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。N-terminal acetylation modestly enhances phase separation and reduces aggregation of the low-complexity domain of RNA-binding protein fused in sarcoma
Anna S. Bock et al.
PROTEIN SCIENCE (2021)
Mechanism of karyopherin-β2 binding and nuclear import of ALS variants FUS(P525L) and FUS(R495X)
Abner Gonzalez et al.
SCIENTIFIC REPORTS (2021)
Symmetric dimethylation of poly-GR correlates with disease duration in C9orf72 FTLD and ALS and reduces poly-GR phase separation and toxicity
Lauren M. Gittings et al.
ACTA NEUROPATHOLOGICA (2020)
C9orf72 arginine-rich dipeptide repeat proteins disrupt karyopherin-mediated nuclear import
Lindsey R. Hayes et al.
ELIFE (2020)
Nonclassical nuclear localization signals mediate nuclear import of CIRBP
Benjamin Bourgeois et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2020)
Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions
Saskia Hutten et al.
CELL REPORTS (2020)
Arginine-rich dipeptide-repeat proteins as phase disruptors in C9-ALS/FTD
Hana M. Odeh et al.
EMERGING TOPICS IN LIFE SCIENCES (2020)
Redox-mediated regulation of an evolutionarily conserved cross-β structure formed by the TDP43 low complexity domain
Yi Lin et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2020)
Widespread FUS mislocalization is a molecular hallmark of amyotrophic lateral sclerosis
Giulia E. Tyzack et al.
BRAIN (2019)
Cryo-EM structures of four polymorphic TDP-43 amyloid cores
Qin Cao et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2019)
The mutational landscape of a prion-like domain
Benedetta Bolognesi et al.
NATURE COMMUNICATIONS (2019)
C9orf72-generated poly-GR and poly-PR do not directly interfere with nucleocytoplasmic transport
Joni Vanneste et al.
SCIENTIFIC REPORTS (2019)
A Solid-State Conceptualization of Information Transfer from Gene to Message to Protein
Masato Kato et al.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 87 (2018)
Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites
Takuya Yoshizawa et al.
CELL (2018)
Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation
Mario Hofweber et al.
CELL (2018)
Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains
Lin Guo et al.
CELL (2018)
FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions
Seema Qamar et al.
CELL (2018)
Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation
Veronica H. Ryan et al.
MOLECULAR CELL (2018)
Oligomerization of a molecular chaperone modulates its activity
Tomohide Saio et al.
ELIFE (2018)
C9orf72-mediated ALS and FTD: multiple pathways to disease
Rubika Balendra et al.
NATURE REVIEWS NEUROLOGY (2018)
Cross-β polymerization and hydrogel formation by low-complexity sequence proteins
Masato Kato et al.
METHODS (2017)
Toxic PRn poly-dipeptides encoded by the C9orf72 repeat expansion block nuclear import and export
Kevin Y. Shi et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2017)
Fibril structure of amyloid-β(1-42) by cryo-electron microscopy
Lothar Gremer et al.
SCIENCE (2017)
Extensive cargo identification reveals distinct biological roles of the 12 importin pathways
Makoto Kimura et al.
ELIFE (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)
Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity
Zachary Monahan et al.
EMBO JOURNAL (2017)
Inside out: the role of nucleocytoplasmic transport in ALS and FTLD
Steven Boeynaems et al.
ACTA NEUROPATHOLOGICA (2016)
C9orf72 Dipeptide Repeats Impair the Assembly, Dynamics, and Function of Membrane-Less Organelles
Kyung-Ha Lee et al.
CELL (2016)
Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers
Yi Lin et al.
CELL (2016)
Reduced hnRNPA3 increases C9orf72 repeat RNA levels and dipeptide-repeat protein deposition
Kohji Mori et al.
EMBO REPORTS (2016)
The C9orf72 repeat expansion disrupts nucleocytoplasmic transport
Ke Zhang et al.
NATURE (2015)
GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport
Brian D. Freibaum et al.
NATURE (2015)
Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS
Ana Jovicic et al.
NATURE NEUROSCIENCE (2015)
Accumulation of dipeptide repeat proteins predates that of TDP-43 in frontotemporal lobar degeneration associated with hexanucleotide repeat expansions in C9ORF72 gene
A. Baborie et al.
NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY (2015)
ClpB N-terminal domain plays a regulatory role in protein disaggregation
Rina Rosenzweig et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2015)
C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins
Sarah Mizielinska et al.
SCIENCE (2014)
Poly-dipeptides encoded by the C9orf72 repeats bind nucleoli, impede RNA biogenesis, and kill cells
Ilmin Kwon et al.
SCIENCE (2014)
Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone
Tomohide Saio et al.
SCIENCE (2014)
Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins
Kohji Mori et al.
ACTA NEUROPATHOLOGICA (2013)
RAN proteins and RNA foci from antisense transcripts in C9ORF72 ALS and frontotemporal dementia
Tao Zu et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2013)
Co-aggregation of RNA binding proteins in ALS spinal motor neurons: evidence of a common pathogenic mechanism
Brian A. Keller et al.
ACTA NEUROPATHOLOGICA (2012)
Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
Masato Kato et al.
CELL (2012)
Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS
Dorothee Dormann et al.
EMBO JOURNAL (2012)
Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)
Zi Chao Zhang et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2012)
Very fast prediction and rationalization of pKa values for protein-ligand complexes
Delphine C. Bas et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2008)
Structure-based design of a pathway-specific nuclear import inhibitor
Ahmet E. Cansizoglu et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2007)
Integrated modeling program, applied chemical theory (IMPACT)
JL Banks et al.
JOURNAL OF COMPUTATIONAL CHEMISTRY (2005)
Very fast empirical prediction and rationalization of protein pKa values
H Li et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2005)
TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail - An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
E Buratti et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
SE Ong et al.
NATURE METHODS (2004)
Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
P Schuck
BIOPHYSICAL JOURNAL (2000)
分享论文
