Karthikeyan Annamalai
Ulm, BW, Germany
Last Updated: 09/26/2026
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Found 9 publications
Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability.
Journal: The Journal of biological chemistry
Published: September 10, 2020
Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril.
Journal: Biomolecular NMR assignments
Published: June 22, 2020
Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis.
Journal: Nature communications
Published: December 06, 2018
Physical basis of amyloid fibril polymorphism.
Journal: Nature communications
Published: July 25, 2017
Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.
Journal: Angewandte Chemie (International ed. in English)
Published: February 17, 2017
Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril.
Journal: Proceedings of the National Academy of Sciences of the United States of America
Published: May 18, 2016
Polymorphism of Amyloid Fibrils In Vivo.
Journal: Angewandte Chemie (International ed. in English)
Published: December 11, 2015
Systemic Amyloid A Amyloidosis in Island Foxes (Urocyon littoralis): Severity and Risk Factors.
Journal: Veterinary pathology
Published: October 01, 2015
Molecular basis of β-amyloid oligomer recognition with a conformational antibody fragment.
Journal: Proceedings of the National Academy of Sciences of the United States of America
Published: July 21, 2012
Showing 1-9 of 9
Last Updated: 09/26/2026