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Sebastian K.T.S. Wärmländer

Researcher at Stockholm University

Publications -  105
Citations -  2846

Sebastian K.T.S. Wärmländer is an academic researcher from Stockholm University. The author has contributed to research in topics: Amyloid & Peptide. The author has an hindex of 28, co-authored 92 publications receiving 2231 citations. Previous affiliations of Sebastian K.T.S. Wärmländer include University of California, Los Angeles & University of California, Santa Barbara.

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Effects of in vivo conditions on amyloid aggregation.

TL;DR: The aim of this review is to document the progress in the research onAmyloid formation from a physicochemical perspective with a special focus on the physiological factors influencing the aggregation of the amyloid-β peptide, the islet amyloids polypeptide, α-synuclein, and the hungingtin protein.
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Variation in the Measurement of Cranial Volume and Surface Area Using 3D Laser Scanning Technology

TL;DR: Assessment of the repeatability and precision of cranial volume and surface area measurements using 3D laser scanner models created by different operators using different protocols for collecting and processing data suggests that observer‐related errors do not pose major obstacles for sharing, combining, or comparing such measurements.
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Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis

TL;DR: It is argued that the amyloids cascade hypothesis in Alzheimer disease should be expanded to include cross-interactions between Aβ and other amyloid proteins.
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Comparison of coordinate measurement precision of different landmark types on human crania using a 3D laser scanner and a 3D digitiser: Implications for applications of digital morphometrics

TL;DR: The results indicate that the suitability of certain landmark types as reference points for geometric operations, such as partial Procrustes analysis, depends on the method by which they are measured, and both techniques yield coordinate data with a precision sufficient for most craniometric research.
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In vitro and mechanistic studies of an antiamyloidogenic self-assembled cyclic D,L-α-peptide architecture.

TL;DR: The results support studies suggesting that toxic early oligomeric states of Aβ may be composed of antiparallel β-peptide structures and that the interaction of A β with CP-2 promotes formation of more benign parallel β-structures.