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

HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.

The Journal of biological chemistry - 23 Feb 2018

Baughman Hannah E R, Clouser Amanda F, Klevit Rachel E, Nath Abhinav

Abstract excerpt

The microtubule-associated protein tau forms insoluble, amyloid-type aggregates in various dementias, most notably Alzheimer's disease. Cellular chaperone proteins play important roles in maintaining protein solubility and preventing aggregation in the crowded cellular environment. Although tau is known to interact with numerous chaperones, it remains unclear how these chaperones function mechanistically to...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Anticoagulants
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heparin

Share to HSC70 Heat-Shock Proteins

Share to HSP27 Heat-Shock Proteins

Share to Protein Aggregation, Pathological

Share to Solubility

Source

Open in PubMed Open full text

Identifiers

PMID: 29298892
DOI: 10.1074/jbc.M117.803411
PMCID: PMC5827454

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

HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.PMID 29298892Read ↗

Hsp40s play complementary roles in the prevention of tau amyloid formation.Semantic proximity Read ↗

Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent speciesSemantic proximity Read ↗

Synergistic MAPT mutations as a platform to uncover modifiers of tau pathogenesisSemantic proximity Read ↗

Small heat shock protein HspB8: its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity.Semantic proximity Read ↗

Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic InterventionSemantic proximity Read ↗

Inhibition of α-synuclein aggregation by small heat shock proteins.Semantic proximity Read ↗

Mechanistic studies unravel the complexity inherent in tau aggregation leading to Alzheimer's disease and the tauopathies.Semantic proximity Read ↗

Modulation of amyloid-β protein precursor expression by HspB1.Semantic proximity Read ↗

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

Dihydropyridine Derivatives Modulate Heat Shock Responses and have a Neuroprotective Effect in a Transgenic Mouse Model of Alzheimer's Disease.Semantic proximity Read ↗

HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cellsSemantic proximity Read ↗

Small heat shock proteins in neurodegenerative diseases.Semantic proximity Read ↗

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