Sara Linse

Professor

Lund University

Sweden

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Professor Sara Linse is a faculty member at Lund University in Sweden. Her research focuses on protein aggregation and amyloid diseases, exploring topics such as the design of tau aggregation inhibitors, kinetics of seeded protein aggregation, and the role of chaperone proteins in amyloid suppression. Recent publications highlight her contributions to understanding the mechanisms of amyloid-beta coaggregation and lipid-induced condensate formation related to Alzheimer's disease.

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2022

Collaborators (18)

Tuomas Knowles

Professor of Physical Chemistry and Biophysics

University of Cambridge

UNITED KINGDOM

Sara Linse

Research Interests

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About

Articles (29)

General integrated rate law for complex self-assembly reactions reveals the mechanism of amyloid-beta coaggregation

Reduced protein solubility – cause or consequence in amyloid disease?

α-Synuclein interaction with POPC/POPS vesicles

Air–Water Interfacial Adsorption of the Chaperone Protein DNAJB6b

Design of Tau Aggregation Inhibitors Using Iterative Machine Learning and a Polymorph-Specific Brain-Seeded Fibril Amplification Assay

Kinetics of seeded protein aggregation: Theory and application

The Role of α-Synuclein–DNAJB6b Coaggregation in Amyloid Suppression

On the reversibility of amyloid fibril formation

Lipid-induced condensate formation from the Alzheimer’s Aβ peptide triggers amyloid aggregation

On the self-assembly of αB-crystallin

Self-replication of A β 42 aggregates occurs on small and isolated fibril sites

Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces

A Relationship between the Structures and Neurotoxic Effects of Aβ Oligomers Stabilized by Different Metal Ions

The Ability of DNAJB6b to Suppress Amyloid Formation Depends on the Chaperone Aggregation State

Interplay of α-synuclein with Lipid Membranes: Cooperative Adsorption, Membrane Remodeling and Coaggregation

Kinetic models reveal the interplay of protein production and aggregation

Structural characterisation of α-synuclein–membrane interactions and the resulting aggregation using small angle scattering

Structural characterization of E22G Aβ1–42 fibrils via1H detected MAS NMR

Amyloid formation as a protein phase transition

A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ42 Aggregation

Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates

Amyloids and protein aggregation

Photo-Induced Cross-Linking of Unmodified α-Synuclein Oligomers

Direct observation of secondary nucleation along the fibril surface of the amyloid β 42 peptide

Morphology-Dependent Interactions between α-Synuclein Monomers and Fibrils

On the micelle formation of DNAJB6b

Ganglioside Micelles Affect Amyloid β Aggregation by Coassembly

α-Synuclein Interaction with Lipid Bilayer Discs

Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary Nucleation

Collaborators (18)

Tuomas Knowles

Enming Zhang

Christopher Waudby

Ulf Olsson

Michele Vendruscolo

Katarzyna Makasewicz

Thomas Michaels

Max Lindberg

Tinna Pálmadóttir

Marco Fornasier

Francesco Simone Ruggeri

Yun Liu

Daoyuan Qian

Robert Griffin

Ryan Limbocker

Emma Sparr

Andela Saric

Anders Malmendal

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