相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。The extreme N-terminus of TDP-43 mediates the cytoplasmic aggregation of TDP-43 and associated toxicity in vivo
Hiroki Sasaguri et al.
BRAIN RESEARCH (2016)
The TDP-43 N-terminal domain structure at high resolution
Miguel Mompean et al.
FEBS JOURNAL (2016)
Complex System Assembly Underlies a Two-Tiered Model of Highly Delocalized Electrons
Miguel Mompean et al.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS (2016)
Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation
Miguel Mompean et al.
PLOS BIOLOGY (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)
Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion
Alba Espargaro et al.
FRONTIERS IN MOLECULAR NEUROSCIENCE (2016)
Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains
Fuyuki Kametani et al.
SCIENTIFIC REPORTS (2016)
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Avinash Patel et al.
CELL (2015)
Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43
Miguel Mompean et al.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS (2015)
Review: Prion-like mechanisms of transactive response DNA binding protein of 43kDa (TDP-43) in amyotrophic lateral sclerosis (ALS)
P. Smethurst et al.
NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY (2015)
The structural integrity of TDP-43N-terminus is required for efficient aggregate entrapment and consequent loss of protein function
Valentina Romano et al.
PRION (2015)
TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domain
Mauricio Budini et al.
HUMAN MOLECULAR GENETICS (2015)
Structural characterization of the minimal segment of TDP-43 competent for aggregation
Miguel Mompean et al.
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS (2014)
An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution
Li Zhu et al.
HUMAN MOLECULAR GENETICS (2014)
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)
Self-Assembling Properties of Peptides Derived from TDP-43 C-Terminal Fragment
Akash Saini et al.
LANGMUIR (2014)
TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells
Claudia Capitini et al.
PLOS ONE (2014)
The Influence of Pathological Mutations and Proline Substitutions in TDP-43 Glycine-Rich Peptides on Its Amyloid Properties and Cellular Toxicity
Chia-Sui Sun et al.
PLOS ONE (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)
Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients
Yu-Sheng Fang et al.
NATURE COMMUNICATIONS (2014)
TDP-43 skeins show properties of amyloid in a subset of ALS cases
John L. Robinson et al.
ACTA NEUROPATHOLOGICA (2013)
Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid
Eileen H. Bigio et al.
ACTA NEUROPATHOLOGICA (2013)
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)
Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion
Lei-Lei Jiang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2013)
The Truncated C-terminal RNA Recognition Motif of TDP-43 Protein Plays a Key Role in Forming Proteinaceous Aggregates
Yi-Ting Wang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (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)
Prion-like Properties of Pathological TDP-43 Aggregates from Diseased Brains
Takashi Nonaka et al.
CELL REPORTS (2013)
Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
Masato Kato et al.
CELL (2012)
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)
TDP-43: gumming up neurons through protein-protein and protein-RNA interactions
Emanuele Buratti et al.
TRENDS IN BIOCHEMICAL SCIENCES (2012)
A harmonized classification system for FTLD-TDP pathology
Ian R. A. Mackenzie et al.
ACTA NEUROPATHOLOGICA (2011)
Delineation of the Core Aggregation Sequences of TDP-43 C-Terminal Fragment
Akash Saini et al.
CHEMBIOCHEM (2011)
TDP-43: new aspects of autoregulation mechanisms in RNA binding proteins and their connection with human disease
Emanuele Buratti et al.
FEBS JOURNAL (2011)
Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1
Owen A. Brady et al.
JOURNAL OF NEUROCHEMISTRY (2011)
Amyotrophic lateral sclerosis
Matthew C. Kiernan et al.
LANCET (2011)
Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43
Magdalini Polymenidou et al.
NATURE NEUROSCIENCE (2011)
Characterizing the RNA targets and position-dependent splicing regulation by TDP-43
James R. Tollervey et al.
NATURE NEUROSCIENCE (2011)
An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
Weirui Guo et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2011)
Hyperphosphorylation as a Defense Mechanism to Reduce TDP-43 Aggregation
Huei-Ying Li et al.
PLOS ONE (2011)
Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43
Rodrigo A. Fuentealba et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
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)
Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
Manuela Neumann et al.
ACTA NEUROPATHOLOGICA (2009)
Identification of casein kinase-1 phosphorylation sites on TDP-43
Fuyuki Kametani et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2009)
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
G. Scott Pesiridis et al.
HUMAN MOLECULAR GENETICS (2009)
Structural insights into TDP-43 in nucleic-acid binding and domain interactions
Pan-Hsien Kuo et al.
NUCLEIC ACIDS RESEARCH (2009)
Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases
Wen-Lang Lin et al.
ACTA NEUROPATHOLOGICA (2008)
Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Masato Hasegawa et al.
ANNALS OF NEUROLOGY (2008)
Fine structural analysis of the neuronal inclusions of frontotemporal lobar degeneration with TDP-43 proteinopathy
Julian R. Thorpe et al.
JOURNAL OF NEURAL TRANSMISSION (2008)
A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDR-43 aggregation and cellular toxicity
Brian S. Johnson et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis - Protein misfolding diseases without amyloidosis
Manuela Neumann et al.
ARCHIVES OF NEUROLOGY (2007)
TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions
Nigel J. Cairns et al.
AMERICAN JOURNAL OF PATHOLOGY (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)
Human, Drosophila, and C-elegans TDP43:: Nucleic acid binding properties and splicing regulatory function
YM Ayala et al.
JOURNAL OF MOLECULAR BIOLOGY (2005)