISTRY

The Folding and Aggregation Energy Landscapes of Tethered RRM Domains of Human TDP-43 Are Coupled via a Metastable Molten Globule-like Oligomer

(2018) Meenakshi Pillai et al.   BIOCHEMISTRY

An Alternatively Packed Dry Molten Globule-like Intermediate in the Native State Ensemble of a Multidomain Protein

(2017) Prajna Mishra et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Pathology of Neurodegenerative Diseases

(2017) Brittany N. Dugger et al.   Cold Spring Harbor Perspectives in Biology

Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates

(2017) Cyrille Garnier et al.   Scientific Reports

The N-terminal dimerization is required for TDP-43 splicing activity

(2017) Lei-Lei Jiang et al.   Scientific Reports

The hnRNP family: insights into their role in health and disease

(2016) Thomas Geuens et al.   HUMAN GENETICS

Unraveling the Molecular Mechanism of pH-Induced Misfolding and Oligomerization of the Prion Protein

(2016) Jogender Singh et al.   JOURNAL OF MOLECULAR BIOLOGY

Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins

(2016) Antonia Ratti et al.   JOURNAL OF NEUROCHEMISTRY

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

A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy

(2016) Matthias Christoph Munder et al.   eLife

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

The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids

(2014) P.-H. Kuo et al.   NUCLEIC ACIDS RESEARCH

TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA

(2014) Haina Qin et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Filament formation by metabolic enzymes is a specific adaptation to an advanced state of cellular starvation

(2014) Ivana Petrovska et al.   eLife

Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

(2013) Peter J Lukavsky et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

(2013) Shuo-Chien Ling et al.   NEURON

Maximum Allowed Solvent Accessibilites of Residues in Proteins

(2013) Matthew Z. Tien et al.   PLoS One

TDP-43 in central nervous system development and function: clues to TDP-43-associated neurodegeneration

(2012) Chantelle F. Sephton et al.   BIOLOGICAL CHEMISTRY

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

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

Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)

(2012) Eva Bentmann et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates

(2012) Sarah J. Parker et al.   NEUROCHEMISTRY INTERNATIONAL

TDP-43 pathological changes in early onset familial and sporadic Alzheimer’s disease, late onset Alzheimer’s disease and Down’s Syndrome: association with age, hippocampal sclerosis and clinical phenotype

(2011) Yvonne S. Davidson et al.   ACTA NEUROPATHOLOGICA

Intracellular pH is a tightly controlled signal in yeast

(2011) Rick Orij et al.   BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS

Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration

(2011) Edward B. Lee et al.   NATURE REVIEWS NEUROSCIENCE

Frontotemporal Lobar Degeneration

(2010) Gil D. Rabinovici et al.   CNS DRUGS

TDP-43 regulates its mRNA levels through a negative feedback loop

(2010) Youhna M Ayala et al.   EMBO JOURNAL

TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

(2010) C. Lagier-Tourenne et al.   HUMAN MOLECULAR GENETICS

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

TDP-43 Is a Developmentally Regulated Protein Essential for Early Embryonic Development

(2009) Chantelle F. Sephton 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

Disturbance of Nuclear and Cytoplasmic TAR DNA-binding Protein (TDP-43) Induces Disease-like Redistribution, Sequestration, and Aggregate Formation

(2008) Matthew J. Winton et al.   JOURNAL OF BIOLOGICAL CHEMISTRY