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Inositol pyrophosphates promote the interaction of SPX doma..:
Ried, Martina K
;
Wild, Rebekka
;
Zhu, Jinsheng
...
DOI:https://doi.org/10.1038/s41467-020-20681-4. , 2021
Link:
https://www.repo.uni-hannover.de/handle/123456789/1236
RT Journal T1
Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis
UL https://suche.suub.uni-bremen.de/peid=base-ftunivhannover:oai:www.repo.uni-hannover.de:123456789_12361&Exemplar=1&LAN=DE A1 Ried, Martina K A1 Wild, Rebekka A1 Zhu, Jinsheng A1 Pipercevic, Joka A1 Sturm, Kristina A1 Broger, Larissa A1 Harmel, Robert K A1 Abriata, Luciano A A1 Hothorn, Ludwig A A1 Fiedler, Dorothea A1 Hiller, Sebastian A1 Hothorn, Michael PB London : Nature Publishing Group YR 2021 K1 binding protein K1 brassinosteroid K1 brassinosteroid receptor kinase bri1 K1 inhibitor protein K1 inhibitor protein bki1 K1 inositol phosphate K1 inositol pyrophosphate K1 Pi starvation response transcription factor K1 plant protein K1 receptor K1 spx domain containing protein K1 transcription factor K1 unclassified drug K1 Arabidopsis protein K1 nuclear protein K1 PHR1 protein K1 Arabidopsis K1 protein binding K1 pyrophosphoric acid derivative K1 recombinant protein K1 SPX1 protein K1 concentration (composition) K1 DNA K1 eukaryote K1 homeostasis K1 inorganic phosphorus K1 mutation K1 phosphate K1 protein K1 starvation K1 Agrobacterium tumefaciens K1 Arabidopsis thaliana K1 Chaetomium thermophilum K1 comparative study K1 complex formation K1 controlled study K1 crystal structure K1 dimerization K1 dissociation constant K1 DNA binding K1 gene expression K1 gene interaction K1 gene mutation K1 gene rearrangement K1 in vitro study K1 isothermal titration calorimetry K1 metabolic regulation JF DOI:https://doi.org/10.1038/s41467-020-20681-4 LK http://dx.doi.org/https://www.repo.uni-hannover.de/handle/123456789/12361 DO https://www.repo.uni-hannover.de/handle/123456789/12361 SF ELIB - SuUB Bremen
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