Cargando…

Redox-mediated regulation of an evolutionarily conserved cross-β structure formed by the TDP43 low complexity domain

A methionine-rich low complexity (LC) domain is found within a C-terminal region of the TDP43 RNA-binding protein. Self-association of this domain leads to the formation of labile cross-β polymers and liquid-like droplets. Treatment with H(2)O(2) caused phenomena of methionine oxidation and droplet...

Descripción completa

Detalles Bibliográficos
Autores principales:	Lin, Yi, Zhou, Xiaoming, Kato, Masato, Liu, Daifei, Ghaemmaghami, Sina, Tu, Benjamin P., McKnight, Steven L.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	National Academy of Sciences 2020
Materias:	Biological Sciences
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7682574/ https://www.ncbi.nlm.nih.gov/pubmed/33144500 http://dx.doi.org/10.1073/pnas.2012216117

Ejemplares similares

Oxidative regulation of TDP-43 self-association by a β-to-α conformational switch
por: Gu, Jinge, et al.
Publicado: (2023)

Oxidative regulation of TDP-43 self-association by a β-to-α conformational switch
por: Gu, Jinge, et al.
Publicado: (2023)

Structural insights into TDP-43 in nucleic-acid binding and domain interactions
por: Kuo, Pan-Hsien, et al.
Publicado: (2009)

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

RNA-binding deficient TDP-43 drives cognitive decline in a mouse model of TDP-43 proteinopathy
por: Necarsulmer, Julie C, et al.
Publicado: (2023)

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

The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores
por: Kato, Masato, et al.
Publicado: (2021)

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

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

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43
por: Li, Qiuye, et al.
Publicado: (2021)

Stage-specific control of oligodendrocyte survival and morphogenesis by TDP-43
por: Heo, Dongeun, et al.
Publicado: (2022)

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 basis of clinicopathological heterogeneity in TDP-43 proteinopathy
por: Kawakami, Ito, et al.
Publicado: (2019)

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

Functional implication of ubiquitinating and deubiquitinating mechanisms in TDP-43 proteinopathies
por: Tran, Non-Nuoc, et al.
Publicado: (2022)

How do protein domains of low sequence complexity work?
por: Kato, Masato, et al.
Publicado: (2022)

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

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

TDP-43 self-interaction is modulated by redox-active compounds Auranofin, Chelerythrine and Riluzole
por: Oberstadt, Moritz, et al.
Publicado: (2018)

Transiently structured head domains control intermediate filament assembly
por: Zhou, Xiaoming, et al.
Publicado: (2021)

The Role of HDAC6 in TDP-43-Induced Neurotoxicity and UPS Impairment
por: Lee, Shinrye, et al.
Publicado: (2020)

Wnt/β-catenin signaling is an evolutionarily conserved determinant of chordate dorsal organizer
por: Kozmikova, Iryna, et al.
Publicado: (2020)

Cilia Distal Domain: Diversity in Evolutionarily Conserved Structures
por: Soares, Helena, et al.
Publicado: (2019)

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

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

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

TDP-43 mislocalization drives neurofilament changes in a novel model of TDP-43 proteinopathy
por: Atkinson, Rachel, 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)

TDP-43 α-helical structure tunes liquid–liquid phase separation and function
por: Conicella, Alexander E., et al.
Publicado: (2020)

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

TDP-43 stabilises the processing intermediates of mitochondrial transcripts
por: Izumikawa, Keiichi, et al.
Publicado: (2017)

Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments
por: Sysoev, Vasiliy O., et al.
Publicado: (2020)

TDP-43 accelerates age-dependent degeneration of interneurons
por: Tsuiji, Hitomi, et al.
Publicado: (2017)

TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle
por: Vogler, Thomas O., et al.
Publicado: (2018)

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)

TDP43 Exacerbates Atherosclerosis Progression by Promoting Inflammation and Lipid Uptake of Macrophages
por: Huangfu, Ning, et al.
Publicado: (2021)

Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons
por: Vishal, Sonali S., et al.
Publicado: (2022)

CRELD1 is an evolutionarily-conserved maturational enhancer of ionotropic acetylcholine receptors
por: D'Alessandro, Manuela, et al.
Publicado: (2018)

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)

Cannot write session to /tmp/vufind_sessions/sess_b2lkjb3vkip8lo1efje5s6t376