ReviewCold Spring Harbor perspectives in biology2017
The Amyloid Phenomenon and Its Links with Human Disease.
Review in Cold Spring Harbor perspectives in biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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
55 citing papers in PubMed, 150 citations in OpenAlex.
- Biomolecular coacervation-mediated materials: Phase states, phase transitions, and biomedical applications.Bioactive materials · 2027Review
- Chaperone proteins protect against desmin fragment amyloid aggregation.Biophysical journal · 2026Article
- Protein codes and mobility together shape cellular function and disease.Trends in biochemical sciences · 2026Review
- Synthetic chaperone based on Hsp90-Tau interaction inhibits Tau aggregation and rescues physiological Tau-Microtubule interaction.Nature communications · 2025Article
- Identification of an on-pathway intermediate illuminates the kinetic competition between protein folding and misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Physics of Protein Aggregation in Normal and Accelerated Brain Aging.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Harnessing deep learning for proteome-scale detection of amyloid signaling motifs.Bioinformatics (Oxford, England) · 2025Article
- Massively parallel genetic perturbation suggests the energetic structure of an amyloid-β transition state.Science advances · 2025Article
- Raman spectroscopy and imaging of protein droplet formation and aggregation.Current opinion in structural biology · 2025Review
- The Promising Role of Selenium and Yeast in the Fight Against Protein Amyloidosis.Biological trace element research · 2025Review
- The mechanism of amyloid fibril growth from Φ-value analysis.Nature chemistry · 2025Article
- Amyloids in bladder cancer hijack cancer-related proteins and are positive correlated to tumor stage.Scientific reports · 2025Article
- Discovery of an on-pathway protein folding intermediate illuminates the kinetic competition between folding and misfolding.bioRxiv : the preprint server for biology · 2024Article
- Advanced glycation end-products accelerate amyloid deposits in adipocyte's lipid droplets.Cell death & disease · 2024Article
- The role of biomolecular condensates in protein aggregation.Nature reviews. Chemistry · 2024Review
- Recent Advancements in Biosensors for the Detection and Characterization of Amyloids: A Review.The protein journal · 2024Review
- Liquid-liquid phase separation of α-synuclein is highly sensitive to sequence complexity.Protein science : a publication of the Protein Society · 2024Article
- Deciphering amyloid fibril molecular maturation through FLIM-phasor analysis of thioflavin T.Biophysical reports · 2024Article
- Mushroom-derived bioactive components with definite structures in alleviating the pathogenesis of Alzheimer's disease.Frontiers in pharmacology · 2024Review
- Disruption of the nascent polypeptide-associated complex leads to reduced polyglutamine aggregation and toxicity.PloS one · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ability of normally soluble proteins to convert into amyloid fibrils is now recognized to be a generic phenomenon. The overall cross-β architecture of the core elements of such structures is closely similar for different amino acid sequences, as this architecture is dominated by interactions associated with the common polypeptide main chain. In contrast, the multiplicity of complex and intricate structures of the functional states of proteins is dictated by specific interactions involving the variable side chains, the sequence of which is unique to a given protein. Nevertheless, the side chains dictate important aspects of the amyloid structure, including the regions of the sequence that form the core elements of the fibrils and the kinetics and mechanism of the conversion process. The formation of the amyloid state of proteins is of particular importance in the context of a range of medical disorders that include Alzheimer's and Parkinson's diseases and type 2 diabetes. These disorders are becoming increasingly common in the modern world, primarily as a consequence of increasing life spans and changing lifestyles, and now affect some 500 million people worldwide. This review describes recent progress in our understanding of the molecular origins of these conditions and discusses emerging ideas for new and rational therapeutic strategies by which to combat their onset and progression.
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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.