Related references
Note: Only part of the references are listed.Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
Archana Prasad et al.
FRONTIERS IN MOLECULAR NEUROSCIENCE (2019)
Isolation and characterization of soluble human full-length TDP-43 associated with neurodegeneration
Mirella Vivoli Vega et al.
FASEB JOURNAL (2019)
The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43
Hao-Ru Li et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2018)
A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing
Ailin Wang et al.
EMBO JOURNAL (2018)
Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity
Edoardo Del Poggetto et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2018)
Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions
Miguel Mompean et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2017)
Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation
Tariq Afroz et al.
NATURE COMMUNICATIONS (2017)
Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories
Supratik Sen Mojumdar et al.
NATURE COMMUNICATIONS (2017)
The N-terminal dimerization is required for TDP-43 splicing activity
Lei-Lei Jiang et al.
SCIENTIFIC REPORTS (2017)
The N-Terminal Domain of ALS-Linked TDP-43 Assembles without Misfolding
Phoebe S. Tsoi et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2017)
Phase to Phase with TDP-43
Yulong Sun et al.
BIOCHEMISTRY (2017)
The TDP-43 N-terminal domain structure at high resolution
Miguel Mompean et al.
FEBS JOURNAL (2016)
A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity
Theodoros K. Karamanos et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2016)
ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain
Alexander E. Conicella et al.
STRUCTURE (2016)
Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation
Lei-Lei Jiang et al.
SCIENTIFIC REPORTS (2016)
ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43
Liangzhong Lim et al.
PLOS BIOLOGY (2016)
Structural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation
Chien-Hao Chiang et al.
SCIENTIFIC REPORTS (2016)
TDP-43 proteinopathies: pathological identification of brain regions differentiating clinical phenotypes
Rachel H. Tan et al.
BRAIN (2015)
Systemic Amyloidosis: Lessons from β2-Microglobulin
Monica Stoppini et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2015)
Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy
Andras Micsonai et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2015)
A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein
Ryo P. Honda et al.
STRUCTURE (2015)
The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis
Edoardo Del Poggetto et al.
SCIENTIFIC REPORTS (2015)
Folding of the RNA Recognition Motif (RRM) Domains of the Amyotrophic Lateral Sclerosis (ALS)-linked Protein TDP-43 Reveals an Intermediate State
Brian C. Mackness et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2014)
The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids
Pan-Hsien Kuo et al.
NUCLEIC ACIDS RESEARCH (2014)
Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1
Petur O. Heidarsson et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2014)
TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA
Haina Qin et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2014)
The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation
Yong-Jie Zhang et al.
HUMAN MOLECULAR GENETICS (2013)
Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
Peter J. Lukavsky et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2013)
The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity
Chung-ke Chang et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2012)
Identification of a Conserved Aggregation-Prone Intermediate State in the Folding Pathways of Spc-SH3 Amyloidogenic Variants
H. Krobath et al.
JOURNAL OF MOLECULAR BIOLOGY (2012)
Structure of an Intermediate State in Protein Folding and Aggregation
Philipp Neudecker et al.
SCIENCE (2012)
The Seeds of Neurodegeneration: Prion-like Spreading in ALS
Magdalini Polymenidou et al.
CELL (2011)
Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update
Ian R. A. Mackenzie et al.
ACTA NEUROPATHOLOGICA (2010)
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
Clotilde Lagier-Tourenne et al.
HUMAN MOLECULAR GENETICS (2010)
TDP-43 Is a Developmentally Regulated Protein Essential for Early Embryonic Development
Chantelle F. Sephton et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
TDP43-Positive Intraneuronal Inclusions in a Patient with Motor Neuron Disease and Parkinson's Disease
Jean-Baptiste Chanson et al.
NEURODEGENERATIVE DISEASES (2010)
TDP-43 localizes in mRNA transcription and processing sites in mammalian neurons
Inigo Casafont et al.
JOURNAL OF STRUCTURAL BIOLOGY (2009)
ALS motor phenotype heterogeneity, focality, and spread Deconstructing motor neuron degeneration
John M. Ravits et al.
NEUROLOGY (2009)
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
Pan-Hsien Kuo et al.
NUCLEIC ACIDS RESEARCH (2009)
Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer's disease
Troy T. Rohn
BRAIN RESEARCH (2008)
Colocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease
Claudia Schwab et al.
JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY (2008)
TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression
Youhna M. Ayala et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
Jemeen Sreedharan et al.
SCIENCE (2008)
Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43
Yong-Jie Zhang et al.
JOURNAL OF NEUROSCIENCE (2007)
Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC
Mamie Z. Li et al.
NATURE METHODS (2007)
TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Tetsuaki Arai et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2006)
Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Manuela Neumann et al.
SCIENCE (2006)
Combined NMR-observation of cold denaturation in supercooled water and heat denaturation enables accurate measurement of ΔCp of protein unfolding
T Szyperski et al.
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS (2006)
An obligatory intermediate in the folding pathway of cytochrome c552 from Hydrogenobacter thermophilus
C Travaglini-Allocatelli et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Human, Drosophila, and C-elegans TDP43:: Nucleic acid binding properties and splicing regulatory function
YM Ayala et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)
The Microprocessor complex mediates the genesis of microRNAs
RI Gregory et al.
NATURE (2004)
A partially structured species of β2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis
F Chiti et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)