Cargando…

Post-transcriptional modifications caused by TDP-43 mutations in mouse and man

Detalles Bibliográficos
Autor principal:	Fratta, Pietro
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Springer International Publishing 2015
Materias:	Lecture Presentation
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4797232/ https://www.ncbi.nlm.nih.gov/pubmed/27386215 http://dx.doi.org/10.1186/2193-1801-4-S1-L52

Ejemplares similares

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

Elucidating the mechanisms of TDP-43 aggregation in a cellular model of motor neuron disease
por: Hicks, David, et al.
Publicado: (2015)

Quantitative analysis of cryptic splicing associated with TDP-43 depletion
por: Humphrey, Jack, et al.
Publicado: (2017)

A Nonsense Mutation in Mouse Tardbp Affects TDP43 Alternative Splicing Activity and Causes Limb-Clasping and Body Tone Defects
por: Ricketts, Thomas, et al.
Publicado: (2014)

Structural Insights Into TDP-43 and Effects of Post-translational Modifications
por: François-Moutal, Liberty, et al.
Publicado: (2019)

Corrigendum: Structural Insights Into TDP-43 and Effects of Post-translational Modifications
por: François-Moutal, Liberty, et al.
Publicado: (2020)

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)

Pathological Modification of TDP-43 in Amyotrophic Lateral Sclerosis with SOD1 Mutations
por: Jeon, Gye Sun, et al.
Publicado: (2018)

Analysis of TDP-43 and its binding partners in neurodegenerative diseases
por: Kattuah, Wejdan, et al.
Publicado: (2013)

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 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)

IL-10 secreting regulatory B cells are potent arbiters of autoimmunity in both mouse and man
por: Mauri, Claudia, et al.
Publicado: (2011)

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

Phosphorylation of hnRNP K controls cytosolic accumulation of TDP-43
por: White, Anthony, et al.
Publicado: (2013)

β - but not γ-secretase proteolysis of APP causes synaptic and memory deficits in a mouse model of dementia
por: Tamayev, Robert, et al.
Publicado: (2012)

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

TDP-43 misexpression causes defects in dendritic growth
por: Herzog, Josiah J., et al.
Publicado: (2017)

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

Cell environment shapes TDP-43 function with implications in neuronal and muscle disease
por: Šušnjar, Urša, et al.
Publicado: (2022)

Aggregation of TDP-43 fragments triggers cellular aberrant function: implication in neurodegeneration
por: Che, Meixia, et al.
Publicado: (2012)

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)

Widespread RNA metabolism impairment in sporadic inclusion body myositis TDP43-proteinopathy()
por: Cortese, Andrea, et al.
Publicado: (2014)

A robust TDP-43 knock-in mouse model of ALS
por: Huang, Shih-Ling, et al.
Publicado: (2020)

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)

Does a loss of TDP-43 function cause neurodegeneration?
por: Xu, Zuo-Shang
Publicado: (2012)

Progranulin deficiency causes impairment of autophagy and TDP-43 accumulation
por: Chang, Michael C., et al.
Publicado: (2017)

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

Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43(A315T) ALS/FTD mouse model
por: Bargsted, Leslie, et al.
Publicado: (2017)

NOS1AP is a novel molecular target and critical factor in TDP-43 pathology
por: Cappelli, Sara, et al.
Publicado: (2022)

Mis-spliced transcripts generate de novo proteins in TDP-43-related ALS/FTD
por: Seddighi, Sahba, et al.
Publicado: (2023)

Mice Carrying ALS Mutant TDP-43, but Not Mutant FUS, Display In Vivo Defects in Axonal Transport of Signaling Endosomes
por: Sleigh, James N., et al.
Publicado: (2020)

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)

Cannot write session to /tmp/vufind_sessions/sess_nees00aobpf9lindpu1t3qn1ri