Dimerization and phosphatase activity of calcyclin‐binding protein/Siah‐1 interacting protein: the influence of oxidative stress
Author:
Affiliation:
1. Nencki Institute of Experimental Biology, Polish Academy of SciencesWarsawPoland
2. Center for Structural Biology, Vanderbilt UniversityNashvilleTennesseeUSA
3. International Institute of Molecular and Cell BiologyWarsawPoland
Funder
European Commission
National Institutes of Health
Narodowe Centrum Nauki
American Cancer Society
Publisher
Wiley
Subject
Genetics,Molecular Biology,Biochemistry,Biotechnology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.14-264770
Reference39 articles.
1. p30, a novel protein target of mouse calcyclin (S100A6)
2. Molecular Cloning and Expression of a Mouse Brain cDNA Encoding a Novel Protein Target of Calcyclin
3. Siah-1, SIP, and Ebi Collaborate in a Novel Pathway for β-Catenin Degradation Linked to p53 Responses
4. Calcyclin (S100A6) Binding Protein (CacyBP) Is Highly Expressed in Brain Neurons
5. CacyBP/SIP interacts with tubulin in neuroblastoma NB2a cells and induces formation of globular tubulin assemblies
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1. Evaluation of the Expression and Localization of the Multifunctional Protein CacyBP/SIP and Elements of the MAPK Signaling Pathway in the Adrenal Glands of Rats with Primary and Secondary Hypertension;International Journal of Molecular Sciences;2023-12-20
2. The Effect of CacyBP/SIP on the Phosphorylation of ERK1/2 and p38 Kinases in Clear Cell Renal Cell Carcinoma;International Journal of Molecular Sciences;2023-06-20
3. Molecular and immunological characterization of the calcyclin binding protein in rodent malaria parasite;Experimental Parasitology;2023-03
4. Siah-1-interacting protein regulates mutated huntingtin protein aggregation in Huntington’s disease models;Cell & Bioscience;2022-03-19
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