Results 71 to 80 of about 187,834 (297)

Localized Amyloidosis of the Oral Cavity: A Rare Clinical Entity

open access: yesClinical Case Reports
Amyloidosis is a complex disease which rarely affects the oral cavity. While localized and systemic variants have a similar clinical presentation, these entities differ vastly in their natural history and prognosis.
Brian Maloney   +2 more
doaj   +1 more source

Different Amyloid-β Self-Assemblies Have Distinct Effects on Intracellular Tau Aggregation. [PDF]

open access: yes, 2019
Alzheimer's disease (AD) pathology is characterized by the aggregation of beta-amyloid (Aβ) and tau in the form of amyloid plaques and neurofibrillary tangles in the brain.
Bitan, Gal   +6 more
core  

The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy [PDF]

open access: yes, 2015
Structural analysis of protein fibrillation is inherently challenging. Given the crucial role of fibrils in amyloid diseases, method advancement is urgently needed.
Annette E. Langkilde   +50 more
core   +1 more source

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

open access: yesFEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane   +11 more
wiley   +1 more source

AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils

open access: yesNature Communications, 2021
Systemic AA amyloidosis is a protein misfolding disease caused by the formation of amyloid fibrils from serum amyloid A (SAA) protein. Here, the authors present the cryo-EM structures of AA amyloid fibrils isolated from mouse tissue and in vitro formed ...
Akanksha Bansal   +8 more
doaj   +1 more source

The effects of cross linking on collagen type 1 nanostructure and nanostructural response to uniaxial tension : a thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Engineering at Massey University, Manawatu, New Zealand [PDF]

open access: yes, 2016
Reproduced by permission of The Royal Society of Chemistry: Kayed, H. R., Sizeland, K. H., Kirby, N., Hawley, A., Mudie, S. T., & Haverkamp, R. G. (2015). Collagen cross linking and fibril alignment in pericardium. RSC Advances, 5, 3611-3618.
Kayed, Hanan
core  

A Hot Downflowing Model Atmosphere For Umbral Flashes And The Physical Properties Of Their Dark Fibrils [PDF]

open access: yes, 2017
We perform NLTE inversions in a large set of umbral flashes, including the dark fibrils visible within them, and in the quiescent umbra by using the inversion code NICOLE on a set of full Stokes high-resolution Ca II 8542 A observations of a sunspot at ...
Henriques, Vasco M. J.   +3 more
core   +2 more sources

Early‐life high‐fat diet exposure increases Achilles tendon stiffness and induces transcriptomic alterations

open access: yesFEBS Open Bio, EarlyView.
Early‐life exposure to a high‐fat diet altered intact Achilles tendons in rat offspring, making them thinner, stiffer, and molecularly distinct even without injury. These findings suggest that developmental high‐fat diet exposure may impair tendon quality and increase susceptibility to mechanical overload or tendon injury later in life.
Heyong Yin   +3 more
wiley   +1 more source

Formation of amyloid fibrils by the regulatory 14-3-3ζ protein

open access: yesOpen Biology
The 14-3-3 proteins are a highly conserved adaptor protein family with multi-layer functions, abundantly expressed in the brain. The 14-3-3 proteins modulate phosphorylation, regulate enzymatic activity and can act as chaperones.
Darius Šulskis   +4 more
doaj   +1 more source

Structure-based inhibitors of amyloid beta core suggest a common interface with tau. [PDF]

open access: yes, 2019
Alzheimer's disease (AD) pathology is characterized by plaques of amyloid beta (Aβ) and neurofibrillary tangles of tau. Aβ aggregation is thought to occur at early stages of the disease, and ultimately gives way to the formation of tau tangles which ...
Bowler, Jeannette   +13 more
core   +1 more source

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