Last Updated: 09/26/2026
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Found 12 publications
Feasibility of using real-world free thyroxine data from the US and Europe to enable fast and efficient transfer of reference intervals from one population to another.
Journal: Practical laboratory medicine
Published: May 12, 2023
Molecular mechanism of amyloidogenic mutations in hypervariable regions of antibody light chains.
Journal: The Journal of biological chemistry
Published: September 03, 2020
Domain Interactions Determine the Amyloidogenicity of Antibody Light Chain Mutants.
Journal: Journal of molecular biology
Published: July 07, 2020
Peptides in proteins.
Journal: Journal of peptide science : an official publication of the European Peptide Society
Published: October 25, 2019
Fatal amyloid formation in a patient's antibody light chain is caused by a single point mutation.
Journal: eLife
Published: September 28, 2019
A single residue switch reveals principles of antibody domain integrity.
Journal: The Journal of biological chemistry
Published: August 23, 2018
The Antibody Light-Chain Linker Regulates Domain Orientation and Amyloidogenicity.
Journal: Journal of molecular biology
Published: July 13, 2018
A peptide extension dictates IgM assembly.
Journal: Proceedings of the National Academy of Sciences of the United States of America
Published: October 05, 2017
ThT 101: a primer on the use of thioflavin T to investigate amyloid formation.
Journal: Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis
Published: April 11, 2017
Determinants of the assembly and function of antibody variable domains.
Journal: Scientific reports
Published: February 23, 2017
Solid- and solution-state nuclear magnetic resonance spectroscopic studies on antibody light chain amyloid formation and interactions with epigallocatechin gallate.
Journal: Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis
Published: December 27, 2016
Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.
Journal: Scientific reports
Published: September 27, 2016
Showing 1-12 of 12
Last Updated: 09/26/2026