ReviewThe Journal of membrane biology2004
Amyloid peptide channels.
Review in The Journal of membrane biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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.
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
57 citing papers in PubMed, 175 citations in OpenAlex.
- Amyloid Prefibrillar Oligomers: The Surprising Commonalities in Their Structure and Activity.International journal of molecular sciences · 2021Review
- An Unbalanced Synaptic Transmission: Cause or Consequence of the Amyloid Oligomers Neurotoxicity?International journal of molecular sciences · 2021Review
- Ion channel formation by N-terminally truncated Aβ (4-42): relevance for the pathogenesis of Alzheimer's disease.Nanomedicine : nanotechnology, biology, and medicine · 2020Article
- Medin Oligomer Membrane Pore Formation: A Potential Mechanism of Vascular Dysfunction.Biophysical journal · 2020Article
- Modelling mitochondrial dysfunction in Alzheimer's disease using human induced pluripotent stem cells.World journal of stem cells · 2019Review
- Cause and consequence of Aβ - Lipid interactions in Alzheimer disease pathogenesis.Biochimica et biophysica acta. Biomembranes · 2018Review
- Endogenously generated amyloid-β increases stiffness in human neuroblastoma cells.European biophysics journal : EBJ · 2017Article
- Monosialoganglioside-GM1 triggers binding of the amyloid-protein salmon calcitonin to a Langmuir membrane model mimicking the occurrence of lipid-rafts.Biochemistry and biophysics reports · 2016Article
- Small molecule NPT-440-1 inhibits ionic flux through AβNanomedicine : nanotechnology, biology, and medicine · 2016Article
- The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes.Biophysical journal · 2016Article
- Ion Channel Formation by Tau Protein: Implications for Alzheimer's Disease and Tauopathies.Biochemistry · 2015Article
- Congo red modulates ACh-induced Ca(2+) oscillations in single pancreatic acinar cells of mice.Acta pharmacologica Sinica · 2014Article
- Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Chemical Society reviews · 2014Review
- Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) pores.The journal of physical chemistry. B · 2014Article
- Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansion.Brain sciences · 2014Article
- Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models.Current pharmaceutical design · 2014Review
- The role of amyloidogenic protein oligomerization in neurodegenerative disease.Journal of molecular medicine (Berlin, Germany) · 2013Review
- Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.Journal of chemical theory and computation · 2013Article
- Amyloid β-protein oligomers and Alzheimer's disease.Alzheimer's research & therapy · 2013Review
- Activation of PARP by oxidative stress induced by β-amyloid: implications for Alzheimer's disease.Neurochemical research · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
At least 16 distinct clinical syndromes including Alzheimer's disease (AD), Parkinson's disease (PD), rheumatoid arthritis, type II diabetes mellitus (DM), and spongiform encephelopathies (prion diseases), are characterized by the deposition of amorphous, Congo red-staining deposits known as amyloid. These "misfolded" proteins adopt beta-sheet structures and aggregate spontaneously into similar extended fibrils despite their widely divergent primary sequences. Many, if not all, of these peptides are capable of forming ion-permeable channels in vitro and possibly in vivo. Common channel properties include irreversible, spontaneous insertion into membranes, relatively large, heterogeneous single-channel conductances, inhibition of channel formation by Congo red, and blockade of inserted channels by Zn2+. Physiologic effects of amyloid, including Ca2+ dysregulation, membrane depolarization, mitochondrial dysfunction, inhibition of long-term potentiation (LTP), and cytotoxicity, suggest that channel formation in plasma and intracellular membranes may play a key role in the pathophysiology of the amyloidoses.
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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.