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

Carboxy terminus heat shock protein 70 interacting protein reduces tau-associated degenerative changes.

Journal of Alzheimer's disease : JAD - 1 Jan 2015

Saidi Laiq-Jan, Polydoro Manuela, Kay Kevin R, Sanchez Laura, Mandelkow Eva-Maria, Hyman Bradley T, Spires-Jones Tara L

Abstract excerpt

One of the hallmarks of Alzheimer's disease is the formation of neurofibrillary tangles, intracellular aggregates of hyperphosphorylated, mislocalized tau protein, which are associated with neuronal loss. Changes in tau are known to impair cellular transport (including that of mitochondria) and are associated with cell death in cell culture and mouse models of tauopathy. Thus clearing pathological forms of tau...

Read the complete abstract on PubMed

Topics

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

Share to Caspase 3
Share to Cell Proliferation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Green Fluorescent Proteins

Share to HSP70 Heat-Shock Proteins

Share to Mitochondria

Share to Neuroblastoma

Share to tau Proteins

Share to Ubiquitin-Protein Ligases

Source

Identifiers

PMID: 25374103
DOI: 10.3233/JAD-142094

Genes

TPR

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

Carboxy terminus heat shock protein 70 interacting protein reduces tau-associated degenerative changes.PMID 25374103Read ↗

Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: a mechanistic link between Abeta and tau pathology.Semantic proximity Read ↗

U‐box protein carboxyl terminus of Hsc70‐interacting protein (CHIP) mediates poly‐ubiquitylation preferentially on four‐repeat Tau and is involved in neurodegeneration of tauopathySemantic proximity Read ↗

CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival.Semantic proximity Read ↗

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation.Semantic proximity Read ↗

<i>In vivo</i> evidence of CHIP up‐regulation attenuating tau aggregationSemantic proximity Read ↗

Direct Visualization of CHIP-Mediated Degradation of Alpha-Synuclein In Vivo: Implications for PD TherapeuticsSemantic proximity Read ↗

Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species.Semantic proximity Read ↗

C-terminus of Hsp70 Interacting Protein (CHIP) and Neurodegeneration: Lessons from the Bench and Bedside.Semantic proximity Read ↗

CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo.Semantic proximity Read ↗

Evolutionarily conserved regulators of tau identify targets for new therapiesSemantic proximity Read ↗

Protein misfolding in neurodegenerative diseases: implications and strategiesSemantic proximity Read ↗

Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies.Semantic proximity Read ↗

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