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dc.contributor.authorLondhe, Avinash D.
dc.contributor.authorBergeron, Alexandre
dc.contributor.authorCurley, Stephanie M.
dc.contributor.authorZhang, Fuming
dc.contributor.authorRivera, Keith D.
dc.contributor.authorKannan, Akaash
dc.contributor.authorCoulis, Gérald
dc.contributor.authorRizvi, Syed H.M.
dc.contributor.authorKim, Seung Jun
dc.contributor.authorPappin, Darryl J.
dc.contributor.authorTonks, Nicholas K.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorBoivin, Benoit
dc.date2020
dc.date.accessioned2022-06-23T04:45:59Z
dc.date.available2022-06-23T04:45:59Z
dc.date.issued2020-02-01
dc.identifier.citationRegulation 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.issn15524469
dc.identifier.issn15524450
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5397
dc.identifier.urihttps://doi.org/10.1038/s41589-019-0433-0
dc.descriptionNature Chemical Biology, 16, 122-125
dc.descriptionNote : 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.abstractWe 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.sponsorshipNational Institutes of Health
dc.languageen_US
dc.language.isoENG
dc.publisherNature
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofNature Chemical Biology
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleRegulation of PTP1B activation through disruption of redox-complex formation
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1038/s41589-019-0433-0
dc.rights.holderIn 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.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages122-125
rpi.description.volume16


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