Mapping Unstructured Regions and Synergistic Folding in Intrinsically Disordered Proteins with Amide H/D Exchange Mass Spectrometry-Reference-Cited by-同舟云学术

Mapping Unstructured Regions and Synergistic Folding in Intrinsically Disordered Proteins with Amide H/D Exchange Mass Spectrometry

Published:2011-09-19 Issue:40 Volume:50 Page:8722-8732
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Keppel Theodore R.¹,Howard Brent A.¹,Weis David D.¹

Affiliation:

1. Department of Chemistry and ‡Ralph N. Adams Institute for Bioanalytical Chemistry, University of Kansas, 1251 Wescoe Hall Drive, Lawrence, Kansas 66045, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200875p

Reference70 articles.

1. Acid blobs and negative noodles

2. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity.

3. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

4. Why are ?natively unfolded? proteins unstructured under physiologic conditions?

Cited by 75 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. Exploration of Resveratrol as a Potent Modulator of α-Synuclein Fibril Formation;ACS Chemical Neuroscience;2024-01-09

2. Allosteric Regulation of Glycogen Phosphorylase by Order/Disorder Transition of the 250′ and 280s Loops;Biochemistry;2023-03-29

3. Online Fully Automated System for Hydrogen/Deuterium-Exchange Mass Spectrometry with Millisecond Time Resolution;Analytical Chemistry;2023-03-10

4. Developments in rapid hydrogen–deuterium exchange methods;Essays in Biochemistry;2023-03

5. Methods for measuring structural disorder in proteins;Structure and Intrinsic Disorder in Enzymology;2023