Thermodynamic and fibril formation studies of full length immunoglobulin light chain AL-09 and its germline protein using scan rate dependent thermal unfolding-Reference-Cited by-同舟云学术

Thermodynamic and fibril formation studies of full length immunoglobulin light chain AL-09 and its germline protein using scan rate dependent thermal unfolding

Published:2015-12 Issue: Volume:207 Page:13-20
ISSN:0301-4622
Container-title:Biophysical Chemistry
language:en
Short-container-title:Biophysical Chemistry

Author:

Blancas-Mejía Luis M.,Horn Timothy J.,Marin-Argany Marta,Auton Matthew,Tischer Alexander,Ramirez-Alvarado Marina

Funder

National Institutes of Health

Dr. Morie Gertz

Seidler Professorship

Mayo Foundation

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Biophysics

Reference30 articles.

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3. Systemic amyloidoses;Blancas-Mejia;Annu. Rev. Biochem.,2013

4. Thermal stability threshold for amyloid formation in light chain amyloidosis;Poshusta;Int. J. Mol. Sci.,2013

5. Physical and chemical properties of amyloid fibers. II. Isolation of a unique protein constituting the major component from human splenic amyloid fibril concentrates;Glenner;J. Histochem. Cytochemi. Off. J. Histochem. Soc.,1969

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