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Alternative splicing as a regulator of development and tissue identity

Nature reviews. Molecular cell biology, 2017-07, Vol.18 (7), p.437

2017

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Alternative splicing and liver disease

Annals of hepatology, 2021-12, Vol.26, p.100534-100534, Article 100534

2021

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The role of TDP-43 in the pathogenesis of ALS and FTLD

Biochemical Society transactions, 2013-12, Vol.41 (6), p.1536

2013

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TDP-43: gumming up neurons through protein–protein and protein–RNA interactions

Trends in biochemical sciences (Amsterdam. Regular ed.), 2012-06, Vol.37 (6), p.237-247

2012

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

The EMBO journal, 2011-01, Vol.30 (2), p.277-288

2011

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The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation

RNA biology, 2010-07, Vol.7 (4), p.420-429

2010

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TDP-43 and FUS RNA-binding Proteins Bind Distinct Sets of Cytoplasmic Messenger RNAs and Differently Regulate Their Post-transcriptional Fate in Motoneuron-like Cells

The Journal of biological chemistry, 2012-05, Vol.287 (19), p.15635-15647

2012

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Genomic variants in exons and introns: identifying the splicing spoilers

Nature reviews. Genetics, 2004-05, Vol.5 (5), p.389-396

2004

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Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

Nature structural & molecular biology, 2013-12, Vol.20 (12), p.1443

2013

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Influence of RNA Secondary Structure on the Pre-mRNA Splicing Process

Molecular and cellular biology, 2004-12, Vol.24 (24), p.10505-10514

2004

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TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domain

Human molecular genetics, 2015-01, Vol.24 (1), p.9-20

2015

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The TDP‐43 N‐terminal domain structure at high resolution

The FEBS journal, 2016-04, Vol.283 (7), p.1242-1260

2016

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Nuclear factor TDP-43 can affect selected microRNA levels

The FEBS journal, 2010-05, Vol.277 (10), p.2268-2281

2010

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Thioridazine reverts the phenotype in cellular and Drosophila models of amyotrophic lateral sclerosis by enhancing TDP-43 aggregate clearance

Neurobiology of disease, 2021-12, Vol.160, p.105515-105515, Article 105515

2021

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

Journal of cell science, 2008-11, Vol.121 (Pt 22), p.3778-3785

2008

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

The EMBO journal, 2011-01, Vol.30 (2), p.277-288

2011

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Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior

FEBS letters, 2009-05, Vol.583 (10), p.1586-1592

2009

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TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression

Proceedings of the National Academy of Sciences - PNAS, 2008-03, Vol.105 (10), p.3785-3789

2008

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Characterizing TDP-43 interaction with its RNA targets

Nucleic acids research, 2013-05, Vol.41 (9), p.5062

2013

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TDP-43 regulates Drosophila neuromuscular junctions growth by modulating Futsch/MAP1B levels and synaptic microtubules organization

PloS one, 2011-03, Vol.6 (3), p.e17808-e17808

2011

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Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions

The Journal of biological chemistry, 2017-07, Vol.292 (28), p.11992-12006

2017

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Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection

Genes & development, 2012-08, Vol.26 (15), p.1679-1684

2012

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

The Journal of biological chemistry, 2012-03, Vol.287 (10), p.7512-7525

2012

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RNA structure and splicing regulation

Biochimica et biophysica acta. Gene regulatory mechanisms, 2019-11, Vol.1862 (11-12), p.194448-194448, Article 194448

2019

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Absence of TDP-43 is difficult to digest

The EMBO journal, 2016-01, Vol.35 (2), p.115-117

2016

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Alternative splicing as a regulator of development and tissue identity

Alternative splicing and liver disease

The role of TDP-43 in the pathogenesis of ALS and FTLD

TDP-43: gumming up neurons through protein–protein and protein–RNA interactions

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

The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation

TDP-43 and FUS RNA-binding Proteins Bind Distinct Sets of Cytoplasmic Messenger RNAs and Differently Regulate Their Post-transcriptional Fate in Motoneuron-like Cells

Genomic variants in exons and introns: identifying the splicing spoilers

Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

Influence of RNA Secondary Structure on the Pre-mRNA Splicing Process

TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domain

The TDP‐43 N‐terminal domain structure at high resolution

Nuclear factor TDP-43 can affect selected microRNA levels

Thioridazine reverts the phenotype in cellular and Drosophila models of amyotrophic lateral sclerosis by enhancing TDP-43 aggregate clearance

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

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

Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior

TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression

Characterizing TDP-43 interaction with its RNA targets

TDP-43 regulates Drosophila neuromuscular junctions growth by modulating Futsch/MAP1B levels and synaptic microtubules organization

Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions

Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selection

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

RNA structure and splicing regulation

Absence of TDP-43 is difficult to digest

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