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Cellular localization of p-tau217 in brain and its association with p-tau217 plasma levelsNeuronal α-amylase is important for neuronal activity and glycogenolysis and reduces in presence of amyloid beta pathologyAmyloid-beta 1-40 is associated with alterations in NG2+ pericyte population ex vivo and in vitroA Potential Role for α-Amylase in Amyloid-β-Induced Astrocytic Glycogenolysis and ActivationLevels of retinal IAPP are altered in Alzheimer's disease patients and correlate with vascular changes and hippocampal IAPP levelsIncreased plasma and brain immunoglobulin A in Alzheimer's disease is lost in apolipoprotein E ε4 carriersBrain alpha-amylase - a novel energy regulator important in Alzheimer disease?Plasma IAPP-Autoantibody Levels in Alzheimer's Disease Patients Are Affected by APOE4 StatusThe fluorescent ligand bTVBT2 reveals increased p-tau uptake by retinal microglia in Alzheimer's disease patients and AppNL-F/NL-F miceThe Relationship between p-tau217, p-tau231, and p-tau205 in the Human Brain Is Affected by the Cellular Environment and Alzheimer's Disease PathologyLevels of Retinal Amyloid-β Correlate with Levels of Retinal IAPP and Hippocampal Amyloid-β in Neuropathologically Evaluated IndividualsContraction of human brain vascular pericytes in response to islet amyloid polypeptide is reversed by pramlintide
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Malin Wennström