4.6 Article

Robustness and Vulnerability of the Autoregulatory System That Maintains Nuclear TDP-43 Levels: A Trade-off Hypothesis for ALS Pathology Based on in Silico Data

Related references

Note: Only part of the references are listed.
Article Biochemistry & Molecular Biology

Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD

Bahram Khosravi et al.

HUMAN MOLECULAR GENETICS (2017)

Article Cell Biology

hnRNPA1 autoregulates its own mRNA expression to remain non-cytotoxic

Hiroaki Suzuki et al.

MOLECULAR AND CELLULAR BIOCHEMISTRY (2017)

Article Immunology

Progranulin deficiency causes impairment of autophagy and TDP-43 accumulation

Michael C. Chang et al.

JOURNAL OF EXPERIMENTAL MEDICINE (2017)

Review Medicine, General & Internal

Amyotrophic lateral sclerosis

Michael A. van Es et al.

LANCET (2017)

Article Multidisciplinary Sciences

Amyotrophic lateral sclerosis-linked mutations increase the viscosity of liquid-like TDP-43 RNP granules in neurons

Pallavi P. Gopal et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2017)

Article Multidisciplinary Sciences

Loss of function CHCHD10 mutations in cytoplasmic TDP-43 accumulation and synaptic integrity

Jung-A A. Woo et al.

NATURE COMMUNICATIONS (2017)

Article Neurosciences

Autophagy Dysregulation in ALS: When Protein Aggregates Get Out of Hand

Nandini Ramesh et al.

FRONTIERS IN MOLECULAR NEUROSCIENCE (2017)

Article Biochemistry & Molecular Biology

Phase to Phase with TDP-43

Yulong Sun et al.

BIOCHEMISTRY (2017)

Article Multidisciplinary Sciences

Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA

Andreas C. Woerner et al.

SCIENCE (2016)

Review Clinical Neurology

Inside out: the role of nucleocytoplasmic transport in ALS and FTLD

Steven Boeynaems et al.

ACTA NEUROPATHOLOGICA (2016)

Article Clinical Neurology

Exosome secretion is a key pathway for clearance of pathological TDP-43

Yohei Iguchi et al.

BRAIN (2016)

Review Biochemistry & Molecular Biology

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

Antonia Ratti et al.

JOURNAL OF NEUROCHEMISTRY (2016)

Review Multidisciplinary Sciences

Decoding ALS: from genes to mechanism

J. Paul Taylor et al.

NATURE (2016)

Article Biochemistry & Molecular Biology

Increased cytoplasmic TARDBP mRNA in affected spinal motor neurons in ALS caused by abnormal autoregulation of TDP-43

Akihide Koyama et al.

NUCLEIC ACIDS RESEARCH (2016)

Article Cell Biology

TDP-43 is intercellularly transmitted across axon terminals

Marisa S. Feiler et al.

JOURNAL OF CELL BIOLOGY (2015)

Article Multidisciplinary Sciences

The C9orf72 repeat expansion disrupts nucleocytoplasmic transport

Ke Zhang et al.

NATURE (2015)

Article Multidisciplinary Sciences

GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport

Brian D. Freibaum et al.

NATURE (2015)

Article Biochemistry & Molecular Biology

Mitochondrial Dysfunction and Decrease in Body Weight of a Transgenic Knock-in Mouse Model for TDP-43

Carola Stribl et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2014)

Article Clinical Neurology

Stages of pTDP-43 Pathology in Amyotrophic Lateral Sclerosis

Johannes Brettschneider et al.

ANNALS OF NEUROLOGY (2013)

Review Biochemistry & Molecular Biology

Rodent models of amyotrophic lateral sclerosis

Philip McGoldrick et al.

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE (2013)

Article Biochemistry & Molecular Biology

Accelerated Disease Onset with Stabilized Familial Amyotrophic Lateral Sclerosis (ALS)-linked Mutant TDP-43 Proteins

Shoji Watanabe et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2013)

Article Clinical Neurology

Amyotrophic lateral sclerosis-a model of corticofugal axonal spread

Heiko Braak et al.

NATURE REVIEWS NEUROLOGY (2013)

Article Multidisciplinary Sciences

ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43

Eveline S. Arnold et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2013)

Article Cell Biology

Prion-like Properties of Pathological TDP-43 Aggregates from Diseased Brains

Takashi Nonaka et al.

CELL REPORTS (2013)

Article Clinical Neurology

TDP-43 plasma levels are higher in amyotrophic lateral sclerosis

Esther Verstraete et al.

AMYOTROPHIC LATERAL SCLEROSIS (2012)

Article Biochemistry & Molecular Biology

Cellular Model of TAR DNA-binding Protein 43 (TDP-43) Aggregation Based on Its C-terminal Gln/Asn-rich Region

Mauricio Budini et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2012)

Review Neurosciences

Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration

Edward B. Lee et al.

NATURE REVIEWS NEUROSCIENCE (2012)

Article Biochemistry & Molecular Biology

The Seeds of Neurodegeneration: Prion-like Spreading in ALS

Magdalini Polymenidou et al.

Article Biochemistry & Molecular Biology

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

Youhna M. Ayala et al.

EMBO JOURNAL (2011)

Article Biochemistry & Molecular Biology

TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1

Karli K. McDonald et al.

HUMAN MOLECULAR GENETICS (2011)

Article Clinical Neurology

Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis

Brian C. Kraemer et al.

ACTA NEUROPATHOLOGICA (2010)

Review Pharmacology & Pharmacy

In Silico Dynamic Molecular Interaction Networks for the Discovery of New Therapeutic Targets

Todor Vujasinovic et al.

CURRENT PHARMACEUTICAL DESIGN (2010)

Article Biochemistry & Molecular Biology

ALS-associated fused in sarcoma (FUS) mutations disrupt Transportin-mediated nuclear import

Dorothee Dormann et al.

EMBO JOURNAL (2010)

Article Biochemistry & Molecular Biology

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

Chantelle F. Sephton et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2010)

Article Chemistry, Multidisciplinary

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

Allan K. -H. Chen et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2010)

Article Multidisciplinary Sciences

ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS

Shuo-Chien Ling et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)

Article Multidisciplinary Sciences

Deletion of TDP-43 down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism

Po-Min Chiang et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)

Article Clinical Neurology

Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis

Takashi Kasai et al.

ACTA NEUROPATHOLOGICA (2009)

Article Clinical Neurology

TARDBP 3'-UTR variant in autopsy-confirmed frontotemporal lobar degeneration with TDP-43 proteinopathy

Michael A. Gitcho et al.

ACTA NEUROPATHOLOGICA (2009)

Article Biochemistry & Molecular Biology

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

Takashi Nonaka et al.

HUMAN MOLECULAR GENETICS (2009)

Article Biochemistry & Molecular Biology

Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies

Lionel M. Igaz et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2009)

Article Biochemistry & Molecular Biology

TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity

Brian S. Johnson et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2009)

Article Clinical Neurology

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

Masato Hasegawa et al.

ANNALS OF NEUROLOGY (2008)

Article Cell Biology

Structural determinants of the cellular localization and shuttling of TDP-43

Youhna M. Ayala et al.

JOURNAL OF CELL SCIENCE (2008)

Article Biochemistry & Molecular Biology

TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor

I. -Fan Wang et al.

JOURNAL OF NEUROCHEMISTRY (2008)

Article Genetics & Heredity

TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis

Edor Kabashi et al.

NATURE GENETICS (2008)

Article Biochemistry & Molecular Biology

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)

Article Multidisciplinary Sciences

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

Manuela Neumann et al.

SCIENCE (2006)