Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Evidence of A Negative Feedback Network Between TDP-43 and miRNAs Dependent on TDP-43 Nuclear Localization

31 Oct 2020

Abstract excerpt

TAR DNA-binding protein 43 (TDP-43) is a DNA/RNA-binding protein that is integral to RNA processing. Among these functions is a critical role in microRNA (miRNA) biogenesis through interactions with the DROSHA and DICER complexes. It has been previously shown that there is a general reduction in miRNA levels within the spinal cord and spinal motor neurons of amyotrophic lateral sclerosis (ALS) patients. In...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyotrophic Lateral Sclerosis Research
Share to Cancer-related gene regulation
Share to Neurogenetic and Muscular Disorders Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 33137311
DOI: 10.1016/j.jmb.2020.10.029

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence of A Negative Feedback Network Between TDP-43 and miRNAs Dependent on TDP-43 Nuclear LocalizationPMID 33137311Read ↗

TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexesSemantic proximity Read ↗

Proteomics Analysis of the TDP ‐43 Interactome in Cellular Models of ALS PathogenesisSemantic proximity Read ↗

Nuclear factor TDP‐43 can affect selected microRNA levelsSemantic proximity Read ↗

TDP-43—The key to understanding amyotrophic lateral sclerosisSemantic proximity Read ↗

Cytoplasmic TDP43 Binds microRNAs: New Disease Targets in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

The role of TDP-43 in the pathogenesis of ALS and FTLDSemantic proximity Read ↗

Alteration of POLDIP3 Splicing Associated with Loss of Function of TDP-43 in Tissues Affected with ALSSemantic proximity Read ↗

Differential toxicity of TAR DNA-binding protein 43 isoforms depends on their submitochondrial localization in neuronal cells.Semantic proximity Read ↗

An ALS-linked mutation in TDP-43 disrupts normal protein interactions in the motor neuron response to oxidative stress.Semantic proximity Read ↗

TDP-43 and ER Stress in Neurodegeneration: Friends or Foes?Semantic proximity Read ↗

Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation.Semantic proximity Read ↗

Altered TDP-43 Structure and Function: Key Insights into Aberrant RNA, Mitochondrial, and Cellular and Systemic Metabolism in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.