Journal article
Fully automated radiosynthesis of N1-[18F]fluoroethyl-tryptophan and study of its biological activity as a new potential substrate for indoleamine 2,3-dioxygenase PET imaging
- Abstract:
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Introduction Indoleamine 2,3-dioxygenase (IDO) catalyzes the initial step in the catabolism of l-tryptophan along the kynurenine pathway and exerts immunosuppressive properties in inflammatory and tumor tissues by blocking locally T-lymphocyte proliferation. Recently, 1-(2-[19F]fluoroethyl)-dl-tryptophan (1-[19F]FE-dl-Trp) was reported as a good and specific substrate of this enzyme. Herein, the radiosynthesis of its radioactive isotopomer (1-[18F]FE-dl-Trp, dl-[18F]5) is presented along with...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Accepted manuscript, pdf, 962.1KB, Terms of use)
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- Publisher copy:
- 10.1016/j.nucmedbio.2016.03.001
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Bibliographic Details
- Publisher:
- Elsevier
- Journal:
- Nuclear Medicine and Biology More from this journal
- Volume:
- 43
- Issue:
- 6
- Pages:
- 379-389
- Publication date:
- 2016-03-11
- Acceptance date:
- 2016-03-07
- DOI:
- EISSN:
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1872-9614
- ISSN:
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0969-8051
- Pmid:
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27260779
Item Description
- Language:
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English
- Keywords:
- Pubs id:
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pubs:809049
- UUID:
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uuid:14be154d-fc89-4f77-96c9-8f1cd16e213b
- Local pid:
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pubs:809049
- Source identifiers:
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809049
- Deposit date:
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2017-12-11
Terms of use
- Copyright holder:
- *Copyright holder name ("et al" as required)*
- Copyright date:
- 2016
- Notes:
- © 2016 Elsevier Inc. All rights reserved. This is the accepted manuscript version of the article. The final version is available online from Elsevier at: https://doi.org/10.1016/j.nucmedbio.2016.03.001
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