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

Transcriptional profiles for distinct aggregation states of mutant Huntingtin exon 1 protein unmask new Huntington's disease pathways.

Molecular and cellular neurosciences - 1 Sept 2017

Moily Nagaraj S, Ormsby Angelique R, Stojilovic Aleksandar, Ramdzan Yasmin M, Diesch Jeannine, Hannan Ross D, Zajac Michelle S, Hannan Anthony J, Oshlack Alicia, Hatters Danny M

Abstract excerpt

Huntington's disease is caused by polyglutamine (polyQ)-expansion mutations in the CAG tandem repeat of the Huntingtin gene. The central feature of Huntington's disease pathology is the aggregation of mutant Huntingtin (Htt) protein into micrometer-sized inclusion bodies. Soluble mutant Htt states are most proteotoxic and trigger an enhanced risk of death whereas inclusions confer different changes to cellular...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line, Tumor
Share to Cyclic AMP Response Element-Binding Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Huntingtin Protein

Share to Huntington Disease

Share to Protein Aggregation, Pathological

Share to Signal Transduction

Share to Transcriptome

Source

Identifiers

PMID: 28743452
DOI: 10.1016/j.mcn.2017.07.004

Genes

BRD4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Transcriptional profiles for distinct aggregation states of mutant Huntingtin exon 1 protein unmask new Huntington's disease pathways.PMID 28743452Read ↗

Biphasic Temporal Remodeling Of The Proteome In A Polyglutamine-Expanded Huntingtin In Vitro Aggregation Cell Model: From Early Rna-Regulatory Compensation To Selective Mitochondrial Energy FailureSemantic proximity Read ↗

The huntingtin–HAP40 complex is a bidirectional cellular rheostatSemantic proximity Read ↗

Misfolded polyglutamine, polyalanine, and superoxide dismutase 1 aggregate via distinct pathways in the cell.Semantic proximity Read ↗

The dynamics of early-state transcriptional changes and aggregate formation in a Huntington's disease cell model.Semantic proximity Read ↗

Heat shock promotes inclusion body formation of mutant huntingtin (mHtt) and alleviates mHtt-induced transcription factor dysfunction.Semantic proximity Read ↗

Multimodal spatial transcriptomics determines repeat expansion, huntingtin aggregation, and selective cortical neuron loss in Huntington’s DiseaseSemantic proximity Read ↗

Pluripotent stem cell derived models of neurological diseases reveal early transcriptional heterogeneitySemantic proximity Read ↗

Structure-function dissection of huntingtin exon 1 identifies a PRD-driven modifier of neuronal toxicity in Huntington’s diseaseSemantic proximity Read ↗

Polyglutamine aggregation in Huntington and related diseases.Semantic proximity Read ↗

Comparative Huntington and Parkinson Disease mRNA Analysis Reveals Common Inflammatory ProcessesSemantic proximity Read ↗

Integrated Stress Response Signatures Drive Monocyte Dysfunction in GBA1- and LRRK2-Linked Parkinson’s DiseaseSemantic proximity Read ↗

Huntingtin and mutant SOD1 form aggregate structures with distinct molecular properties in human cells.Semantic proximity Read ↗

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