ArticleBiochemistry2011
Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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.
Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- The role of shear rates on amyloid formation from biofilm peptide phenol-soluble modulins.Biophysical journal · 2024Article
- Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation.ACS chemical neuroscience · 2023Article
- Blocking tau transmission by biomimetic graphene nanoparticles.Journal of materials chemistry. B · 2023Article
- The Role of Copper in Tau-Related Pathology in Alzheimer's Disease.Frontiers in molecular neuroscience · 2020Review
- Mapping interactions with the chaperone network reveals factors that protect against tau aggregation.Nature structural & molecular biology · 2018Article
- Structure-based inhibitors of tau aggregation.Nature chemistry · 2018Article
- Novel cell-penetrating-amyloid peptide conjugates preferentially kill cancer cells.MedChemComm · 2018Article
- Structural evaluations of tau protein conformation: methodologies and approaches.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2017Review
- How Does Hyperphopsphorylation Promote Tau Aggregation and Modulate Filament Structure and Stability?ACS chemical neuroscience · 2016Article
- Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits.Nature medicine · 2015Article
- Tau assembly: the dominant role of PHF6 (VQIVYK) in microtubule binding region repeat R3.The journal of physical chemistry. B · 2015Article
- Interactions between amyloid-β and Tau fragments promote aberrant aggregates: implications for amyloid toxicity.The journal of physical chemistry. B · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Tau protein was scanned for highly amyloidogenic sequences in amphiphilic motifs (X)(n)Z, Z(X)(n)Z (n ≥ 2), or (XZ)(n) (n ≥ 2), where X is a hydrophobic residue and Z is a charged or polar residue. N-Acetyl peptides homologous to these sequences were used to study aggregation. Transmission electron microscopy (TEM) showed seven peptides, in addition to well-known primary nucleating sequences Ac(275)VQIINK (AcPHF6*) and Ac(306)VQIVYK (AcPHF6), formed fibers, tubes, ribbons, or rolled sheets. Of the peptides shown by TEM to form amyloid, Ac(10)VME, AcPHF6*, Ac(375)KLTFR, and Ac(393)VYK were found to enhance the fraction of β-structure of AcPHF6 formed at equilibrium, and Ac(375)KLTFR was found to inhibit AcPHF6 and AcPHF6* aggregation kinetics in a dose-dependent manner, consistent with its participation in a hybrid steric zipper model. Single site mutants were generated which transformed predicted amyloidogenic sequences in tau into non-amyloidogenic ones. A M11K mutant had fewer filaments and showed a decrease in aggregation kinetics and an increased lag time compared to wild-type tau, while a F378K mutant showed significantly more filaments. Our results infer that sequences throughout tau, in addition to PHF6 and PHF6*, can seed amyloid formation or affect aggregation kinetics or thermodynamics.
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Registered trials
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.