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

Huntingtin fragments that aggregate go their separate ways.

Molecular cell - 1 Aug 2002

DiFiglia Marian

Abstract excerpt

N-terminal region of mutant huntingtin forms intranuclear and cytoplasmic aggregates in neurons that may contribute to neuronal death in Huntington's disease. show that different endoprotease-cleaved huntingtin fragments form nuclear and cytoplasmic inclusions.

Read the complete abstract on PubMed

Topics

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

Share to Cell Nucleus
Share to Cytoplasm
Share to Huntingtin Protein
Share to Inclusion Bodies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nerve Tissue Proteins

Share to Neurons

Share to Nuclear Proteins

Share to Peptide Fragments

Source

Identifiers

PMID: 12191468
DOI: 10.1016/s1097-2765(02)00609-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Huntingtin fragments that aggregate go their separate ways.PMID 12191468Read ↗

Huntington's Disease Intranuclear Inclusions Contain Truncated, Ubiquitinated Huntingtin ProteinSemantic proximity Read ↗

Are there multiple pathways in the pathogenesis of Huntington'sdisease?Semantic proximity Read ↗

Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions.Semantic proximity Read ↗

Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.Semantic proximity Read ↗

Complex interplay between the length and composition of the huntingtin-derived peptides modulates the intracellular behavior of the N-terminal fragments of mutant huntingtin.Semantic proximity Read ↗

Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell cultureSemantic proximity Read ↗

Lowering Mutant Huntingtin Levels and Toxicity: Autophagy-Endolysosome Pathways in Huntington's DiseaseSemantic proximity Read ↗

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

Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle.Semantic proximity Read ↗

Huntingtin processing in pathogenesis of Huntington disease.Semantic proximity Read ↗

Huntingtin forms toxic NH2-terminal fragment complexes that are promoted by the age-dependent decrease in proteasome activity.Semantic proximity Read ↗

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death.Semantic proximity Read ↗

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