ArticleMolecular neurodegeneration2011
A glycine zipper motif mediates the formation of toxic β-amyloid oligomers in vitro and in vivo.
Article in Molecular neurodegeneration, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 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
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- A toxic effector of T7SS facilitates bacterial competition and virulence through membrane damage in Streptococcus suis.Veterinary research · 2026Article
- Modulating Amyloid-β Toxicity: In Vitro Analysis of Aβ42(G37V) Variant Impact on Aβ42 Aggregation and Cytotoxicity.International journal of molecular sciences · 2024Article
- Delineating the Role of GxxxG Motif in Amyloidogenesis: A New Perspective in Targeting Amyloid-Beta Mediated AD Pathogenesis.ACS bio & med chem Au · 2024Review
- A glycine zipper motif is required for the translocation of a T6SS toxic effector into target cells.EMBO reports · 2023Article
- Oxidation and Antioxidation of Natural Products in the Model OrganismAntioxidants (Basel, Switzerland) · 2022Review
- Azepine-Indole Alkaloids FromFrontiers in neuroscience · 2022Article
- Amyloid beta acts synergistically as a pro-inflammatory cytokine.Neurobiology of disease · 2021Article
- Vitamin BCell reports · 2021Article
- Physicochemical Features and Peculiarities of Interaction of AMP with the Membrane.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Mechanisms of Resistance to the Contact-Dependent Bacteriocin CdzC/D inJournal of bacteriology · 2019Article
- Cross species application of quantitative neuropathology assays developed for clinical Alzheimer's disease samples.Pathobiology of aging & age related diseases · 2019Article
- In vivo induction of membrane damage by β-amyloid peptide oligomers.Acta neuropathologica communications · 2018Article
- Key Residues for the Formation of Aβ42 Amyloid Fibrils.ACS omega · 2018Article
- Common fibrillar spines of amyloid-β and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors.The Journal of biological chemistry · 2018Article
- Contact-dependent killing byeLife · 2017Article
- Identification of the primary peptide contaminant that inhibits fibrillation and toxicity in synthetic amyloid-β42.PloS one · 2017Article
- A critical role for the self-assembly of Amyloid-β1-42 in neurodegeneration.Scientific reports · 2016Article
- Glycines from the APP GXXXG/GXXXA Transmembrane Motifs Promote Formation of Pathogenic Aβ Oligomers in Cells.Frontiers in aging neuroscience · 2016Article
- Identifying Aβ-specific pathogenic mechanisms using a nematode model of Alzheimer's disease.Neurobiology of aging · 2015Article
- Protective role of DNJ-27/ERdj5 in Caenorhabditis elegans models of human neurodegenerative diseases.Antioxidants & redox signaling · 2014Article
Corrections and comments
- Erratum issuedLacor, Pascale [corrected to Lacor, Pascale N]; Velasco, Pauline T [added]
Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe β-amyloid peptide (Aβ) contains a Gly-XXX-Gly-XXX-Gly motif in its C-terminal region that has been proposed to form a "glycine zipper" that drives the formation of toxic Aβ oligomers. We have tested this hypothesis by examining the toxicity of Aβ variants containing substitutions in this motif using a neuronal cell line, primary neurons, and a transgenic C. elegans model.
resultsWe found that a Gly37Leu substitution dramatically reduced Aβ toxicity in all models tested, as measured by cell dysfunction, cell death, synaptic alteration, or tau phosphorylation. We also demonstrated in multiple models that Aβ Gly37Leu is actually anti-toxic, thereby supporting the hypothesis that interference with glycine zipper formation blocks assembly of toxic Aβ oligomers. To test this model rigorously, we engineered second site substitutions in Aβ predicted by the glycine zipper model to compensate for the Gly37Leu substitution and expressed these in C. elegans. We show that these second site substitutions restore in vivo Aβtoxicity, further supporting the glycine zipper model.
conclusionsOur structure/function studies support the view that the glycine zipper motif present in the C-terminal portion of Aβ plays an important role in the formation of toxic Aβ oligomers. Compounds designed to interfere specifically with formation of the glycine zipper could have therapeutic potential.
Identifiers
What OpenQuestion holds
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.