Related references
Note: Only part of the references are listed.A Solid-State Conceptualization of Information Transfer from Gene to Message to Protein
Masato Kato et al.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 87 (2018)
Structure-based inhibitors of tau aggregation
P. M. Seidler et al.
NATURE CHEMISTRY (2018)
Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks
Michael P. Hughes et al.
SCIENCE (2018)
Phase separation of a yeast prion protein promotes cellular fitness
Titus M. Franzmann et al.
SCIENCE (2018)
Casein Kinase 2 Is Linked to Stress Granule Dynamics through Phosphorylation of the Stress Granule Nucleating Protein G3BP1
Lucas C. Reineke et al.
MOLECULAR AND CELLULAR BIOLOGY (2017)
Cryo-EM structures of tau filaments from Alzheimer's disease
Anthony W. P. Fitzpatrick et al.
NATURE (2017)
RNA phase transitions in repeat expansion disorders
Ankur Jain et al.
NATURE (2017)
Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains
Dylan T. Murray et al.
CELL (2017)
RNA-binding proteins with prion-like domains in health and disease
Alice Ford Harrison et al.
BIOCHEMICAL JOURNAL (2017)
Structural Studies of Amyloid Proteins at the Molecular Level
David S. Eisenberg et al.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 86 (2017)
Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease
Zachary M. March et al.
BRAIN RESEARCH (2016)
A Designed Inhibitor of p53 Aggregation Rescues p53 Tumor Suppression in Ovarian Carcinomas
Alice Soragni et al.
CANCER CELL (2016)
The collection of MicroED data for macromolecular crystallography
Dan Shi et al.
NATURE PROTOCOLS (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)
In Vivo Formation of Vacuolated Multi-phase Compartments Lacking Membranes
Hermann Broder Schmidt et al.
CELL REPORTS (2016)
The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei
Siheng Xiang et al.
CELL (2015)
Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization
Amandine Molliex et al.
CELL (2015)
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Avinash Patel et al.
CELL (2015)
Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
Yuan Lin et al.
MOLECULAR CELL (2015)
Structure of the toxic core of α-synuclein from invisible crystals
Jose A. Rodriguez et al.
NATURE (2015)
TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD
Jonathan P. Ling et al.
SCIENCE (2015)
MicroED data collection and processing
Johan Hattne et al.
ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES (2015)
Structural characterization of the minimal segment of TDP-43 competent for aggregation
Miguel Mompean et al.
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS (2014)
Self-Assembling Properties of Peptides Derived from TDP-43 C-Terminal Fragment
Akash Saini et al.
LANGMUIR (2014)
The amyloid state and its association with protein misfolding diseases
Tuomas P. J. Knowles et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2014)
Welander distal myopathy is caused by a mutation in the RNA-binding protein TIA1
Peter Hackman et al.
ANNALS OF NEUROLOGY (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)
Characterization of β-domains in C-terminal fragments of TDP-43 by scanning tunneling microscopy
Meng Xu et al.
JOURNAL OF STRUCTURAL BIOLOGY (2013)
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Hong Joo Kim et al.
NATURE (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)
Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Shuo-Chien Ling et al.
NEURON (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)
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)
Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)
Eva Bentmann et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2012)
Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity
Pin-Nan Cheng et al.
NATURE CHEMISTRY (2012)
Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
Edward B. Lee et al.
NATURE REVIEWS NEUROSCIENCE (2012)
Overview of the CCP4 suite and current developments
Martyn D. Winn et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2011)
Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS
Patricia S. Estes et al.
HUMAN MOLECULAR GENETICS (2011)
TDP-43 Is Directed to Stress Granules by Sorbitol, a Novel Physiological Osmotic and Oxidative Stressor
Colleen M. Dewey et al.
MOLECULAR AND CELLULAR BIOLOGY (2011)
An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
Weirui Guo et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2011)
XDS
Wolfgang Kabsch
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (2010)
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Paul D. Adams et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2010)
Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
Daryl A. Bosco et al.
HUMAN MOLECULAR GENETICS (2010)
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
Clotilde Lagier-Tourenne et al.
HUMAN MOLECULAR GENETICS (2010)
Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43
Rodrigo A. Fuentealba et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
Prion-like disorders: blurring the divide between transmissibility and infectivity
Mimi Cushman et al.
JOURNAL OF CELL SCIENCE (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)
Identifying the amylome, proteins capable of forming amyloid-like fibrils
Lukasz Goldschmidt et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)
The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation
Emanuele Buratti et al.
RNA BIOLOGY (2010)
Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis
G. Scott Pesiridis et al.
HUMAN MOLECULAR GENETICS (2009)
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)
TDP-43 is recruited to stress granules in conditions of oxidative insult
Claudia Colombrita et al.
JOURNAL OF NEUROCHEMISTRY (2009)
TDP-43 A315T mutation in familial motor neuron disease
Michael A. Gitcho et al.
ANNALS OF NEUROLOGY (2008)
Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Masato Hasegawa et al.
ANNALS OF NEUROLOGY (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)
TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
Edor Kabashi et al.
NATURE GENETICS (2008)
Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin)
Jed J. W. Wiltzius et al.
PROTEIN SCIENCE (2008)
A short history of SHELX
George M. Sheldrick
ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES (2008)
Concurrence of TDP-43, tau and α-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies
Shinji Higashi et al.
BRAIN RESEARCH (2007)
Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases
Hanae Nakashima-Yasuda et al.
ACTA NEUROPATHOLOGICA (2007)
Phaser crystallographic software
Airlie J. McCoy et al.
JOURNAL OF APPLIED CRYSTALLOGRAPHY (2007)
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Michael R. Sawaya et al.
NATURE (2007)
TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease
Catalina Amador-Ortiz et al.
ANNALS OF NEUROLOGY (2007)
Eukaryotic initiation factor 2α-independent pathway of stress granule induction by the natural product pateamine A
Yongjun Dang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Manuela Neumann et al.
SCIENCE (2006)
Probing the pressure-temperature stability of amyloid fibrils provides new insights into their molecular properties
F Meersman et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2006)
Intrinsically unstructured proteins and their functions
HJ Dyson et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2005)
Stress granule assembly is mediated by prion-like aggregation of TIA-1
N Gilks et al.
MOLECULAR BIOLOGY OF THE CELL (2004)
Coot:: model-building tools for molecular graphics
P Emsley et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2004)
Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules
N Kedersha et al.
JOURNAL OF CELL BIOLOGY (2000)
Share Paper
