Neuronal Expression of UBQLN2P497H Exacerbates TDP-43 Pathology in TDP-43G348C Mice through Interaction with Ubiquitin

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 1559-1182

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: Neuronal Expression of UBQLN2P497H Exacerbates TDP-43 Pathology in TDP-43G348C Mice through Interaction with Ubiquitin ; day:30 ; month:10 ; year:2018 ; pages:1-17
Molecular neurobiology ; (30.10.2018), 1-17

Creator: Picher-Martel, Vincent
Renaud, Laurence
Bareil, Christine
Julien, Jean-Pierre

Contributor: SpringerLink (Online service)

DOI: 10.1007/s12035-018-1411-3

URN: urn:nbn:de:101:1-2018121820383494359200

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:44 AM CEST

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Picher-Martel, Vincent
Renaud, Laurence
Bareil, Christine
Julien, Jean-Pierre
SpringerLink (Online service)

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Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD

Evidence of cerebellar TDP-43 loss of function in FTLD-TDP

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Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

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The regulation of TDP-43 ubiquitinylation by UBE2E ubiquitin-conjugating enzymes and ubiquitin Isopeptidase Y

The Regulation of TDP-43 Ubiquitinylation by UBE2E Ubiquitin-conjugating Enzymes and Ubiquitin Isopeptidase Y

TDP-43 pathology is associated with increased tau burdens and seeding

TDP-43 Pathology in Alzheimer’s Disease

Spreading of TDP-43 pathology via pyramidal tract induces ALS-like phenotypes in TDP-43 transgenic mice

Implications of TDP-43 in non-neuronal systems

Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology

Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD

Evidence of cerebellar TDP-43 loss of function in FTLD-TDP

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

Hochschulschrift

The regulation of TDP-43 ubiquitinylation by UBE2E ubiquitin-conjugating enzymes and ubiquitin Isopeptidase Y

The Regulation of TDP-43 Ubiquitinylation by UBE2E Ubiquitin-conjugating Enzymes and Ubiquitin Isopeptidase Y

TDP-43 pathology is associated with increased tau burdens and seeding

TDP-43 Pathology in Alzheimer’s Disease

Spreading of TDP-43 pathology via pyramidal tract induces ALS-like phenotypes in TDP-43 transgenic mice

Implications of TDP-43 in non-neuronal systems

Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology

Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD

Evidence of cerebellar TDP-43 loss of function in FTLD-TDP

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

Hochschulschrift

The regulation of TDP-43 ubiquitinylation by UBE2E ubiquitin-conjugating enzymes and ubiquitin Isopeptidase Y

The Regulation of TDP-43 Ubiquitinylation by UBE2E Ubiquitin-conjugating Enzymes and Ubiquitin Isopeptidase Y

TDP-43 pathology is associated with increased tau burdens and seeding

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Neuronal Expression of UBQLN2P497H Exacerbates TDP-43 Pathology in TDP-43G348C Mice through Interaction with Ubiquitin

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Other Objects (12)

TDP-43 Pathology in Alzheimer’s Disease

Spreading of TDP-43 pathology via pyramidal tract induces ALS-like phenotypes in TDP-43 transgenic mice

Implications of TDP-43 in non-neuronal systems

Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology

Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD

Evidence of cerebellar TDP-43 loss of function in FTLD-TDP

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

The regulation of TDP-43 ubiquitinylation by UBE2E ubiquitin-conjugating enzymes and ubiquitin Isopeptidase Y

The Regulation of TDP-43 Ubiquitinylation by UBE2E Ubiquitin-conjugating Enzymes and Ubiquitin Isopeptidase Y

TDP-43 pathology is associated with increased tau burdens and seeding

TDP-43 Pathology in Alzheimer’s Disease

Spreading of TDP-43 pathology via pyramidal tract induces ALS-like phenotypes in TDP-43 transgenic mice

Implications of TDP-43 in non-neuronal systems

Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology

Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD

Evidence of cerebellar TDP-43 loss of function in FTLD-TDP

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

The regulation of TDP-43 ubiquitinylation by UBE2E ubiquitin-conjugating enzymes and ubiquitin Isopeptidase Y

The Regulation of TDP-43 Ubiquitinylation by UBE2E Ubiquitin-conjugating Enzymes and Ubiquitin Isopeptidase Y

TDP-43 pathology is associated with increased tau burdens and seeding

TDP-43 Pathology in Alzheimer’s Disease

Spreading of TDP-43 pathology via pyramidal tract induces ALS-like phenotypes in TDP-43 transgenic mice

Implications of TDP-43 in non-neuronal systems

Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology

Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD

Evidence of cerebellar TDP-43 loss of function in FTLD-TDP

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

The regulation of TDP-43 ubiquitinylation by UBE2E ubiquitin-conjugating enzymes and ubiquitin Isopeptidase Y

The Regulation of TDP-43 Ubiquitinylation by UBE2E Ubiquitin-conjugating Enzymes and Ubiquitin Isopeptidase Y

TDP-43 pathology is associated with increased tau burdens and seeding

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