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Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
P Tziortzouda, L Van Den Bosch, F Hirth - Nature Reviews …, 2021 - nature.com
Cytoplasmic aggregation of TAR DNA-binding protein 43 (TDP43; also known as TARDBP
or TDP-43) is a key pathological feature of several neurodegenerative diseases, including …
or TDP-43) is a key pathological feature of several neurodegenerative diseases, including …
The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies
M Jo, S Lee, YM Jeon, S Kim, Y Kwon… - Experimental & molecular …, 2020 - nature.com
Abstract TAR DNA-binding protein 43 (TDP-43) is a highly conserved nuclear RNA/DNA-
binding protein involved in the regulation of RNA processing. The accumulation of TDP-43 …
binding protein involved in the regulation of RNA processing. The accumulation of TDP-43 …
TDP-43 condensation properties specify its RNA-binding and regulatory repertoire
Mutations causing amyotrophic lateral sclerosis (ALS) often affect the condensation
properties of RNA-binding proteins (RBPs). However, the role of RBP condensation in the …
properties of RNA-binding proteins (RBPs). However, the role of RBP condensation in the …
TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
The cytoplasmic mislocalization and aggregation of TAR DNA-binding protein-43 (TDP-43)
is a common histopathological hallmark of the amyotrophic lateral sclerosis and …
is a common histopathological hallmark of the amyotrophic lateral sclerosis and …
Nuclear-import receptors reverse aberrant phase transitions of RNA-binding proteins with prion-like domains
RNA-binding proteins (RBPs) with prion-like domains (PrLDs) phase transition to functional
liquids, which can mature into aberrant hydrogels composed of pathological fibrils that …
liquids, which can mature into aberrant hydrogels composed of pathological fibrils that …
The C9orf72 repeat expansion disrupts nucleocytoplasmic transport
The hexanucleotide repeat expansion (HRE) GGGGCC (G4C2) in C9orf72 is the most
common cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) …
common cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) …
Monomerization of TDP-43 is a key determinant for inducing TDP-43 pathology in amyotrophic lateral sclerosis
K Oiwa, S Watanabe, K Onodera, Y Iguchi… - Science …, 2023 - science.org
The cytoplasmic aggregation of TAR DNA binding protein-43 (TDP-43), also known as TDP-
43 pathology, is the pathological hallmark of amyotrophic lateral sclerosis (ALS). However …
43 pathology, is the pathological hallmark of amyotrophic lateral sclerosis (ALS). However …
Nuclear pore complexes—a doorway to neural injury in neurodegeneration
The genetic underpinnings and end-stage pathological hallmarks of neurodegenerative
diseases are increasingly well defined, but the cellular pathophysiology of disease initiation …
diseases are increasingly well defined, but the cellular pathophysiology of disease initiation …
TDP-43 pathology in Alzheimer's disease
Transactive response DNA binding protein of 43 kDa (TDP-43) is an intranuclear protein
encoded by the TARDBP gene that is involved in RNA splicing, trafficking, stabilization, and …
encoded by the TARDBP gene that is involved in RNA splicing, trafficking, stabilization, and …
Physiological functions and pathobiology of TDP‐43 and FUS/TLS proteins
The multiple roles played by RNA binding proteins in neurodegeneration have become
apparent following the discovery of TAR DNA binding protein 43 kDa (TDP‐43) and fused in …
apparent following the discovery of TAR DNA binding protein 43 kDa (TDP‐43) and fused in …