Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery
Author:
Funder
Start-up package from the University of Colorado at Denver
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
http://link.springer.com/content/pdf/10.1007/s12104-018-9857-9.pdf
Reference26 articles.
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2. Bao L, Kimzey A, Sauter G et al (2004) Prevalent overexpression of prolyl isomerase Pin1 in human cancers. Am J Pathol 164:1727–1737. https://doi.org/10.1016/S0002-9440(10)63731-5
3. Bayer E, Goettsch S, Mueller JW et al (2003) Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding. J Biol Chem 278:26183–26193. https://doi.org/10.1074/jbc.M300721200
4. Blair LJ, Baker JD, Sabbagh JJ, Dickey CA (2015) The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer’s disease. J Neurochem 133:1–13. https://doi.org/10.1111/jnc.13033
5. Born A, Henen M, Nichols P et al (2018) Efficient stereospecific Hβ2/3 NMR assignment strategy for mid-size proteins. Magnetochemistry 4:25. https://doi.org/10.3390/magnetochemistry4020025
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