Binding of Ca2+ and Zn2+ to Human Nuclear S100A2 and Mutant Proteins
Open Access
- 1 July 1998
- journal article
- Published by Elsevier
- Vol. 273 (30) , 18826-18834
- https://doi.org/10.1074/jbc.273.30.18826
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Ion-binding properties of recombinant S100β and two derivatives with either an inactivated Ca2+ site II or a normalized Ca2+ site IBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
- Nuclear calcium and the regulation of the nuclear pore complexBioEssays, 1997
- Nereis sarcoplasmic Ca2+‐binding protein has a highly unstructured apo state which is switched to the native state upon binding of the first Ca2+ ionFEBS Letters, 1996
- Characterization of the Human and Mouse cDNAsCoding for S100A13, a New Member of the S100 Protein FamilyBiochemical and Biophysical Research Communications, 1996
- Interaction of Cardiotonic Thiadiazinone Derivatives with Cardiac Troponin CPublished by Elsevier ,1996
- Solution Structure of Rat Apo-S100B(ββ) As Determined by NMR Spectroscopy,Biochemistry, 1996
- Purification and Characterization of the Recombinant Human Calcium-Binding S100 Proteins CAPL and CACYBiochemistry, 1994
- Metastasis-Associatedmts1Gene Expression Correlates with Increased p53 Detection in the B16 Murine MelanomaDNA and Cell Biology, 1994
- Calcyclin is a calcium and zinc binding proteinFEBS Letters, 1990
- Fluorescence studies on the Ca2+and Zn2+binding properties of the α-subunit of bovine brain S-100a proteinFEBS Letters, 1987