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

Phase to Phase with TDP-43.

Biochemistry - 14 Feb 2017

Sun Yulong, Chakrabartty Avijit

Abstract excerpt

TDP-43 is a dimeric nuclear protein that plays a central role in RNA metabolism. In recent years, this protein has become a focal point of research in the amyotrophic lateral sclerosis and frontotemporal dementia (ALS/FTD) disease spectrum, as pathognomonic inclusions within affected neurons contain post-translationally modified TDP-43. A key question in TDP-43 research involves determining the mechanisms and...

Read the complete abstract on PubMed

Topics

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

Share to Protein Folding
Share to Protein Aggregation, Pathological
Share to Amyotrophic Lateral Sclerosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Frontotemporal Dementia

Share to Nerve Tissue Proteins

Share to Neurons

Share to Protein Interaction Domains and Motifs

Share to RNA-Binding Proteins

Source

Identifiers

PMID: 28112502
DOI: 10.1021/acs.biochem.6b01088

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phase to Phase with TDP-43.PMID 28112502Read ↗

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.Semantic proximity Read ↗

Phase Behavior of TDP-43 and hnRNPH1: From Soluble and Aggregated States to Liquid-Like DropletsSemantic proximity Read ↗

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

Cellular modifiers of TDP-43 phase transition and cytoplasmic aggregationSemantic proximity Read ↗

Molecular Dissection of TDP-43 as a Leading Cause of ALS/FTLDSemantic proximity Read ↗

TDP-43 oligomers detected as initial intermediate species during aggregate formationSemantic proximity Read ↗

Disrupting pathologic phase transitions in neurodegenerationSemantic proximity Read ↗

Synaptic Paths to Neurodegeneration: The Emerging Role of TDP-43 and FUS in Synaptic FunctionsSemantic proximity Read ↗

Molecular Mechanisms of Protein Aggregation in ALS-FTD: Focus on TDP-43 and Cellular Protective ResponsesSemantic proximity Read ↗

Stress Induces Dynamic, Cytotoxicity-Antagonizing TDP-43 Nuclear Bodies via Paraspeckle LncRNA NEAT1-Mediated Liquid-Liquid Phase Separation.Semantic proximity Read ↗

Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregationSemantic proximity Read ↗

The implications of physiological biomolecular condensates in amyotrophic lateral sclerosis.Semantic proximity Read ↗

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