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A new era for understanding amyloid structures and disease

Nature reviews. Molecular cell biology, 2018-12, Vol.19 (12), p.755-773

2018

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Macromolecular Crowding Enhances the Detection of DNA and Proteins by a Solid-State Nanopore

Nano letters, 2020-07, Vol.20 (7), p.5553-5561

2020

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Cellular proteostasis: degradation of misfolded proteins by lysosomes

Essays in biochemistry, 2016-10, Vol.60 (2), p.173-180

2016

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Modulation of β-Amyloid Fibril Formation in Alzheimer's Disease by Microglia and Infection

Frontiers in molecular neuroscience, 2020-11, Vol.13, p.609073-609073

2020

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Fibril Fragmentation Enhances Amyloid Cytotoxicity

The Journal of biological chemistry, 2009-12, Vol.284 (49), p.34272-34282

2009

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Direct three-dimensional visualization of membrane disruption by amyloid fibrils

Proceedings of the National Academy of Sciences - PNAS, 2012-12, Vol.109 (50), p.20455-20460

2012

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The MHC class I antigen presentation pathway: strategies for viral immune evasion

Immunology, 2003-10, Vol.110 (2), p.163-169

Hewitt, Eric W.

2003

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pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers

Proceedings of the National Academy of Sciences - PNAS, 2015-05, Vol.112 (18), p.5691-5696

2015

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Single molecule delivery into living cells

Nature communications, 2024-05, Vol.15 (1), p.4403-4403, Article 4403

2024

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Why are Functional Amyloids Non-Toxic in Humans?

Biomolecules (Basel, Switzerland), 2017-09, Vol.7 (4), p.71

2017

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Structural mapping of oligomeric intermediates in an amyloid assembly pathway

eLife, 2019-09, Vol.8

2019

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Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation

Journal of molecular biology, 2016-02, Vol.428 (3), p.631-643

2016

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β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH

PloS one, 2014-08, Vol.9 (8), p.e104492-e104492

2014

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Kaposi's Sarcoma-Associated Herpesvirus RTA Promotes Degradation of the Hey1 Repressor Protein through the Ubiquitin Proteasome Pathway

Journal of Virology, 2009-07, Vol.83 (13), p.6727-6738

2009

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Aggregation Modulators Interfere with Membrane Interactions of β2-Microglobulin Fibrils

Biophysical journal, 2013-08, Vol.105 (3), p.745-755

2013

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Analysis of familial hemophagocytic lymphohistiocytosis type 4 (FHL-4) mutant proteins reveals that S-acylation is required for the function of syntaxin 11 in natural killer cells

PloS one, 2014-06, Vol.9 (6), p.e98900-e98900

2014

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Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters

Prion, 2010-01, Vol.4 (1), p.20-25

2010

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Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease?

Trends in biochemical sciences (Amsterdam. Regular ed.), 2015-12, Vol.40 (12), p.719-727

2015

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Natural killer cell cytotoxicity: how do they pull the trigger

Immunology, 2009-09, Vol.128 (1), p.7-15

2009

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A Systematic Study of the Effect of Physiological Factors on β2-Microglobulin Amyloid Formation at Neutral pH

Biochemistry (Easton), 2006-02, Vol.45 (7), p.2311-2321

2006

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Structural and Functional Dissection of the Human Cytomegalovirus Immune Evasion Protein US6

Journal of Virology, 2008-04, Vol.82 (7), p.3271-3282

2008

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Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils

PloS one, 2011-11, Vol.6 (11), p.e27353-e27353

2011

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Ligand binding to distinct states diverts aggregation of an amyloid-forming protein

Nature chemical biology, 2011-08, Vol.7 (10), p.730-739

2011

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β2-Microglobulin Amyloid Fibrils Are Nanoparticles That Disrupt Lysosomal Membrane Protein Trafficking and Inhibit Protein Degradation by Lysosomes

The Journal of biological chemistry, 2014-12, Vol.289 (52), p.35781-35794

2014

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Organelle proteomics: identification of the exocytic machinery associated with the natural killer cell secretory lysosome

Molecular & cellular proteomics, 2007-05, Vol.6 (5), p.767-780

2007

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A new era for understanding amyloid structures and disease

Macromolecular Crowding Enhances the Detection of DNA and Proteins by a Solid-State Nanopore

Cellular proteostasis: degradation of misfolded proteins by lysosomes

Modulation of β-Amyloid Fibril Formation in Alzheimer's Disease by Microglia and Infection

Fibril Fragmentation Enhances Amyloid Cytotoxicity

Direct three-dimensional visualization of membrane disruption by amyloid fibrils

The MHC class I antigen presentation pathway: strategies for viral immune evasion

pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers

Single molecule delivery into living cells

Why are Functional Amyloids Non-Toxic in Humans?

Structural mapping of oligomeric intermediates in an amyloid assembly pathway

Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation

β2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pH

Kaposi's Sarcoma-Associated Herpesvirus RTA Promotes Degradation of the Hey1 Repressor Protein through the Ubiquitin Proteasome Pathway

Aggregation Modulators Interfere with Membrane Interactions of β2-Microglobulin Fibrils

Analysis of familial hemophagocytic lymphohistiocytosis type 4 (FHL-4) mutant proteins reveals that S-acylation is required for the function of syntaxin 11 in natural killer cells

Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters

Amyloid Fibres: Inert End-Stage Aggregates or Key Players in Disease?

Natural killer cell cytotoxicity: how do they pull the trigger

A Systematic Study of the Effect of Physiological Factors on β2-Microglobulin Amyloid Formation at Neutral pH

Structural and Functional Dissection of the Human Cytomegalovirus Immune Evasion Protein US6

Characterization of the response of primary cells relevant to dialysis-related amyloidosis to β2-microglobulin monomer and fibrils

Ligand binding to distinct states diverts aggregation of an amyloid-forming protein

β2-Microglobulin Amyloid Fibrils Are Nanoparticles That Disrupt Lysosomal Membrane Protein Trafficking and Inhibit Protein Degradation by Lysosomes

Organelle proteomics: identification of the exocytic machinery associated with the natural killer cell secretory lysosome

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