Tuomas P. J. Knowles

Molecular Biology · 2006–2020

A researcher in the Science corpus: 15 papers; trusts 9 researchers and is trusted by 9 researchers here, as inferred from the citation graph.

Subfields

Molecular Biology — 168 citations into it; #5,278 of 17,773 by trust here, #4,050 by citations
Physiology — 109 citations into it; #341 of 2,276 by trust here, #342 by citations
Cell Biology — 37 citations into it; #1,193 of 2,073 by trust here, #1,487 by citations
Materials Chemistry — 33 citations into it
Biomaterials — 29 citations into it; #803 of 2,152 by trust here, #808 by citations
Pharmacology — 12 citations into it
Ecology — 7 citations into it
Computational Theory and Mathematics — 5 citations into it

Whom Tuomas P. J. Knowles trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

Who trusts Tuomas P. J. Knowles overall

Papers from Tuomas P. J. Knowles's perspective

Ordered by how strongly the researchers Tuomas P. J. Knowles trusts endorse each paper. Same corpus, a different order for every researcher.

Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis (Science)
Amyloid fibrils from muscle myoglobin (Nature)
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (Nature)
The physical basis of how prion conformations determine strain phenotypes (Nature)
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)
Opposing Activities Protect Against Age-Onset Proteotoxicity (Science)
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)
Adapting Proteostasis for Disease Intervention (Science)
Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. (Proceedings of the National Academy of Sciences of the United States of America)

Their papers

Characterization of the nanoscale properties of individual amyloid fibrils (2006) — 620 citations
The amyloid state and its association with protein misfolding diseases (2014) — 977 citations
An Analytical Solution to the Kinetics of Breakable Filament Assembly (2009) — 1,109 citations
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism (2013) — 1,339 citations
Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils (2007) — 747 citations
Nanomechanics of functional and pathological amyloid materials. (2011) — 745 citations
On the lag phase in amyloid fibril formation (2015) — 629 citations
Strength of Nanotubes, Filaments, and Nanowires From Sonication‐Induced Scission (2009) — 151 citations
The amyloid state and its association with protein misfolding diseases (2014) — 1,371 citations
FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions (2018) — 818 citations
Biomimetic peptide self-assembly for functional materials (2020) — 600 citations
Molecular mechanisms of protein aggregation from global fitting of kinetic models (2016) — 682 citations
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation (2015) — 634 citations
Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation (2014) — 658 citations
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein (2012) — 885 citations