ReviewCold Spring Harbor perspectives in medicine2017
Prion-Like Protein Aggregates and Type 2 Diabetes.
Review in Cold Spring Harbor perspectives in medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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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.
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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.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- Integrated analysis of methylome and transcriptome responses to exercise training in children with overweight/obesity.Physiological genomics · 2025Trial
- Mechanisms of IGF1R signaling in type 2 diabetes-related neurodegeneration and therapeutic implications of exercise.European journal of medical research · 2025Article
- Proteostasis and Its Role in Disease Development.Cell biochemistry and biophysics · 2025Review
- Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response.Diseases (Basel, Switzerland) · 2023Review
- Multi-Tiered Assessment of Gene Expression Provides Evidence for Mechanisms That Underlie Risk for Type 2 Diabetes.Diabetes, metabolic syndrome and obesity : targets and therapy · 2023Article
- Polyphenols from Conyza dioscoridis (L.) ameliorate Alzheimer's disease- like alterations through multi-targeting activities in two animal models.BMC complementary medicine and therapies · 2022Article
- Cellular Prion Protein Is Closely Associated with Early Recurrence and Poor Survival in Patients with Hepatocellular Carcinoma.Diagnostics (Basel, Switzerland) · 2022Article
- Linking hIAPP misfolding and aggregation with type 2 diabetes mellitus: a structural perspective.Bioscience reports · 2022Review
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- Altered cellular localisation and expression, together with unconventional protein trafficking, of prion protein, PrPDiabetologia · 2021Article
- Characterization of the structural forces governing the reversibility of the thermal unfolding of the human acidic fibroblast growth factor.Scientific reports · 2021Article
- Bacterial Extracellular DNA Promotes β-Amyloid Aggregation.Microorganisms · 2021Article
- Mixed pathologies in pancreatic β cells from subjects with neurodegenerative diseases and their interaction with prion protein.Acta neuropathologica communications · 2021Article
- Peripherally misfolded proteins exacerbate ischemic stroke-induced neuroinflammation and brain injury.Journal of neuroinflammation · 2021Article
- p53, A Victim of the Prion Fashion.Cancers · 2021Review
- Review
- The COVID-19 Pandemic during the Time of the Diabetes Pandemic: Likely Fraternal Twins?Pathogens (Basel, Switzerland) · 2020Review
- Secretory Autophagy and Its Relevance in Metabolic and Degenerative Disease.Frontiers in endocrinology · 2020Review
- The diabetes pandemic and associated infections: suggestions for clinical microbiology.Reviews in medical microbiology : a journal of the Pathological Society of Great Britain and Ireland · 2019Article
- Recent Insights on Alzheimer's Disease Originating from Yeast Models.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Type 2 diabetes (T2D) is a highly prevalent metabolic disease characterized by chronic insulin resistance and β-cell dysfunction and loss, leading to impaired insulin release and hyperglycemia. Although the mechanism responsible for β-cell dysfunction and death is not completely understood, recent findings suggest that the accumulation of misfolded aggregates of the islet amyloid polypeptide (IAPP) in the islets of Langerhans may play an important role in pancreatic damage. Misfolding and aggregation of diverse proteins and their accumulation as amyloid in different organs is the hallmark feature in a group of chronic, degenerative diseases termed protein misfolding disorders (PMDs). PMDs include highly prevalent human illnesses such as Alzheimer's and Parkinson's disease, as well as more than 25 rarer disorders. Among them, prion diseases are unique because the pathology can be transmitted by a proteinaceous infectious agent, termed a prion, which induces disease by propagating protein misfolding and aggregation. This phenomenon has a striking resemblance to the process of protein misfolding and aggregation in all of the PMDs, suggesting that misfolded aggregates have an intrinsic potential to be transmissible. Indeed, recent studies have shown that the pathological hallmarks of various PMDs can be induced in vivo under experimental conditions by inoculating tissue extracts containing protein aggregates into animal models. In this review, we describe our current understanding of the molecular mechanism underlying the prion-like transmission of protein aggregates and its possible role in T2D.
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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.