Isolation and Characterization of Rhodanese Intermediates during Thermal Inactivation and Their Implications for the Mechanism of Protein Aggregation
Author:
Affiliation:
1. Department of Biochemistry, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3900
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi011726q
Reference47 articles.
Cited by 10 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Polymorphic Variants of Human Rhodanese Exhibit Differences in Thermal Stability and Sulfur Transfer Kinetics;Journal of Biological Chemistry;2015-09
2. Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates;Journal of Molecular Biology;2013-04
3. The 69 kDaEscherichia colimaltodextrin glucosidase does not get encapsulated underneath GroES and folds throughtransmechanism during GroEL/ GroES‐assisted folding;The FASEB Journal;2007-05-10
4. Protection of GroEL by its methionine residues against oxidation by hydrogen peroxide;Biochemical and Biophysical Research Communications;2006-08
5. On the chaperonin activity of GroEL at heat-shock temperature;The International Journal of Biochemistry & Cell Biology;2005-07
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