Phosphorylation of p23-1 cochaperone by protein kinase CK2 affects root development in Arabidopsis
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2045-2322
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Phosphorylation of p23-1 cochaperone by protein kinase CK2 affects root development in Arabidopsis ; volume:9 ; number:1 ; day:8 ; month:7 ; year:2019 ; pages:1-10 ; date:12.2019
Scientific reports ; 9, Heft 1 (8.7.2019), 1-10, 12.2019
- Classification
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Biowissenschaften, Biologie
- Creator
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D’Alessandro, Stefano
Golin, Serena
Zanin, Sofia
Cendron, Laura
Zottini, Michela
Ruzzene, Maria
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s41598-019-46327-0
- URN
-
urn:nbn:de:101:1-2019103105192960150660
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:30 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- D’Alessandro, Stefano
- Golin, Serena
- Zanin, Sofia
- Cendron, Laura
- Zottini, Michela
- Ruzzene, Maria
- SpringerLink (Online service)
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Phosphorylation of Arabidopsis SINA2 by CDKG1 affects its ubiquitin ligase activity
NEK10 kinase ablation affects mitochondrial morphology, function and protein phosphorylation status
Phosphorylation-dependent stabilization of MZF1 upregulates N-cadherin expression during protein kinase CK2-mediated epithelial-mesenchymal transition
Role of protein kinase CK2 in antitumor drug resistance
Selective modulation of the protein kinase CK2 : discovery, syntheses and characterizationof non-ATP site inhibitors of CK2
CK2-mediated CCDC106 phosphorylation is required for p53 degradation in cancer progression
RP1 is a phosphorylation target of CK2 and is involved in cell adhesion
CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site
Glucosamine affects intracellular signalling through inhibition of mitogen-activated protein kinase phosphorylation in human chondrocytes
Die Protein-Kinase CK2 reguliert ein anti-apoptotisches Programm in Pankreaskarzinomzellen
Benzimidazole inhibitors of protein kinase CK2 potently inhibit the activity of atypical protein kinase Rio1
CK2-mediated phosphorylation of Che-1/AATF is required for its pro-proliferative activity
Phosphorylation of Arabidopsis SINA2 by CDKG1 affects its ubiquitin ligase activity
NEK10 kinase ablation affects mitochondrial morphology, function and protein phosphorylation status
Phosphorylation-dependent stabilization of MZF1 upregulates N-cadherin expression during protein kinase CK2-mediated epithelial-mesenchymal transition
Role of protein kinase CK2 in antitumor drug resistance
Selective modulation of the protein kinase CK2 : discovery, syntheses and characterizationof non-ATP site inhibitors of CK2
CK2-mediated CCDC106 phosphorylation is required for p53 degradation in cancer progression
RP1 is a phosphorylation target of CK2 and is involved in cell adhesion
CK2-mediated phosphorylation of SUZ12 promotes PRC2 function by stabilizing enzyme active site
Glucosamine affects intracellular signalling through inhibition of mitogen-activated protein kinase phosphorylation in human chondrocytes
Die Protein-Kinase CK2 reguliert ein anti-apoptotisches Programm in Pankreaskarzinomzellen
Benzimidazole inhibitors of protein kinase CK2 potently inhibit the activity of atypical protein kinase Rio1