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Amyloid
The Journal of Protein Folding Disorders
Volume 24, 2017 - Issue sup1: PROCEEDINGS OF THE XVth INTERNATIONAL SYMPOSIUM ON AMYLOIDOSIS
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Letters

Recruitment of human light chain proteins by synthetic fibrils is dependent on disease state and may be used to predict amyloidogenic propensity

Emily B. MartinDepartment of Medicine and Correspondence[email protected]
,
Angela WilliamsDepartment of Medicine and
,
Craig WooliverDepartment of Medicine and
,
R. Eric HeidelDepartment of Surgery, University of Tennessee Medical Center, Knoxville, TN, USA,
,
Sarah AdamsDepartment of Surgery, University of Tennessee Medical Center, Knoxville, TN, USA,
,
John DunlapMicroscopy and Imaging Center, University of Tennessee, Knoxville, TN, USA,
,
Marina Ramirez-AlvaradoDepartments of Biochemistry and Molecular Biology, and Immunology, Mayo Clinic, Rochester, NY, USA, and
,
Luis Blancas-MejiaDepartments of Biochemistry and Molecular Biology, and Immunology, Mayo Clinic, Rochester, NY, USA, and
,
Stephen J. KennelDepartment of Medicine and ;Department of Radiology, University of Tennessee Medical Center, Knoxville, TN, USA
&
Jonathan S. WallDepartment of Medicine and ;Department of Radiology, University of Tennessee Medical Center, Knoxville, TN, USA
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Pages 24-25 | Received 15 Nov 2016, Accepted 12 Feb 2017, Published online: 22 Apr 2017
 
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"Recruitment of human light chain proteins by synthetic fibrils is dependent on disease state and may be used to predict amyloidogenic propensity." Amyloid, 24(sup1), pp. 24–25

Declaration of interest

EBM and JSW are named on a patent application that describes the use of a recruitment assay to discriminate LC proteins with amyloidogenic potential.

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