Show simple item record

dc.contributor.authorThapa, Chandan J.
dc.contributor.authorHaataja, Tatu
dc.contributor.authorPentikäinen, Ulla
dc.contributor.authorPermi, Perttu
dc.date.accessioned2020-06-03T04:16:49Z
dc.date.available2020-06-03T04:16:49Z
dc.date.issued2020
dc.identifier.citationThapa, Chandan J.; Haataja, Tatu; Pentikäinen, Ulla; Permi, Perttu (2020). 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16). Biomolecular NMR Assignments, Early online. DOI: 10.1007/s12104-020-09951-w
dc.identifier.otherCONVID_35788340
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/69659
dc.description.abstractProtein Phosphatase 2A, PP2A, the principal Serine/threonine phosphatase, has major roles in broad range of signaling pathways that include regulation of cell cycle, cell proliferation and neuronal signaling. The loss of function of PP2A is linked with many human diseases, like cancer and neurodegenerative disorders. Protein phosphatase 2A (PP2A) functions as tumor suppressor and its tumor suppressor activity is inhibited by the overexpression of PP2A inhibitor proteins in most of the cancers. ARPP-19/ARPP-16 has been identified as one of the potential PP2A inhibitor proteins. Here, we report the resonance assignment of backbone 1H, 13C and 15N atoms of human ARPP-19 and ARPP-16 proteins. These chemical shift values can provide valuable information for the further study of the dynamics and interaction of ARPP-proteins to PP2A using NMR spectroscopy.en
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.publisherSpringer
dc.relation.ispartofseriesBiomolecular NMR Assignments
dc.rightsCC BY 4.0
dc.subject.otherassignments
dc.subject.othercAMP-regulated phosphoprotein-19
dc.subject.otherHA-detection, intrinsically disordered protein
dc.subject.otherNMR spectroscopy
dc.title1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16)
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202006033917
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.description.reviewstatuspeerReviewed
dc.relation.issn1874-2718
dc.relation.volumeEarly online
dc.type.versionpublishedVersion
dc.rights.copyright© The Authors, 2020
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber283481
dc.relation.grantnumber288235
dc.subject.ysosoluviestintä
dc.subject.ysoentsyymit
dc.subject.ysoNMR-spektroskopia
dc.subject.ysoproteiinit
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p28740
jyx.subject.urihttp://www.yso.fi/onto/yso/p4769
jyx.subject.urihttp://www.yso.fi/onto/yso/p26254
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.1007/s12104-020-09951-w
dc.relation.funderSuomen Akatemiafi
dc.relation.funderSuomen Akatemiafi
dc.relation.funderAcademy of Finlanden
dc.relation.funderAcademy of Finlanden
jyx.fundingprogramAkatemiatutkijan tutkimuskulut, SAfi
jyx.fundingprogramAkatemiahanke, SAfi
jyx.fundingprogramResearch costs of Academy Research Fellow, AoFen
jyx.fundingprogramAcademy Project, AoFen
jyx.fundinginformationOpen access funding provided by University of Jyväskylä (JYU). This work is supported by grants from Academy of Finland (Number 288235 to PP and 28348 to UP). Chandan Thapa is a recipient of doctoral student scholarship from the University of Jyvaskyla Graduate School (JYUGS), Department of Biological and Environmental science, University of Jyvaskyla.


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

CC BY 4.0
Except where otherwise noted, this item's license is described as CC BY 4.0