Results 51 to 60 of about 3,632,451 (277)
Force Sensitivity in
mSphere, 2016 Many fungal adhesins have short, β-aggregation-prone sequences that play important functional roles, and in the Candida albicans adhesin Als5p, these sequences cluster the adhesins after exposure to shear force.
Cho X. J. Chan +6 more
doaj +1 more source
Nonpathological extracellular amyloid is present during normal epididymal sperm maturation. [PDF]
PLoS ONE, 2012 Amyloids are aggregated proteins characterized by a specific cross-β-sheet structure and are typically associated with neurodegenerative diseases including Alzheimer's disease.
Sandra Whelly +5 more
doaj +1 more source
The emerging concept of functional amyloid [PDF]
Journal of Internal Medicine, 2009 Abstract.Although amyloid has usually been considered a pathological structure, growing evidence indicates that amyloid may also be a productive part of cell biology contributing to normal physiology. In fact, amyloid formation seems to be an intrinsic propensity of polypeptides in general and the amyloid β‐fold an evolutionary highly conserved ...
openaire +2 more sources
NeuroImage: Clinical, 2018 Changes in functional connectivity of cortical networks have been observed in resting-state EEG studies in healthy aging as well as preclinical and clinical stages of AD.
Stefan Teipel +10 more
doaj +1 more source
FEBS Letters, EarlyView.Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley +1 more source
Fold modulating function: bacterial toxins to functional amyloids [PDF]
Frontiers in Microbiology, 2014 Many bacteria produce cytolytic toxins that target host cells or other competing microbes. It is well known that environmental factors control toxin expression, however, recent work suggests that some bacteria manipulate the fold of these protein toxins to control their function.
Syed, Adnan K., Boles, Blaise R.
openaire +3 more sources
Targeting Bacterial Biofilms by the Green Tea Polyphenol EGCG
Molecules, 2019 Bacterial biofilms are multicellular aggregates in which cells are embedded in an extracellular matrix of self-produced biopolymers. Being refractory to antibiotic treatment and host immune systems, biofilms are involved in most chronic infections, and ...
Regine Hengge
doaj +1 more source
Amyloid-β inhibits No-cGMP signaling in a CD36- and CD47-dependent manner. [PDF]
PLoS ONE, 2010 Amyloid-β interacts with two cell surface receptors, CD36 and CD47, through which the matricellular protein thrombospondin-1 inhibits soluble guanylate cyclase activation. Here we examine whether amyloid-β shares this inhibitory activity.
Thomas W Miller +4 more
doaj +1 more source
Microbiome‐blood–brain barrier interactions in aging — mechanisms and therapeutic potential
FEBS Letters, EarlyView.Aging reshapes the gut microbiome (↓SCFA‐producing commensals; ↑pro‐inflammatory outputs), shifting circulating metabolites (↓SCFAs; ↑LPS, ↑TMAO, ↑PAA) that act at the BBB to increase nonspecific transcytosis, alter transport, and promote astrocyte reactivity, heightening brain vulnerability.
Daniel Cuervo‐Zanatta +3 more
wiley +1 more source
Diversity, biogenesis and function of microbial amyloids [PDF]
Trends in Microbiology, 2012 Amyloid is a distinct β-sheet-rich fold that many proteins can acquire. Frequently associated with neurodegenerative diseases in humans, including Alzheimer's, Parkinson's and Huntington's diseases, amyloids are traditionally considered the product of protein misfolding.
Luz P, Blanco +4 more
openaire +2 more sources