Folliculin, a tumor suppressor associated with Birt-Hogg-Dubé (BHD) syndrome, is a novel modifier of TDP-43 cytoplasmic translocation and aggregation. (Q52147386)

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scientific article published on 29 October 2015

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English	Folliculin, a tumor suppressor associated with Birt-Hogg-Dubé (BHD) syndrome, is a novel modifier of TDP-43 cytoplasmic translocation and aggregation.	scientific article published on 29 October 2015

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

Folliculin, a tumor suppressor associated with Birt-Hogg-Dubé (BHD) syndrome, is a novel modifier of TDP-43 cytoplasmic translocation and aggregation. (English)

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

author name string

Qin Xia

1

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

Guanghui Wang

2

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

Hongfeng Wang

3

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

Qingsong Hu

4

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

Zheng Ying

5

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

publication date

29 October 2015

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Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

Human Molecular Genetics

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Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

25

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Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

1

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

83-96

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis

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Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

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Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation

1 reference

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Characterizing the RNA targets and position-dependent splicing regulation by TDP-43.

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Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9

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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

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

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Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis

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Molecular neuropathology of TDP-43 proteinopathies

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Rethinking ALS: the FUS about TDP-43.

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TDP-43 is recruited to stress granules in conditions of oxidative insult.

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TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor

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TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1.

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Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue

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21 January 2018

Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates

1 reference

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21 January 2018

TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies

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21 January 2018

TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

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21 January 2018

Understanding the role of TDP-43 and FUS/TLS in ALS and beyond.

1 reference

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21 January 2018

Cell stress induces TDP-43 pathological changes associated with ERK1/2 dysfunction: implications in ALS.

1 reference

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21 January 2018

High-content RNAi screening identifies the Type 1 inositol triphosphate receptor as a modifier of TDP-43 localization and neurotoxicity

1 reference

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21 January 2018

Activation of AMP-activated protein kinase α1 mediates mislocalization of TDP-43 in amyotrophic lateral sclerosis.

1 reference

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21 January 2018

Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system.

1 reference

https://api.crossref.org/works/10.1093%2FHMG%2FDDV450

21 January 2018

Differential roles of the ubiquitin proteasome system and autophagy in the clearance of soluble and aggregated TDP-43 species

1 reference

https://api.crossref.org/works/10.1093%2FHMG%2FDDV450

21 January 2018

Autophagy activation ameliorates neuronal pathogenesis of FTLD-U mice: a new light for treatment of TARDBP/TDP-43 proteinopathies

1 reference

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21 January 2018

Regulation of autophagy by neuropathological protein TDP-43.

1 reference

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21 January 2018

Folliculin regulates ampk-dependent autophagy and metabolic stress survival

1 reference

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21 January 2018

FLCN, a novel autophagy component, interacts with GABARAP and is regulated by ULK1 phosphorylation

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21 January 2018

Nucleolar stress and impaired stress granule formation contribute to C9orf72 RAN translation-induced cytotoxicity

1 reference

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21 January 2018

G3BP1 promotes stress-induced RNA granule interactions to preserve polyadenylated mRNA.

1 reference

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21 January 2018

Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1.

1 reference

https://api.crossref.org/works/10.1093%2FHMG%2FDDV450

21 January 2018

Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly

1 reference

https://api.crossref.org/works/10.1093%2FHMG%2FDDV450

21 January 2018

Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function

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21 January 2018

TDP-43 aggregation in neurodegeneration: are stress granules the key?

1 reference

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21 January 2018

Altered ribostasis: RNA-protein granules in degenerative disorders

1 reference

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21 January 2018

Stress granules as crucibles of ALS pathogenesis.

1 reference

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21 January 2018

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

1 reference

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21 January 2018

TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing

1 reference

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Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS).

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Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6

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Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43.

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Axonal transport of TDP-43 mRNA granules is impaired by ALS-causing mutations

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Roles of ataxin-2 in pathological cascades mediated by TAR DNA-binding protein 43 (TDP-43) and Fused in Sarcoma (FUS)

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Phosphorylation of hnRNP K by cyclin-dependent kinase 2 controls cytosolic accumulation of TDP-43.

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TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97.

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VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death

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Cytoplasmic translocation, aggregation, and cleavage of TDP-43 by enteroviral proteases modulate viral pathogenesis

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Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo

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Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration

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Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP

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Exit from pluripotency is gated by intracellular redistribution of the bHLH transcription factor Tfe3

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The tumor suppressor folliculin regulates AMPK-dependent metabolic transformation

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The folliculin tumor suppressor is a GAP for the RagC/D GTPases that signal amino acid levels to mTORC1.

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Recruitment of folliculin to lysosomes supports the amino acid-dependent activation of Rag GTPases

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DJ-1, a cancer and Parkinson's disease associated protein, regulates autophagy through JNK pathway in cancer cells

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Identifiers

10.1093/HMG/DDV450

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 April 2018

http://europepmc.org/abstract/MED/26516189

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