ReviewApplied biochemistry and biotechnology2012
Ubiquitous amyloids.
Review in Applied biochemistry and biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 59 citations in OpenAlex.
- Surface properties of lysozyme aqueous solutions in the presence of reducing agents: The effect of disulfide bonds reshuffling.Biophysical journal · 2025Article
- Extracellular matrix dysregulation in aging, calcification, and cancer diseases: insights into cellular senescence, inflammation, and novel therapeutic strategies.International journal of biological sciences · 2025Review
- Genetic Algorithm for Automated Parameterization of Network Hamiltonian Models of Amyloid Fibril Formation.The journal of physical chemistry. B · 2024Article
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor.Sensors (Basel, Switzerland) · 2023Article
- Network Hamiltonian models reveal pathways to amyloid fibril formation.Scientific reports · 2020Article
- Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAPBiophysical journal · 2020Article
- Unraveling VEALYL Amyloid Formation Using Advanced Vibrational Spectroscopy and Microscopy.Biophysical journal · 2020Article
- Bridging the Gap Between Fluid Biomarkers for Alzheimer's Disease, Model Systems, and Patients.Frontiers in aging neuroscience · 2020Review
- From EST to structure models for functional inference of APP, BACE1, PSEN1, PSEN2 genes.Bioinformation · 2019Article
- Setting the stage for the next step in cardiac amyloidosis imaging: Serial quantitative studies to assess disease activity.Journal of nuclear cardiology : official publication of the American Society of Nuclear Cardiology · 2018Article
- Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces.Langmuir : the ACS journal of surfaces and colloids · 2018Article
- Targeting Beta-Amyloid at the CSF: A New Therapeutic Strategy in Alzheimer's Disease.Frontiers in aging neuroscience · 2018Article
- (E)-2-Methoxy-4-(3-(4-methoxyphenyl) prop-1-en-1-yl) Phenol Ameliorates LPS-Mediated Memory Impairment by Inhibition of STAT3 Pathway.Neuromolecular medicine · 2017Article
- Propagation of Fibrillar Structural Forms in Proteins Stopped by Naturally Occurring Short Polypeptide Chain Fragments.Pharmaceuticals (Basel, Switzerland) · 2017Article
- Small-molecule PET Tracers for Imaging Proteinopathies.Seminars in nuclear medicine · 2017Review
- Design of multi-phase dynamic chemical networks.Nature chemistry · 2017Article
- CSGene: a literature-based database for cell senescence genes and its application to identify critical cell aging pathways and associated diseases.Cell death & disease · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The common view of amyloids and prion proteins is that they are associated with many currently incurable diseases and present a great danger to an organism. This danger comes from the fact that not only prion proteins, but also the infectious form(s) of amyloids, as it has been shown recently, are able to transmit the disease. On the other hand, organisms take advantage of the strength and durability of specific forms of amyloids. Such forms do not spread any disease. Also, in nanotechnology there is a constantly growing need to employ amyloid fibrils in many industrial applications. With increasing knowledge about amyloids and prion proteins we are aware that the amyloidal state is inherent to any protein, making the problem of amyloid formation a central one in aging-related diseases. However, the "good" amyloids can be beneficial and even necessary for our health. Furthermore, because of their mechanical properties, the amyloids are of great interest to engineers.
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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.