Evidence map›Paper›PMID 22824345›Full record

ArticleMolecular neurodegeneration2012

Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level.

Georg Nübling, Benedikt Bader, Johannes Levin, Jenna Hildebrandt, Hans Kretzschmar, Armin Giese

Open access · goldAbstract read
In one paragraph

Article in Molecular neurodegeneration, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.1field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 66 citations in OpenAlex.

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  5. Iron and Targeted Iron Therapy in Alzheimer's Disease.International journal of molecular sciences · 2023
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  13. Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021
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  15. Immunotherapies for Aging-Related Neurodegenerative Diseases-Emerging Perspectives and New Targets.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Georg NüblingCenter for Neuropathology and Prion Research, Ludwig-Maximilians-Universität, Feodor-Lynen-Str, 23, 81377, Munich, Germany.
Benedikt Bader
Johannes Levin
Jenna Hildebrandt
Hans Kretzschmar
Armin Giese
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundFibrillar amyloid-like deposits and co-deposits of tau and α-synuclein are found in several common neurodegenerative diseases. Recent evidence indicates that small oligomers are the most relevant toxic aggregate species. While tau fibril formation is well-characterized, factors influencing tau oligomerization and molecular interactions of tau and α-synuclein are not well understood.

resultsWe used a novel approach applying confocal single-particle fluorescence to investigate the influence of tau phosphorylation and metal ions on tau oligomer formation and its coaggregation with α-synuclein at the level of individual oligomers. We show that Al3+ at physiologically relevant concentrations and tau phosphorylation by GSK-3β exert synergistic effects on the formation of a distinct SDS-resistant tau oligomer species even at nanomolar protein concentration. Moreover, tau phosphorylation and Al3+ as well as Fe3+ enhanced both formation of mixed oligomers and recruitment of α-synuclein in pre-formed tau oligomers.

conclusionsOur findings provide a new perspective on interactions of tau phosphorylation, metal ions, and the formation of potentially toxic oligomer species, and elucidate molecular crosstalks between different aggregation pathways involved in neurodegeneration.

Indexed as

alpha-SynucleinCell Line, TumorEscherichia coliGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHumansIronMetalsNeurodegenerative DiseasesPhosphorylationProtein MultimerizationSolventstau Proteinsalpha-SynucleinGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGSK3B protein, humanIronMetalsSolventstau Proteins

Identifiers

PMID22824345
PMCPMC3472288
OpenAlexW2114346543

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.