| dc.contributor.author | Londhe, Avinash D. | |
| dc.contributor.author | Bergeron, Alexandre | |
| dc.contributor.author | Curley, Stephanie M. | |
| dc.contributor.author | Zhang, Fuming | |
| dc.contributor.author | Rivera, Keith D. | |
| dc.contributor.author | Kannan, Akaash | |
| dc.contributor.author | Coulis, Gérald | |
| dc.contributor.author | Rizvi, Syed H.M. | |
| dc.contributor.author | Kim, Seung Jun | |
| dc.contributor.author | Pappin, Darryl J. | |
| dc.contributor.author | Tonks, Nicholas K. | |
| dc.contributor.author | Linhardt, Robert J. | |
| dc.contributor.author | Boivin, Benoit | |
| dc.date | 2020 | |
| dc.date.accessioned | 2022-06-23T04:45:59Z | |
| dc.date.available | 2022-06-23T04:45:59Z | |
| dc.date.issued | 2020-02-01 | |
| dc.identifier.citation | Regulation of PTP1B activation through disruption of redox-complex formation, A. D. Londhe, A. Bergeron, S. M. Curley, F. Zhang, K. D. Rivera, A. Kannan, G. Coulis, S. H. M. Rizvi, S. J. Kim, D. J. Pappin, N. K. Tonks, R. J. Linhardt, B. Boivin, Nature Chemical Biology, 16, 122-125, 2020. | |
| dc.identifier.issn | 15524469 | |
| dc.identifier.issn | 15524450 | |
| dc.identifier.uri | https://hdl.handle.net/20.500.13015/5397 | |
| dc.identifier.uri | https://doi.org/10.1038/s41589-019-0433-0 | |
| dc.description | Nature Chemical Biology, 16, 122-125 | |
| dc.description | Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform. | |
| dc.description.abstract | We have identified a molecular interaction between the reversibly oxidized form of protein tyrosine phosphatase 1B (PTP1B) and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B prevented PTP1B inactivation by reactive oxygen species and decreased epidermal growth factor receptor phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3ζ and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells. | |
| dc.description.sponsorship | National Institutes of Health | |
| dc.language | en_US | |
| dc.language.iso | ENG | |
| dc.publisher | Nature | |
| dc.relation.ispartof | The Linhardt Research Labs Online Collection | |
| dc.relation.ispartof | Rensselaer Polytechnic Institute, Troy, NY | |
| dc.relation.ispartof | Nature Chemical Biology | |
| dc.relation.uri | https://harc.rpi.edu/ | |
| dc.subject | Biology | |
| dc.subject | Chemistry and chemical biology | |
| dc.subject | Chemical and biological engineering | |
| dc.subject | Biomedical engineering | |
| dc.title | Regulation of PTP1B activation through disruption of redox-complex formation | |
| dc.type | Article | |
| dcterms.accessRights | A full text version is available in DSpace@RPI | |
| dcterms.isPartOf | Journal | |
| dcterms.isVersionOf | https://doi.org/10.1038/s41589-019-0433-0 | |
| dc.rights.holder | In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/ | |
| dc.creator.identifier | https://orcid.org/0000-0003-2219-5833 | |
| dc.relation.department | The Linhardt Research Labs. | |
| dc.relation.department | The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS) | |
| rpi.description.pages | 122-125 | |
| rpi.description.volume | 16 | |
