S. Linse
Molecular Biology · 2007–2017
A researcher in the Science corpus: 11 papers; trusts 1 researcher and is trusted by 6 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 62 citations into it; #9,188 of 17,773 by trust here, #2,739 by citations
- Physiology — 48 citations into it; #1,580 of 2,276 by trust here, #776 by citations
Whom S. Linse trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
Who trusts S. Linse overall
Papers from S. Linse's perspective
Ordered by how strongly the researchers S. Linse trusts endorse each paper. Same corpus, a different order for every researcher.
- Oligomeric amyloid β associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques (Proceedings of the National Academy of Sciences of the United States of America)
- An Analytical Solution to the Kinetics of Breakable Filament Assembly (Science)
- Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein (Cell)
- The physical basis of how prion conformations determine strain phenotypes (Nature)
- Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease (Nature Medicine)
- Strength of Nanotubes, Filaments, and Nanowires From Sonication‐Induced Scission
- Global Optimization by Basin-Hopping and the Lowest Energy Structures of Lennard-Jones Clusters Containing up to 110 Atoms
- Protein misfolding, functional amyloid, and human disease. (Annual Review of Biochemistry)
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis (Science)
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (Nature)
Their papers
- Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles (2007) — 3,037 citations
- Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism (2013) — 1,339 citations
- Nucleation of protein fibrillation by nanoparticles (2007) — 836 citations
- On the lag phase in amyloid fibril formation (2015) — 629 citations
- The nanoparticle-protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century. (2007) — 711 citations
- Methods for the detection and analysis of protein–protein interactions (2007) — 656 citations
- Detailed identification of plasma proteins adsorbed on copolymer nanoparticles. (2007) — 825 citations
- Brain damage and behavioural disorders in fish induced by plastic nanoparticles delivered through the food chain (2017) — 665 citations
- Molecular mechanisms of protein aggregation from global fitting of kinetic models (2016) — 682 citations
- Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils (2016) — 704 citations
- Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation (2014) — 658 citations