000476470 001__ 476470
000476470 005__ 20250724151417.0
000476470 0247_ $$2doi$$a10.1042/BCJ20210829
000476470 0247_ $$2ISSN$$a0264-6021
000476470 0247_ $$2ISSN$$a1470-8728
000476470 0247_ $$2datacite_doi$$a10.3204/PUBDB-2022-01747
000476470 0247_ $$2altmetric$$aaltmetric:120822488
000476470 0247_ $$2pmid$$apmid:35023554
000476470 0247_ $$2WOS$$aWOS:000753051700001
000476470 0247_ $$2openalex$$aopenalex:W4220750441
000476470 037__ $$aPUBDB-2022-01747
000476470 041__ $$aEnglish
000476470 082__ $$a540
000476470 1001_ $$0P:(DE-H253)PIP1080467$$aPazicky, Samuel$$b0
000476470 245__ $$aN-terminal phosphorylation regulates the activity of glycogen synthase kinase 3 from Plasmodium falciparum
000476470 260__ $$aLondon [u.a.]$$bPortland Pr.$$c2022
000476470 3367_ $$2DRIVER$$aarticle
000476470 3367_ $$2DataCite$$aOutput Types/Journal article
000476470 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1717066490_148986
000476470 3367_ $$2BibTeX$$aARTICLE
000476470 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000476470 3367_ $$00$$2EndNote$$aJournal Article
000476470 500__ $$aISSN 1470-8728 not unique: **2 hits**.
000476470 520__ $$aAs the decline of malaria cases stalled over the last five years, novel targets in Plasmodium falciparum are necessary for the development of new drugs. Glycogen Synthase Kinase (PfGSK3) has been identified as a potential target, since its selective inhibitors were shown to disrupt the parasitès life cycle. In the uncanonical N-terminal region of the parasite enzyme, we identified several autophosphorylation sites and probed their role in activity regulation of PfGSK3. By combining molecular modeling with experimental small-angle X-ray scattering data, we show that increased PfGSK3 activity is promoted by conformational changes in the PfGSK3 N-terminus, triggered by N-terminal phosphorylation. Our work provides novel insights into the structure and regulation of the malarial PfGSK3.
000476470 536__ $$0G:(DE-HGF)POF4-6G3$$a6G3 - PETRA III (DESY) (POF4-6G3)$$cPOF4-6G3$$fPOF IV$$x0
000476470 588__ $$aDataset connected to CrossRef, Journals: bib-pubdb1.desy.de
000476470 693__ $$0EXP:(DE-H253)P-P12-20150101$$1EXP:(DE-H253)PETRAIII-20150101$$6EXP:(DE-H253)P-P12-20150101$$aPETRA III$$fPETRA Beamline P12$$x0
000476470 7001_ $$aAlder, Arne$$b1
000476470 7001_ $$aMertens, Haydyn$$b2
000476470 7001_ $$aSvergun, Dmitri$$b3
000476470 7001_ $$aGilberger, Tim$$b4
000476470 7001_ $$0P:(DE-H253)PIP1023783$$aLoew, Christian$$b5$$eCorresponding author
000476470 773__ $$0PERI:(DE-600)2007050-0$$a10.1042/BCJ20210829$$gVol. 479, no. 3, p. 337 - 356$$n3$$p337 - 356$$tThe @biochemical journal / Reviews$$v479$$x0264-6021$$y2022
000476470 8564_ $$uhttps://portlandpress.com/biochemj/article/479/3/337/230649/N-terminal-phosphorylation-regulates-the-activity
000476470 8564_ $$uhttps://bib-pubdb1.desy.de/record/476470/files/N%20terminal%20phosphorylation%20regulates%20the%20activity%20of%20glycogen%20synthase%20kinase%203%20from%20Plasmodium%20falciparum.pdf$$yOpenAccess
000476470 8564_ $$uhttps://bib-pubdb1.desy.de/record/476470/files/N%20terminal%20phosphorylation%20regulates%20the%20activity%20of%20glycogen%20synthase%20kinase%203%20from%20Plasmodium%20falciparum.pdf?subformat=pdfa$$xpdfa$$yOpenAccess
000476470 909CO $$ooai:bib-pubdb1.desy.de:476470$$pdnbdelivery$$pdriver$$pVDB$$popen_access$$popenaire
000476470 9101_ $$0I:(DE-H253)_CSSB-20140311$$6P:(DE-H253)PIP1080467$$aCentre for Structural Systems Biology$$b0$$kCSSB
000476470 9101_ $$0I:(DE-H253)_CSSB-20140311$$6P:(DE-H253)PIP1023783$$aCentre for Structural Systems Biology$$b5$$kCSSB
000476470 9131_ $$0G:(DE-HGF)POF4-6G3$$1G:(DE-HGF)POF4-6G0$$2G:(DE-HGF)POF4-600$$3G:(DE-HGF)POF4$$4G:(DE-HGF)POF$$aDE-HGF$$bForschungsbereich Materie$$lGroßgeräte: Materie$$vPETRA III (DESY)$$x0
000476470 9141_ $$y2022
000476470 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000476470 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000476470 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
000476470 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bBIOCHEM J : 2013
000476470 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000476470 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000476470 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000476470 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000476470 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000476470 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000476470 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000476470 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000476470 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000476470 9201_ $$0I:(DE-H253)EMBL-User-20120814$$kEMBL-User$$lEMBL-User$$x0
000476470 9201_ $$0I:(DE-H253)EMBL-20120731$$kEMBL$$lEMBL$$x1
000476470 9201_ $$0I:(DE-H253)CSSB-EMBL-20141216$$kCSSB-EMBL$$lCSSB-EMBL$$x2
000476470 9201_ $$0I:(DE-H253)CSSB-EMBL-CL-20210806$$kCSSB-EMBL-CL$$lCSSB-EMBL-CL$$x3
000476470 980__ $$ajournal
000476470 980__ $$aVDB
000476470 980__ $$aI:(DE-H253)EMBL-User-20120814
000476470 980__ $$aI:(DE-H253)EMBL-20120731
000476470 980__ $$aI:(DE-H253)CSSB-EMBL-20141216
000476470 980__ $$aI:(DE-H253)CSSB-EMBL-CL-20210806
000476470 980__ $$aUNRESTRICTED
000476470 9801_ $$aFullTexts