scispace - formally typeset
P

Pauline T. Velasco

Researcher at Northwestern University

Publications -  52
Citations -  6878

Pauline T. Velasco is an academic researcher from Northwestern University. The author has contributed to research in topics: Tissue transglutaminase & Crystallin. The author has an hindex of 28, co-authored 52 publications receiving 6453 citations. Previous affiliations of Pauline T. Velasco include University of North Carolina at Chapel Hill & Florida State University College of Arts and Sciences.

Papers
More filters
Journal ArticleDOI

Aβ Oligomer-Induced Aberrations in Synapse Composition, Shape, and Density Provide a Molecular Basis for Loss of Connectivity in Alzheimer's Disease

TL;DR: The observed disruption of dendritic spines links ADDLs to a major facet of AD pathology, providing strong evidence that AD DLs in AD brain cause neuropil damage believed to underlie dementia.
Journal ArticleDOI

Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers

TL;DR: The hypothesis that targeting and functional disruption of particular synapses by Aβ oligomers may provide a molecular basis for the specific loss of memory function in early Alzheimer's disease is suggested.
Journal ArticleDOI

Aβ Oligomers Induce Neuronal Oxidative Stress through an N-Methyl-D-aspartate Receptor-dependent Mechanism That Is Blocked by the Alzheimer Drug Memantine

TL;DR: This response provides a pathologically specific mechanism for the therapeutic action of memantine, indicates a role for ROS dysregulation in ADDL-induced cognitive impairment, and supports the unifying hypothesis that ADDLs play a central role in AD pathogenesis.
Journal ArticleDOI

Protection of synapses against Alzheimer's-linked toxins: Insulin signaling prevents the pathogenic binding of Aβ oligomers

TL;DR: The finding that synapse vulnerability to ADDLs can be mitigated by insulin suggests that bolstering brain insulin signaling, which can decline with aging and diabetes, could have significant potential to slow or deter AD pathogenesis.
Journal ArticleDOI

Self-assembly of Aβ1-42 into globular neurotoxins

TL;DR: Aβ 1−42 (Aβ1-42) is a self-associating peptide that becomes neurotoxic upon aggregation as discussed by the authors, and its toxicity originally was attributed to the presence of large, readily formed Aβ fibrils.