Results 71 to 80 of about 18,947 (293)

Intercompartmental communication in senescence

open access: yesFEBS Open Bio, EarlyView.
Senescent cells experience structural changes in the plasma membrane, endoplasmic reticulum, mitochondria, lysosomes, nucleus, and cytoskeleton. These alterations disrupt crosstalk among cellular compartments, impairing vesicular trafficking, contact sites, and molecular flow.
Krystyna Mazan‐Mamczarz   +3 more
wiley   +1 more source

NACore Amyloid Formation in the Presence of Phospholipids

open access: yesFrontiers in Physiology, 2020
Amyloids are implicated in many diseases, and disruption of lipid membrane structures is considered as one possible mechanism of pathology. In this paper we investigate interactions between an aggregating peptide and phospholipid membranes, focusing on ...
Jon Pallbo   +5 more
doaj   +1 more source

Long‐term hippocampal alterations and cognitive impairment in a murine model of surgical sepsis

open access: yesFEBS Open Bio, EarlyView.
Using a mouse model of surgical sepsis, we tested long‐term memory and analyzed the transcriptome of single cells isolated from the hippocampus. Survivor mice showed worse memory, loss of certain brain cell subpopulations, and abnormal immune cell activity—suggesting that post‐sepsis brain alterations may be linked to cognitive deficits.
Dong Seong Cho   +4 more
wiley   +1 more source

Amyloidosis-history and development, emphasis on insulin and prion amyloids

open access: yesBrain Disorders
Amyloidosis is associated with misfolding of protein (normal functional and cellular) into intractable aggregates, commonly known as amyloid fibrils.
Sanjay Kisan Metkar   +3 more
doaj   +1 more source

Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery

open access: yesMolecules, 2019
Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid nature).
Tatiana A. Chernova   +2 more
doaj   +1 more source

Hsp40s play complementary roles in the prevention of tau amyloid formation

open access: yeseLife, 2021
The microtubule-associated protein, tau, is the major subunit of neurofibrillary tangles associated with neurodegenerative conditions, such as Alzheimer's disease.
Rose Irwin   +5 more
doaj   +1 more source

\u3cem\u3eDe Novo\u3c/em\u3e [PSI\u3csup\u3e+\u3c/sup\u3e] Prion Formation Involves Multiple Pathways to Form Infectious Oligomers [PDF]

open access: yes, 2017
Prion and other neurodegenerative diseases are associated with misfolded protein assemblies called amyloid. Research has begun to uncover common mechanisms underlying transmission of amyloids, yet how amyloids form in vivo is still unclear. Here, we take
Manogaran, Anita L.   +5 more
core   +1 more source

Dynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide [PDF]

open access: yes, 2016
Many chronic degenerative diseases result from aggregation of misfolded polypeptides to form amyloids. Many amyloidogenic polypeptides are surfactants and their assembly can be catalysed by hydrophobic-hydrophilic interfaces (an air-water interface in ...
Hawkins, N   +4 more
core   +1 more source

Cutaneous Phosphorylated Alpha‐Synuclein in Lewy Body Dementia

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective To determine the test performance of cutaneous phosphorylated alpha‐synuclein (P‐SYN) in dementia with Lewy bodies (DLB), individuals with reduced Montreal Cognitive Assessment (MoCA) and healthy controls. Methods This is the first subgroup analysis of the Synuclein‐One study, a prospective, blinded study evaluating P‐SYN detection ...
Christopher H. Gibbons   +31 more
wiley   +1 more source

The dual role of amyloid-β-sheet sequences in the cell surface properties of FLO11-encoded flocculins in Saccharomyces cerevisiae

open access: yeseLife, 2021
Fungal adhesins (Als) or flocculins are family of cell surface proteins that mediate adhesion to diverse biotic and abiotic surfaces. A striking characteristic of Als proteins originally identified in the pathogenic Candida albicans is to form functional
Clara Bouyx   +6 more
doaj   +1 more source

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