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

Protein misfolding in neurodegenerative diseases: implications and strategies

13 Mar 2017

Abstract excerpt

A hallmark of neurodegenerative proteinopathies is the formation of misfolded protein aggregates that cause cellular toxicity and contribute to cellular proteostatic collapse. Therapeutic options are currently being explored that target different steps in the production and processing of proteins implicated in neurodegenerative disease, including synthesis, chaperone-assisted folding and trafficking, and...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Endoplasmic Reticulum Stress and Disease
Share to Ubiquitin and proteasome pathways

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28293421
DOI: 10.1186/s40035-017-0077-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protein misfolding in neurodegenerative diseases: implications and strategiesPMID 28293421Read ↗

[Neurodegenerative conformational disease and heat shock proteins].Semantic proximity Read ↗

Dealing with misfolded proteins: examining the neuroprotective role of molecular chaperones in neurodegeneration.Semantic proximity Read ↗

Protein-misfolding diseases and chaperone-based therapeutic approaches.Semantic proximity Read ↗

Molecular mechanisms of proteinopathies across neurodegenerative disease: a reviewSemantic proximity Read ↗

The intrinsic and extrinsic factors that contribute to proteostasis decline and pathological protein misfolding.Semantic proximity Read ↗

Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.Semantic proximity Read ↗

Small HSPs at the crossroad between protein aggregation, autophagy and unconventional secretion: clinical implications and potential therapeutic opportunities in the context of neurodegenerative diseasesSemantic proximity Read ↗

The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease.Semantic proximity Read ↗

Protein folding alterations in amyotrophic lateral sclerosis.Semantic proximity Read ↗

The two faces of protein misfolding: gain‐ and loss‐of‐function in neurodegenerative diseasesSemantic proximity Read ↗

[Conformationally altered proteins cause neurodegenerative diseases].Semantic proximity Read ↗

Induction of Molecular Chaperones as a Therapeutic Strategy for the Polyglutamine DiseasesSemantic proximity Read ↗

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