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https://www.selleckchem.com/products/chir-99021-ct99021-hcl.html The mechanical interpretation of the plethora of factors that governs cellular localization of amyloid aggregates is crucial for planning novel therapeutical interventions in neurodegenerative diseases since these aggregates exert a primary role in the proteostasis machinery. The uptake of Cell Penetrating Peptides (CPPs) conjugated with different amyloid polypeptides occurs via different endocytic processes regulated by cytoskeleton organization and cell morphology. Herein, we deepened the internalization of an amyloid system in cells cultured on nanopatterned surfaces that represent a powerful tool to shape cell and regulate its contractility. We analyzed the behavior of an amyloid model system, employing NPM1264-277 sequence, covalently conjugated to Tat fragment 48-60 as CPP. To investigate its internalization mechanism, we followed the formation of aggregates on two kinds of substrates a flat and a nanopatterned surface. Herein, investigations during time were carried out by employing both confocal and second harmonic generation (SHG) microscopies. We showed that modifications of cellular environment affect peptide localization, its cytoplasmic translocation and the size of amyloid aggregates. It is generally agreed that optimal head positioning is an important consideration in acute stroke management regime. However, there is limited literature investigating the effect of head positioning changes on cerebrovascular physiology in acute ischemic stroke (AIS). We aim to assess cerebral autoregulation (CA) and associated hemodynamic responses during gradual head positioning (GHP) changes, between AIS and controls. Cerebral blood flow velocity (CBFV, transcranial Doppler), blood pressure (BP, Finometer) and end-tidal CO (capnography) were recorded between lying flat (0°) and sitting up (30°) head position, in 16 controls (8 women, mean age 57±16yrs) and 15 AIS patients (7 women, 69±8yrs). AIS patients

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