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

Membrane interaction and disulphide-bridge formation in the unconventional secretion of Tau.

Bioscience reports - 27 Aug 2021

Hellén Marianna, Bhattacharjee Arnab, Uronen Riikka-Liisa, Huttunen Henri J

Abstract excerpt

Misfolded, pathological tau protein propagates from cell to cell causing neuronal degeneration in Alzheimer's disease and other tauopathies. The molecular mechanisms of this process have remained elusive. Unconventional secretion of tau takes place via several different routes, including direct penetration through the plasma membrane. Here, we show that tau secretion requires membrane interaction via disulphide...

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to Disulfides
Share to Protein Conformation, alpha-Helical

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Folding

Share to Protein Interaction Domains and Motifs

Share to Secretory Pathway

Share to Structure-Activity Relationship

Share to tau Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 34308969
DOI: 10.1042/BSR20210148
PMCID: PMC8350431

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Membrane interaction and disulphide-bridge formation in the unconventional secretion of Tau.PMID 34308969Read ↗

Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau proteinSemantic proximity Read ↗

Membranes as targets and modifiers of mutant huntingtin aggregation.Semantic proximity Read ↗

Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesSemantic proximity Read ↗

An interdisciplinary approach to studying mechanistic, structural and toxic features of protein aggregates associated with neurodegenerative disordersSemantic proximity Read ↗

FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregationSemantic proximity Read ↗

Protein transmission in neurodegenerative disease.Semantic proximity Read ↗

ALS mutations in the TIA-1 prion-like domain trigger highly condensed pathogenic structures.Semantic proximity Read ↗

Conformational dynamics of Tau in the cell quantified by an intramolecular FRET biosensor in physiological and pathological contextSemantic proximity Read ↗

FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregationSemantic proximity Read ↗

Tau P301L mutation promotes core 4R tauopathy fibril fold through near-surface water structuring and conformational rearrangementSemantic proximity Read ↗

Liquid-liquid phase separation induces pathogenic tau conformations in vitro.Semantic proximity Read ↗

Revealing the conformational landscape of tau P → L mutants in R23 tau macromolecule: A pathway to targeted therapeutic design.Semantic proximity Read ↗

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