The DOI matches its Crossref record; 140 of the 140 references it cites were found in a registry or an index.
Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
Open accessAbstract
Pin1 is a highly conserved enzyme that only isomerizes specific phosphorylated Ser/Thr-Pro bonds in certain proteins, thereby inducing conformational changes. Such conformational changes represent a novel and tightly controlled signaling mechanism regulating a spectrum of protein activities in physiology and disease, often through phosphorylation-dependent, ubiquitin-mediated proteasomal degradation. In this review, we summarize recent advances in elucidating the role and regulation of Pin1 in controlling protein stability. We also propose a mechanism by which Pin1 functions as a molecular switch to control the fates of phosphoproteins. We finally stress the need to develop tools to directly visualize Pin1-catalyzed protein conformational changes as a way to determine their roles in the development and treatment of human diseases.
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Metadata
- Authors
- Liou, Y.-C., Zhou, X. Z., & Lu, K. P.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2011-10
- Volume
- 36
- Issue
- 10
- Pages
- 501-514
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2059977521
- Cited by
- 326
- References
- 140
- FWCI
- 1.94
- Type
- journal article
- Language
- en
- Open access
- green
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- Liou, Y.-C., Zhou, X. Z., & Lu, K. P. (2011). Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2011.07.001
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