Movement disorders are linked to TDP-43 burden in the substantia nigra of FTLD-TDP brain donors

to related objects

Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource, 1 online resource.

Language: Englisch

Bibliographic citation: Movement disorders are linked to TDP-43 burden in the substantia nigra of FTLD-TDP brain donors ; volume:11 ; number:1 ; day:12 ; month:4 ; year:2023 ; pages:1-9 ; date:12.2023
Acta Neuropathologica Communications ; 11, Heft 1 (12.4.2023), 1-9, 12.2023

Creator: Fiondella, Luigi
Gami-Patel, Priya
Blok, Christian A.
Rozemuller, Annemieke J. M.
Hoozemans, Jeroen J. M.
Pijnenburg, Yolande A. L.
Scarioni, Marta
Dijkstra, Anke A.

Contributor: SpringerLink (Online service)

DOI: 10.1186/s40478-023-01560-7

URN: urn:nbn:de:101:1-2023082609144413744600

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

Last update: 14.08.2025, 10:54 AM CEST

Data provider

This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.

Show original at data provider

Associated

Fiondella, Luigi
Gami-Patel, Priya
Blok, Christian A.
Rozemuller, Annemieke J. M.
Hoozemans, Jeroen J. M.
Pijnenburg, Yolande A. L.
Scarioni, Marta
Dijkstra, Anke A.
SpringerLink (Online service)

Other Objects (12)

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

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

Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43A315T ALS/FTD mouse model

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

Heteromeric amyloid filaments of ANXA11 and TDP-43 in FTLD-TDP type C

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

Archivale

TB-22 T.D.P. Glas und Isolierstoffe

Archivale

TB-22 T.D.P. Glas und Isolierstoffe

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

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

Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43A315T ALS/FTD mouse model

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

Heteromeric amyloid filaments of ANXA11 and TDP-43 in FTLD-TDP type C

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

Archivale

TB-22 T.D.P. Glas und Isolierstoffe

Archivale

TB-22 T.D.P. Glas und Isolierstoffe

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

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

Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43A315T ALS/FTD mouse model

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

Heteromeric amyloid filaments of ANXA11 and TDP-43 in FTLD-TDP type C

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

Archivale

TB-22 T.D.P. Glas und Isolierstoffe

Archivale

TB-22 T.D.P. Glas und Isolierstoffe

Cultural heritage institutions wishing to register will find more information here.

Fields marked * need to be filled in.

Username*

Please enter your username

Email*

Please enter your email address

Please do not fill this field

First name

Last name

Password*

Please enter your password

Confirm password*

Please enter the same password

I have read the terms of use and the privacy policy for the collection of personal data and accept them. *

This field is required.

I would like to subscribe to the newsletter of the Deutsche Digitale Bibliothek. See newsletter subscription info.

Account created

Your "My DDB" account has been successfully created. Before you can log in to your account, you must click the confirmation link in the message we just sent to the email address you provided.

Movement disorders are linked to TDP-43 burden in the substantia nigra of FTLD-TDP brain donors

Object Details

References and Relationships

Contributors, Places and Time

Further information

Data provider

Associated

Other Objects (12)

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

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

Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43A315T ALS/FTD mouse model

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

Heteromeric amyloid filaments of ANXA11 and TDP-43 in FTLD-TDP type C

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

TB-22 T.D.P. Glas und Isolierstoffe

TB-22 T.D.P. Glas und Isolierstoffe

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

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

Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43A315T ALS/FTD mouse model

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

Heteromeric amyloid filaments of ANXA11 and TDP-43 in FTLD-TDP type C

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

TB-22 T.D.P. Glas und Isolierstoffe

TB-22 T.D.P. Glas und Isolierstoffe

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

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

Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43A315T ALS/FTD mouse model

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

Heteromeric amyloid filaments of ANXA11 and TDP-43 in FTLD-TDP type C

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

TB-22 T.D.P. Glas und Isolierstoffe

TB-22 T.D.P. Glas und Isolierstoffe

Related objects

Reset password