Delineation of the Core Aggregation Sequences of TDP-43 C-Terminal Fragment

Mutations That Replace Aromatic Side Chains Promote Aggregation of the Alzheimer’s Aβ Peptide

(2011) Anne H. Armstrong et al.   BIOCHEMISTRY

A Seeding Reaction Recapitulates Intracellular Formation of Sarkosyl-insoluble Transactivation Response Element (TAR) DNA-binding Protein-43 Inclusions

(2011) Yoshiaki Furukawa et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Probing the role of aromaticity in the design of dipeptide based nanostructures

(2011) Aseem Mishra et al.   Nanoscale

An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity

(2011) Weirui Guo et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The C-Terminal TDP-43 Fragments Have a High Aggregation Propensity and Harm Neurons by a Dominant-Negative Mechanism

(2011) Chunxing Yang et al.   PLoS One

Large Proteins Have a Great Tendency to Aggregate but a Low Propensity to Form Amyloid Fibrils

(2011) Hassan Ramshini et al.   PLoS One

TDP-43: A DNA and RNA binding protein with roles in neurodegenerative diseases

(2010) Sadaf T. Warraich et al.   INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY

Prion-like disorders: blurring the divide between transmissibility and infectivity

(2010) M. Cushman et al.   JOURNAL OF CELL SCIENCE

Induction of Amyloid Fibrils by the C-Terminal Fragments of TDP-43 in Amyotrophic Lateral Sclerosis

(2010) Allan K.-H. Chen et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution

(2010) Harry Levine   PROTEIN SCIENCE

Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43

(2009) Takashi Nonaka et al.   HUMAN MOLECULAR GENETICS

Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis

(2009) G. S. Pesiridis et al.   HUMAN MOLECULAR GENETICS

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

Structural insights into TDP-43 in nucleic-acid binding and domain interactions

(2009) P.-H. Kuo et al.   NUCLEIC ACIDS RESEARCH

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

(2009) Y.-J. Zhang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases

(2008) Wen-Lang Lin et al.   ACTA NEUROPATHOLOGICA

Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

(2008) Masato Hasegawa et al.   ANNALS OF NEUROLOGY

TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis

(2008) Edor Kabashi et al.   NATURE GENETICS

A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity

(2008) B. S. Johnson et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

(2008) J. Sreedharan et al.   SCIENCE