Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/92563
DC Field | Value | Language |
---|---|---|
dc.contributor | Department of Applied Biology and Chemical Technology | en_US |
dc.contributor | University Research Facility in Life Sciences | en_US |
dc.contributor | School of Optometry | en_US |
dc.contributor | Research Centre for SHARP Vision | en_US |
dc.creator | Guo, H | en_US |
dc.creator | Yang, Y | en_US |
dc.creator | Zhang, Q | en_US |
dc.creator | Deng, JR | en_US |
dc.creator | Yang, Y | en_US |
dc.creator | Li, S | en_US |
dc.creator | So, PK | en_US |
dc.creator | Lam, TC | en_US |
dc.creator | Wong, M | en_US |
dc.creator | Zhao, Q | en_US |
dc.date.accessioned | 2022-04-26T06:01:02Z | - |
dc.date.available | 2022-04-26T06:01:02Z | - |
dc.identifier.issn | 1554-8929 | en_US |
dc.identifier.uri | http://hdl.handle.net/10397/92563 | - |
dc.language.iso | en | en_US |
dc.publisher | American Chemical Society | en_US |
dc.rights | © 2022 American Chemical Society | en_US |
dc.rights | This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Chemical Biology, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://dx.doi.org/10.1021/acschembio.2c00011. | en_US |
dc.title | Integrated mass spectrometry reveals celastrol as a novel Catechol-O-methyltransferase inhibitor | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.spage | 2003 | en_US |
dc.identifier.epage | 2009 | en_US |
dc.identifier.volume | 17 | en_US |
dc.identifier.issue | 8 | en_US |
dc.identifier.doi | 10.1021/acschembio.2c00011 | en_US |
dcterms.abstract | Natural product celastrol is known to have various biological activities, yet its molecular targets that correspond to many activities remain unclear. Here, we used multiple mass-spectrometry-based approaches to identify catechol-O-methyltransferase (COMT) as a major binding target of celastrol and characterized their interaction comprehensively. Celastrol was found to inhibit the enzymatic activity of COMT and increased the dopamine level in neuroendocrine chromaffin cells significantly. Our study not only revealed a novel binding target of celastrol but also provided a new scaffold and cysteine hot spot for developing new generation COMT inhibitors in combating neurological disorders. | en_US |
dcterms.accessRights | open access | en_US |
dcterms.bibliographicCitation | ACS chemical biology, 19 Aug. 2022, v. 17, no. 8, p. 2003–2009 | en_US |
dcterms.isPartOf | ACS chemical biology | en_US |
dcterms.issued | 2022-08-19 | - |
dc.identifier.eissn | 1554-8937 | en_US |
dc.description.validate | 202204 bchy | en_US |
dc.description.oa | Accepted Manuscript | en_US |
dc.identifier.FolderNumber | a1294-n02 | - |
dc.description.fundingSource | RGC | en_US |
dc.description.fundingText | Research Grants Council-ECS 25301518, GRF 15304819, CRF C5033-19E, and RGC-RIF R5050-18, NSFC 21705136. | en_US |
dc.description.pubStatus | Published | en_US |
Appears in Collections: | Journal/Magazine Article |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Guo_Mass_Spectrometry_Catechol-O-methyltransferase.pdf | Pre-Published version | 2.25 MB | Adobe PDF | View/Open |
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