Identification of Calcium-Independent and Calcium-Enhanced Binding between S100B and the Dopamine D2 Receptor
Author:
Affiliation:
1. Department of Biochemistry, The University of Western Ontario, London, Ontario, Canada N6A 5C1
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi201054x
Reference67 articles.
1. Ions binding to S100 proteins. II. Conformational studies and calcium-induced conformational changes in S100 alpha alpha protein: the effect of acidic pH and calcium incubation on subunit exchange in S100a (alpha beta) protein.
2. The Effects of CapZ Peptide (TRTK-12) Binding to S100B–Ca2+ as Examined by NMR and X-ray Crystallography
3. Calcium-Binding Properties of Wild-Type and EF-Hand Mutants of S100B in the Presence and Absence of a Peptide Derived from the C-Terminal Negative Regulatory Domain of p53
4. Annexin VI binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments
5. Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein.
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