Results 171 to 180 of about 160,241 (252)
Internal Medicine Journal, EarlyView.Abstract Background Amyloidosis encompasses a group of diseases characterised by extracellular deposition of misfolded protein fibrils, potentially leading to organ dysfunction. Liver involvement occurs via direct amyloid infiltration, common in immunoglobulin light chain (AL) amyloidosis, or congestive hepatopathy, more typical in transthyretin (ATTR)
M Tang +9 more
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Architecture and Evolution of Prokaryotic Multicellularity: Common Patterns and Diversity
Molecular Microbiology, EarlyView.Prokaryotes form diverse multicellular structures, like biofilms, filaments, and aggregates, comprising hallmark traits such as adhesion, communication, differentiation, and programmed cell death. This review explores how these forms develop, function, and evolve in response to environmental cues.
Genevieve Sohl +3 more
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Of mice and men—The emerging oral–gut–brain axis of health and disease
Periodontology 2000, EarlyView.Abstract Objectives Oral health's inextricable links to systemic health are highlighted by the emerging oral–gut–brain axis and other well‐known axes. There is growing evidence of a complex oral–gut–brain axis linking mouth and gut microbiomes with the central nervous system.
Yvonne L. Hernandez‐Kapila +1 more
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Contributions of vascular ageing to late‐onset Alzheimer's disease
Experimental Physiology, EarlyView.Abstract Late‐onset Alzheimer's disease (LOAD) is an age‐related disease that is strongly associated with vascular risk factors and cerebrovascular impairments. As such, changes in the vasculature with advancing age likely contribute to LOAD, but the mechanisms underlying these contributions remain incompletely understood.
Skylyn J. Ferguson +2 more
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The Journal of Physiology, EarlyView.Abstract figure legend Downregulation of mitotically associated long non‐coding RNA (MANCR) disturbs transcriptome and proteome in endothelial cells, possibly leading to endothelial and vascular dysfunction in preeclampsia. Abstract Preeclampsia (PE) is a hypertensive disorder during pregnancy, which is characterized by a wide spectrum of endothelial ...
Si‐Yan Zhang, Chi Zhou, Jing Zheng
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DEN Open, Volume 7, Issue 1, April 2027.ABSTRACT Amyloidosis, characterized by the deposition of abnormal protein fibrils in organs, is classified as systemic or localized. Amyloid light chain (AL)‐type localized amyloidosis is uncommon, particularly when confined to the gastrointestinal tract.
Shunsuke Kojimahara +7 more
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Journal of the Science of Food and Agriculture, Volume 106, Issue 15, Page 9713-9727, December 2026.Abstract BACKGROUND Anthocyanins are attractive natural colorants for clean‐label food applications; however, their widespread use is limited by poor thermal stability. Protein nanofibrils have recently emerged as promising natural stabilizers because of their high surface area and ability to interact with anthocyanins through non‐covalent interactions.
Vildan Eyiz +2 more
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MedComm – Biomaterials and Applications, Volume 5, Issue 4, December 2026.Therapeutic peptide self‐assembly is governed by multiple non‐covalent interactions, enabling the construction of diverse supramolecular structures. These self‐assembled systems can be engineered through spontaneous self‐assembly of monomers, co‐assembly, or stimulus‐responsive strategies to improve tumor delivery efficiency.
Yuelin Fang +6 more
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Surface proteins modulate extracellular vesicle mediated inhibition of Aβ(1‐42) aggregation
Protein Science, Volume 35, Issue 12, December 2026.Abstract Aggregation of the amyloid‐β (Aβ) peptide into amyloid oligomers and fibrils is a central pathogenic feature and therapeutic target in Alzheimer's disease (AD). Understanding the aggregation reaction and how it is modulated by the biological environment is therefore important.
Vesa Halipi +6 more
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Protein Science, Volume 35, Issue 12, December 2026.Abstract Progressive β cell death resulting from the aggregation of human islet amyloid polypeptide (hIAPP) in the pancreas is a molecular driver of type 2 diabetes (T2D). Recent studies from our group have shown that hIAPP forms two distinct amyloid oligomers: on‐path donut oligomers (DOs) and off‐path round oligomers (ROs). Previous studies have also
Daniel Warren +3 more
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