Cargando…

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

The RNA binding protein TDP-43 forms cytoplasmic inclusions via its C-terminal prion-like domain in several neurodegenerative diseases. Aberrant TDP-43 aggregation arises upon phase de-mixing and transitions from liquid to solid states, following still unknown structural conversions which are primed...

Descripción completa

Detalles Bibliográficos
Autores principales:	Carrasco, Jaime, Antón, Rosa, Valbuena, Alejandro, Pantoja-Uceda, David, Mukhi, Mayur, Hervás, Rubén, Laurents, Douglas V., Gasset, María, Oroz, Javier
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group UK 2023
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9884275/ https://www.ncbi.nlm.nih.gov/pubmed/36709343 http://dx.doi.org/10.1038/s41467-023-36023-z

Ejemplares similares

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

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

Mechanistic Insights into the Role of Molecular Chaperones in Protein Misfolding Diseases: From Molecular Recognition to Amyloid Disassembly
por: Hervás, Rubén, et al.
Publicado: (2020)

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

The chaperone HSPB8 reduces the accumulation of truncated TDP-43 species in cells and protects against TDP-43-mediated toxicity
por: Crippa, Valeria, et al.
Publicado: (2016)

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

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

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

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

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

Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis
por: Park, Sei-Kyoung, et al.
Publicado: (2017)

Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program
por: Wang, Ping, et al.
Publicado: (2017)

TDP-43 and Limbic-Predominant Age-Related TDP-43 Encephalopathy
por: Zhang, Lumi, et al.
Publicado: (2020)

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

The Pathological Phenotypes of Human TDP-43 Transgenic Mouse Models Are Independent of Downregulation of Mouse Tdp-43
por: Xu, Ya-Fei, et al.
Publicado: (2013)

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

Structural transitions in Orb2 prion-like domain relevant for functional aggregation in memory consolidation
por: Oroz, Javier, et al.
Publicado: (2021)

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration
por: Gendron, Tania F., et al.
Publicado: (2011)

TDP-43 crosses the divide
por: Leslie, Mitch
Publicado: (2015)

TDP-43: From Alzheimer’s Disease to Limbic-Predominant Age-Related TDP-43 Encephalopathy
por: Huang, Wendi, et al.
Publicado: (2020)

TDP-43 mislocalization drives neurofilament changes in a novel model of TDP-43 proteinopathy
por: Atkinson, Rachel, et al.
Publicado: (2021)

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)

Recognition of the TDP-43 nuclear localization signal by importin α1/β
por: Doll, Steven G., et al.
Publicado: (2022)

Evidence of cerebellar TDP-43 loss of function in FTLD-TDP
por: Pickles, Sarah, et al.
Publicado: (2022)

Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation
por: Ramírez de Mingo, D., et al.
Publicado: (2022)

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)

TDP-43 and Phosphorylated TDP-43 Levels in Paired Plasma and CSF Samples in Amyotrophic Lateral Sclerosis
por: Ren, Yuting, et al.
Publicado: (2021)

TREM2 interacts with TDP-43 and mediates microglial neuroprotection against TDP-43-related neurodegeneration
por: Xie, Manling, et al.
Publicado: (2021)

Monomerization of TDP-43 is a key determinant for inducing TDP-43 pathology in amyotrophic lateral sclerosis
por: Oiwa, Kotaro, et al.
Publicado: (2023)

A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43
por: Furukawa, Yoshiaki, et al.
Publicado: (2016)

NMR Fragment-Based Screening against Tandem RNA Recognition Motifs of TDP-43
por: Nshogoza, Gilbert, et al.
Publicado: (2019)

Molecular Neuropathology of TDP-43 Proteinopathies
por: Neumann, Manuela
Publicado: (2009)

Mechanisms and models of TDP-43 proteinopathies
por: Petrucelli, Leonard
Publicado: (2012)

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

Metals in ALS TDP-43 Pathology
por: Koski, Lassi, et al.
Publicado: (2021)

TDP-43 Pathology in Alzheimer’s Disease
por: Meneses, Axel, et al.
Publicado: (2021)

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP
por: Arseni, Diana, et al.
Publicado: (2023)

α-Synuclein emulsifies TDP-43 prion-like domain – RNA liquid droplets to promote heterotypic amyloid fibrils
por: Dhakal, Shailendra, et al.
Publicado: (2023)

Divergent Phenotypes in Mutant TDP-43 Transgenic Mice Highlight Potential Confounds in TDP-43 Transgenic Modeling
por: D’Alton, Simon, et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_f1hh762ojsgm986t2bkrgcum67