Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins-Reference-Cited by-同舟云学术

Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins

Published:2016-08-19 Issue:35 Volume:55 Page:4885-4908
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lea Wendy A.¹,O’Neil Pierce T.¹,Machen Alexandra J.¹,Naik Subhashchandra¹,Chaudhri Tapan²,McGinn-Straub Wesley³,Tischer Alexander⁴,Auton Matthew T.⁴,Burns Joshua R.⁵,Baldwin Michael R.⁵,Khar Karen R.⁶,Karanicolas John⁶,Fisher Mark T.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas 66160, United States

2. Indian Institute of Technology, Delhi, India

3. fortéBIO (a division of Pall Life Sciences), Menlo Park, California 94025, United States

4. Division of Hematology, Department of Internal Medicine, Mayo Clinic, Rochester, Minnesota 55902, United States

5. Department of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri 65212, United States

6. Center for Computational Biology and Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, United States

Funder

National Heart, Lung, and Blood Institute

Office of Experimental Program to Stimulate Competitive Research

National Institute of Allergy and Infectious Diseases

University of Kansas

National Institute of General Medical Sciences

Kansas Board of Regents

US Department of Health and Human Services National Institutes of Health - Biotechnology Training Grant

the Madison and Lila Self Graduate Student Fellowship Grant

J.R. and Inez Jay Fund, University of Kansas

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00293

Reference88 articles.

1. Differential scanning calorimetry as a tool for protein folding and stability

2. Comparison of fluorescence and light scattering based methods to assess formation and stability of protein–protein complexes

3. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

4. Differential Scanning Fluorometry Signatures as Indicators of Enzyme Inhibitor Mode of Action: Case Study of Glutathione S-Transferase

5. Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination

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