Amy Loli

Amy Loli, Carlisle, PA View Details

Cities: Catasauqua PA, Allentown PA, Saint Louis MO

Amy Loli, Carlisle, PA View Details

Locations: Catasauqua PA, Allentown PA, Saint Louis MO

Amy Shark

Amy Louise Billings, known professionally as Amy Shark, is an Australian indie pop singer-songwriter-guitarist and producer from the Gold Coast, Queensland. During 2008 to 2012, her early solo materiaread more...l was released and performed under the name Amy Cushway. Her 2016 single "Adore" peaked at number 3 on the ARIA Singles Chart and was also listed at number 2 on the Triple J Hottest 100, 2016. Her album Love Monster debuted at number 1 on the ARIA Albums Chart. Shark has won 8 ARIA Music Awards from 29 nominations, including winning Best Pop Release three times: in 2017 for her extended play, Night Thinker, 2018 for Love Monster and 2020 for "Everybody Rise".read less...

Amy Acker

Amy Louise Acker is an American actress. She is best known for starring as Winifred Burkle and Illyria on the supernatural drama series Angel (2001–2004), as Kelly Peyton on the action drama series read more...Alias (2005–2006), and as Root on the science-fiction drama series Person of Interest (2012–2016). From 2017 to 2019, she starred as Caitlin Strucker on the superhero drama series The Gifted, based on Marvel Comics' X-Men.read less...

Amyloid beta

Amyloid beta denotes peptides of 36–43 amino acids that are the main component of the amyloid plaques found in the brains of people with Alzheimer's disease. The peptides derive from the amyloid-betread more...a precursor protein (APP), which is cleaved by beta secretase and gamma secretase to yield Aβ in a cholesterol-dependent process and substrate presentation. Aβ molecules can aggregate to form flexible soluble oligomers which may exist in several forms. It is now believed that certain misfolded oligomers can induce other Aβ molecules to also take the misfolded oligomeric form, leading to a chain reaction akin to a prion infection. The oligomers are toxic to nerve cells. The other protein implicated in Alzheimer's disease, tau protein, also forms such prion-like misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau to misfold.read less...

Amyloid

Amyloids are aggregates of proteins characterised by a fibrillar morphology of typically 7–13 nm in diameter, a β-sheet secondary structure and ability to be stained by particular dyes, such as Conread more...go red. In the human body, amyloids have been linked to the development of various diseases. Pathogenic amyloids form when previously healthy proteins lose their normal structure and physiological functions (misfolding) and form fibrous deposits within and around cells. These protein misfolding and deposition processes disrupt the healthy function of tissues and organs.read less...

Amyloid plaques

Amyloid plaques are extracellular deposits of the amyloid beta (Aβ) protein mainly in the grey matter of the brain. Degenerative neuronal elements and an abundance of microglia and astrocytes can be read more...associated with amyloid plaques. Some plaques occur in the brain as a result of aging, but large numbers of plaques and neurofibrillary tangles are characteristic features of Alzheimer's disease. Abnormal neurites in amyloid plaques are tortuous, often swollen axons and dendrites. The neurites contain a variety of organelles and cellular debris, and many of them include characteristic paired helical filaments, the ultrastructural component of neurofibrillary tangles. The plaques are highly variable in shape and size; in tissue sections immunostained for Aβ, they comprise a log-normal size distribution curve with an average plaque area of 400-450 square micrometers (µm²). The smallest plaques, which often consist of diffuse deposits of Aβ, are particularly numerous. The apparent size of plaques is influenced by the type of stain used to detect them, and by the plane through which they are sectioned for analysis under the microscope. Plaques form when Aβ misfolds and aggregates into oligomers and longer polymers, the latter of which are characteristic of amyloid. Misfolded and aggregated Aβ is thought to be neurotoxic, especially in its oligomeric state.read less...

Amyloid-beta precursor protein

Amyloid-beta precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor and has been implicaread more...ted as a regulator of synapse formation, neural plasticity, antimicrobial activity, and iron export. It is coded for by the gene APP and regulated by substrate presentation. APP is best known as the precursor molecule whose proteolysis generates amyloid beta (Aβ), a polypeptide containing 37 to 49 amino acid residues, whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients.read less...