Results 41 to 50 of about 48,475 (224)

TLS/FUS [PDF]

open access: yesCell Cycle, 2012
Comment on: Tan AY, et al. Proc Natl Acad Sci USA 2012; 109:6030-5.
Tan, Adelene Y., Manley, James L.
openaire   +2 more sources

Gene Therapy for Drug-Resistant Glioblastoma via Lipid-Polymer Hybrid Nanoparticles Combined with Focused Ultrasound

open access: yesInternational Journal of Nanomedicine, 2021
Qiang Yang,1 Yanghao Zhou,1 Jin Chen,1 Ning Huang,1 Zhigang Wang,2 Yuan Cheng1 1Department of Neurosurgery, The Second Affiliated Hospital of Chongqing Medical University, Chongqing 400010, People’s Republic of China; 2Institute of Ultrasound ...
Yang Q   +5 more
doaj  

Antiviral Immune Response as a Trigger of FUS Proteinopathy in Amyotrophic Lateral Sclerosis

open access: yesCell Reports, 2019
Summary: Mutations in the FUS gene cause familial amyotrophic lateral sclerosis (ALS-FUS). In ALS-FUS, FUS-positive inclusions are detected in the cytoplasm of neurons and glia, a condition known as FUS proteinopathy.
Tatyana A. Shelkovnikova   +5 more
doaj   +1 more source

Young-Onset Amyotrophic Lateral Sclerosis: Genetic Structure and Phenotypic Features [PDF]

open access: yesАнналы клинической и экспериментальной неврологии
Introduction. Young-onset amyotrophic lateral sclerosis (yALS) is a rare neurodegenerative disease characterized by the onset of clinical manifestations before the age of 45.
Denis V. Shevchuk   +5 more
doaj   +1 more source

FUS Interacts with HSP60 to Promote Mitochondrial Damage. [PDF]

open access: yesPLoS Genetics, 2015
FUS-proteinopathies, a group of heterogeneous disorders including ALS-FUS and FTLD-FUS, are characterized by the formation of inclusion bodies containing the nuclear protein FUS in the affected patients.
Jianwen Deng   +14 more
doaj   +1 more source

Circular RNA circNrip1 Interacts with SYNCRIP to Promote Neuropathic Pain by Stabilizing Tlr2 mRNA in Primary Sensory Neurons

open access: yesAdvanced Science, Volume 13, Issue 37, 3 July 2026.
Model of circNrip1 (cNrip1) upregulation driving neuropathic pain mechanisms. After peripheral nerve injury, increased FUS triggers the formation and upregulation of cNrip1 in injured DRG neurons. Upregulated cNrip1 recruits SYNCRIP to the 3′‐UTR of Tlr2 mRNA by binding to both, thereby promoting SYNCRIP‐triggered Tlr2 mRNA stability and increasing ...
Xiaozhou Feng   +14 more
wiley   +1 more source

Transportin 1 co-localisation with FUS inclusions is not characteristic for ALS-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it from FTLD-FUS [PDF]

open access: yes, 2012
Aims:  Transportin 1 (TNPO 1) is an abundant component of the Fused in Sarcoma (FUS)-immunopositive inclusions seen in a subgroup of frontotemporal lobar degeneration (FTLD-FUS).
Al-Sarraj, Safa   +5 more
core   +1 more source

TET3‐Mediated m5C Modification of CCAT2 Accelerates Cardiac Microvascular Endothelial Cell Damage in Acute Coronary Syndrome

open access: yesThe Kaohsiung Journal of Medical Sciences, Volume 42, Issue 5, May 2026.
ABSTRACT Acute coronary syndrome (ACS) is a clinical syndrome involving myocardial ischemia. This study aimed to elucidate the mechanism of TET3 in ACS‐induced CMEC damage, thereby identifying a new target for ACS treatment. The expression of TET3 in ACS patients and healthy subjects was analyzed.
Jun‐Cheng Liu   +5 more
wiley   +1 more source

HSP60 interacts with FUS, mediating FUS mitochondrial localization. [PDF]

open access: yes, 2016
(A) FUS-HSP60 interaction was detected by co-immunoprecipitation assay. Western blotting (WB) was performed using corresponding specific antibodies following immunoprecipitation of cell lysates with anti-GFP.(B)FUS-HSP60 interaction was detected by co ...
Marsel Mesulam (2207017)   +14 more
core   +1 more source

Full‐Length FUS Protein Condensates Adopt a Domain‐Preferential Spatial Architecture

open access: yesAggregate, Volume 6, Issue 12, December 2025.
We demonstrate a domain‐specific preferential distribution organization of FUS condensate and propose a sequence–structure–function paradigm for biomolecular condensates. ABSTRACT Biomolecular condensates play crucial roles in cellular physiology and are implicated in neurodegenerative diseases and cancer.
Si‐Cheng Tong   +5 more
wiley   +1 more source

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