Cargando…

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

TDP-43 aggregates are the neurohistological landmark of diseases like amyotrophic lateral sclerosis and frontotemporal dementia. Their role in the pathogenesis of these conditions is not yet clear mainly due to the lack of proper models of aggregation that may allow the study of the mechanism of for...

Descripción completa

Detalles Bibliográficos
Autores principales:	Budini, Mauricio, Romano, Valentina, Quadri, Zainuddin, Buratti, Emanuele, Baralle, Francisco E.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Oxford University Press 2015
Materias:	Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4262490/ https://www.ncbi.nlm.nih.gov/pubmed/25122661 http://dx.doi.org/10.1093/hmg/ddu415

Ejemplares similares

TDP-43 aggregation mirrors TDP-43 knockdown, affecting the expression levels of a common set of proteins
por: Prpar Mihevc, S., et al.
Publicado: (2016)

Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation
por: Mompeán, Miguel, et al.
Publicado: (2016)

Autophagy and Its Impact on Neurodegenerative Diseases: New Roles for TDP-43 and C9orf72
por: Budini, Mauricio, et al.
Publicado: (2017)

Chaperone Mediated Autophagy Degrades TDP-43 Protein and Is Affected by TDP-43 Aggregation
por: Ormeño, Fernando, et al.
Publicado: (2020)

The Cellular Prion Protein Increases the Uptake and Toxicity of TDP-43 Fibrils
por: Scialò, Carlo, et al.
Publicado: (2021)

Characterizing TDP-43 interaction with its RNA targets
por: Bhardwaj, Amit, et al.
Publicado: (2013)

Drosophila Answers to TDP-43 Proteinopathies
por: Romano, Maurizio, et al.
Publicado: (2012)

TDP-43 affects splicing profiles and isoform production of genes involved in the apoptotic and mitotic cellular pathways
por: De Conti, Laura, et al.
Publicado: (2015)

Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes
por: Neumann, Manuela, et al.
Publicado: (2020)

An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds
por: Mompeán, Miguel, et al.
Publicado: (2016)

Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
por: Mercado, Pablo Arrisi, et al.
Publicado: (2005)

Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
por: D’Ambrogio, Andrea, et al.
Publicado: (2009)

Predominance of spliceosomal complex formation over polyadenylation site selection in TDP-43 autoregulation
por: Bembich, Sara, et al.
Publicado: (2014)

Phe-Gly motifs drive fibrillization of TDP-43’s prion-like domain condensates
por: Pantoja-Uceda, David, et al.
Publicado: (2021)

TDP-43 Regulates Drosophila Neuromuscular Junctions Growth by Modulating Futsch/MAP1B Levels and Synaptic Microtubules Organization
por: Godena, Vinay K., et al.
Publicado: (2011)

A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defects
por: Langellotti, Simona, et al.
Publicado: (2016)

Parkin beyond Parkinson’s Disease—A Functional Meaning of Parkin Downregulation in TDP-43 Proteinopathies
por: Gaweda-Walerych, Katarzyna, et al.
Publicado: (2021)

DCTN1 Binds to TDP-43 and Regulates TDP-43 Aggregation
por: Deshimaru, Manami, et al.
Publicado: (2021)

Profilin 1 mutants form aggregates that induce accumulation of prion-like TDP-43
por: Tanaka, Yoshinori, et al.
Publicado: (2016)

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation
por: Gruijs da Silva, Lara A, et al.
Publicado: (2022)

TDP-43 Proteinopathy Specific Biomarker Development
por: Cordts, Isabell, et al.
Publicado: (2023)

TDP-43 Epigenetic Facets and Their Neurodegenerative Implications
por: Gimenez, Juliette, et al.
Publicado: (2023)

In vitro prion-like behaviour of TDP-43 in ALS
por: Smethurst, Phillip, et al.
Publicado: (2016)

Reviewing the Potential Links between Viral Infections and TDP-43 Proteinopathies
por: Rahic, Zerina, et al.
Publicado: (2023)

A C-Terminally Truncated TDP-43 Splice Isoform Exhibits Neuronal Specific Cytoplasmic Aggregation and Contributes to TDP-43 Pathology in ALS
por: Shenouda, Marc, et al.
Publicado: (2022)

The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation
por: Rengifo-Gonzalez, Juan Carlos, et al.
Publicado: (2021)

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43
por: Keating, Sean S., et al.
Publicado: (2023)

Inflammation Induces TDP-43 Mislocalization and Aggregation
por: Correia, Ana Sofia, et al.
Publicado: (2015)

Which TDP-43 aggregates are toxic in ALS?
por: Valle, Cristiana, et al.
Publicado: (2016)

Sirtuin-1 sensitive lysine-136 acetylation drives phase separation and pathological aggregation of TDP-43
por: Garcia Morato, Jorge, et al.
Publicado: (2022)

Detection and quantification of novel C‐terminal TDP‐43 fragments in ALS‐TDP
por: Feneberg, Emily, et al.
Publicado: (2021)

Metamorphism in TDP-43 prion-like domain determines chaperone recognition
por: Carrasco, Jaime, et al.
Publicado: (2023)

Lack of TAR-DNA binding protein-43 (TDP-43) pathology in human prion diseases
por: Isaacs, A M, et al.
Publicado: (2008)

SUMOylation Regulates TDP-43 Splicing Activity and Nucleocytoplasmic Distribution
por: Maraschi, AnnaMaria, et al.
Publicado: (2021)

Physiological tissue-specific and age-related reduction of mouse TDP-43 levels is regulated by epigenetic modifications
por: Pacetti, Miriam, et al.
Publicado: (2022)

Inhibition of TDP-43 Aggregation by Nucleic Acid Binding
por: Huang, Yi-Chen, et al.
Publicado: (2013)

TDP-43 is intercellularly transmitted across axon terminals
por: Feiler, Marisa S., et al.
Publicado: (2015)

Optineurin Deficiency and Insufficiency Lead to Higher Microglial TDP-43 Protein Levels
por: Prtenjaca, Nikolina, et al.
Publicado: (2022)

Major hnRNP proteins act as general TDP-43 functional modifiers both in Drosophila and human neuronal cells
por: Appocher, Chiara, et al.
Publicado: (2017)

Cytotoxic immune cells do not affect TDP-43 and p62 sarcoplasmic aggregation but influence TDP-43 localisation
por: McCord, Bryony, et al.
Publicado: (2023)

Cannot write session to /tmp/vufind_sessions/sess_885ljpp99p5smoi1smeenpj1qi